UniProt ID stringlengths 6 10 | Protein Sequence stringlengths 2 35.2k | Functional Description stringlengths 5 30.7k |
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Q9BR50 | MAAGKFASLPRNMPVNHQFPLASSMDLLSSRSPLAEHRPDAYQDVSIHGTLPRKKKGPPPIRSCDDFSHMGTLPHSKSPRQNSPVTQDGIQESPWQDRHGETFTFRDPHLLDPTVEYVKFSKERHIMDRTPEKLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLRCLEEHYGTSPGQAREGSLTKGRPDVAKRLSLTMGGVQAREQNLPRGNLLRNKEKSGSQPACLDHMQDRRALSLKAHQSESYLPIGCKLPPQSSGVDTSPCPNSPVFRTGSEPALSPAVVRRVSSDARAGEALRGSDSQLCPKPPPKPCKVPFLKVPSSPSAWLNSEANYCELNPAFATGCGRGAKLPSCAQGSHTELLTAKQNEAPGPRNSGVNYLILDDDDRERPWEPAAAQMEKGQWDKGEFVTPLLETVSSFRPNEFESKFLPPENKPLETAMLKRAKELFTNNDPKVIAQHVLSMDCRVARILGVSEEMRRNMGVSSGLELITLPHGHQLRLDIIERHNTMAIGIAVDILGCTGTLEDRAATLSKIIQVAVELKDSMGDLYSFSALMKALEMPQITRLEKTWTALRHQYTQTAILYEKQLKPFSKLLHEGRESTCVPPNNVSVPLLMPLVTLMERQAVTFEGTDMWEKNDQSCEIMLNHLATARFMAEAADSYRMNAERILAGFQPDEEMNEICKTEFQMRLLWGSKGAQVNQTERYEKFNQILTALSRKLEPPPVKQAEL | Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (PubMed:24216110). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (PubMed:24216110). Promotes insulin-mediated membrane ruffling (By similarity). In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1 (PubMed:19086031). Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity (By similarity). May inhibit TGFB-SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (By similarity). Regulates EGF-induced DNA synthesis (PubMed:18722344). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling (By similarity). Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA (By similarity). Positively regulates integrin-induced tyrosine phosphorylation of BCAR1 (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (By similarity). However, in a contrasting study, lacks GEF activity towards RAP1 (PubMed:22081014). Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the complex is dependent on integrin mediated-tyrosine phosphorylation of PTPRA (PubMed:22801373). Within the complex, interacts (via SH2 domain) with PTPRA (when phosphorylated on 'Tyr-798') (PubMed:22801373). Interacts (via Ras-GEF domain) with BCAR1 (PubMed:18722344, PubMed:19086031, PubMed:22081014). Interacts (via Ras-GEF domain) with NEDD9 (By similarity). Interacts with PTK2/FAK1 (By similarity). Interacts with PTPN1. Interacts (via SH2 domain) with EGFR (when tyrosine-phosphorylated) (PubMed:18722344). Localization to focal adhesions depends on interaction with PTPRA. Ubiquitously expressed. Found in several cancer cell lines, but not in nonmalignant breast tissue. The SH2 domain mediates interaction with tyrosine-phosphorylated proteins (PubMed:18722344). However, not involved in the binding to phosphorylated BCAR1 (PubMed:18722344). Required for cell cycle progression in response to INS/insulin (PubMed:24216110). Required for regulation of EFR-induced DNA synthesis (PubMed:18722344). The Ras-GEF domain appears to adopt a closed conformation rendering it incapable of carrying out canonical exchange factor function, this closed conformation is probably required for interaction with BCAR1. Phosphorylated on tyrosine residues. Overexpression confers anti-estrogen resistance via RRAS-independent activation of the PI3K pathway, and activation of the cyclin D1 promoter in breast cancer cell lines (PubMed:9582273). Plays a role in insulin-mediated ERK activation and DNA synthesis in breast cancer cells (PubMed:24216110). The guanine nucleotide exchange factor (GEF) activity is controversial. One study showed GEF activity towards RALA, RAP1A and RRAS (By similarity). However, in another study, a construct containing only the Ras-GEF domain lacks GEF activity towards RAP1 (PubMed:22081014). |
Q4R8R1 | MAAGKFASLPRNMPVNHQFPLASSMDLLSSKSPLTEHRPDAYQDVSIHGTLPRKKKGPPPIRSCDDFSHMGTLPHSKSPQQNSPVTQDSIQESPWQDRHCETFTFRDPHLLDPTLEYVKFSKERHIMDRTPEKLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLRCLEERYGISPGQAREGSLTEGRPDVTKRLSLTMGGVQAREQNLPRGNLLRNKEKSGSQPACLDHMQDRRALSLKAHQSESYLPIGCKLPPQSSGVDTSPCPNSPVFRTGSEPALSPAVVRRVSSDARAGEALRGSDSQLCPKPPPKPCKVPFLKAPSSPSAWLNSEANYCELNPAFATGCGRGAKLPLCAQGSPTELLTAKQNGALGPRNSGINYLILDDDDRERPWEPAAAQTEKGQWDKGEFVAPLLETVSSFRPNDFKSKFLPPENKPLETAMLKRAKELFTNNDPKVIAQHILSMDCRVARILEVSEEMRRNMGVSSGLELITLPHGHQLRLDIIERHSTMAIGIAVYILGCTGTLEDRAATLSKVIQVAVELKDSMGDLYSFSALMKALEMPQITRLEKTWTALRHQYTQTAILYEKQLKPFSKILHEGRESTCVPPNNVSVPLLMPLVTLMERQAVTFEGTDMWEKNDQSCEIMLNHLATARLMAEATDSYRMNAERILAGFQPDEEMNEICKTEFQMRLLWGSKGAQVNQAERYEKFNQILTALSRKLEPPPVKQAEL | Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (By similarity). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (By similarity). Promotes insulin-mediated membrane ruffling (By similarity). In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1. Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity. May inhibit TGFB-SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (By similarity). Regulates EGF-induced DNA synthesis (By similarity). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling. Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA. Positively regulates integrin-induced tyrosine phosphorylation of BCAR1. Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (By similarity). However, in a contrasting study, lacks GEF activity towards RAP1 (By similarity). Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the complex is dependent on integrin mediated-tyrosine phosphorylation of PTPRA (By similarity). Within the complex, interacts (via SH2 domain) with PTPRA (when phosphorylated on 'Tyr-798') (By similarity). Interacts (via Ras-GEF domain) with BCAR1 (By similarity). Interacts (via Ras-GEF domain) with NEDD9 (By similarity). Interacts with PTK2/FAK1 (By similarity). Interacts with PTPN1. Interacts (via SH2 domain) with EGFR (when tyrosine-phosphorylated) (By similarity). Localization to focal adhesions depends on interaction with PTPRA. The SH2 domain mediates interaction with tyrosine-phosphorylated proteins (By similarity). However, not involved in the binding to phosphorylated BCAR1 (By similarity). Required for cell cycle progression in response to INS/insulin (By similarity). Required for regulation of EGF-induced DNA synthesis (By similarity). The Ras-GEF domain appears to adopt a closed conformation rendering it incapable of carrying out canonical exchange factor function, this closed conformation is probably required for interaction with BCAR1. Phosphorylated on tyrosine residues. The guanine nucleotide exchange factor (GEF) activity is controversial. One study showed GEF activity towards RALA, RAP1A and RRAS (By similarity). However, in another study, a construct containing only the Ras-GEF domain lacks GEF activity towards RAP1 (By similarity). |
Q3UP10 | MAAGKFASLPRNMPVNHQFPLASSMDLLSSKSPLAERRTDAYQDVSIHGTLPRKKKGPPSIRSCDNAGHSKSPRQSSPLTQDIIQENPLQDRKGENFIFRDPYLLDPTLEYVKFSKERHIMDRTPERLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLWCLEERYGTSPGRGREGSLAEGRPDVVKRLSLTTGSSIQAREHSLPRGNLLRNKEKSGSQPACLDHVQDRKALTLKAHQSESHLPIGCKLPPQSPSMDTSPCPSSPVFRTGSEPTLSPALVRRFSSDARTGEALRGSDSQLCPKPPPKPCKVPFLKTPPSPSPWLTSEANYCELNPAFAVGCDRGAKLPMQAHDSHEMLLTAKQNGPSGPRNSGINYMILDGDDQARHWDPLAVQTDEGQEDKTKFVPPLMETVSSFRPNDFESKLLPPENKPLETAMLKHAKELFTNHDARVIAQHMLSVDCKVARILEVSEDRKRSMGVSSGLELITLPHGRQLRLDIIERHNTMAIGIAVDILGCTGTLENRAGTLNKIIQVAVELKDAMGDLYAFSAIMKALEMPQITRLEKTWTALRHHYTQTAILYEKQLKPFSKILHEGRESTYVPASNVSVPLLMPLVTLMERQAVTFEGTDMWENNDESCEILLNHLATARFMAEASESYRMNAERILADFQPDEEMTEILRTEFQMRLLWGSKGAEVNQNERYDKFNQILTALSRKLEPPSGKQAEL | Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (PubMed:12517963). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (By similarity). Promotes insulin-mediated membrane ruffling (By similarity). In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1 (PubMed:10896938). Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity (PubMed:25499443). May inhibit TGFB-SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (PubMed:25499443). Regulates EGF-induced DNA synthesis (By similarity). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling (PubMed:19365570). Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA (PubMed:22801373). Positively regulates integrin-induced tyrosine phosphorylation of BCAR1 (PubMed:22801373). Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (PubMed:10896938). However, in a contrasting study, lacks GEF activity towards RAP1 (By similarity). Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the complex is dependent on integrin mediated-tyrosine phosphorylation of PTPRA (PubMed:22801373). Within the complex, interacts (via SH2 domain) with PTPRA (when phosphorylated on 'Tyr-825') (PubMed:22801373). Interacts (via Ras-GEF domain) with BCAR1 (PubMed:10438950, PubMed:10896938, PubMed:12517963). Interacts with (via Ras-GEF domain) NEDD9 (PubMed:12517963). Interacts with PTK2B/FAK1 (PubMed:10896938). Interacts with PTPN1. Interacts (via SH2 domain) with EGFR (when tyrosine-phosphorylated) (By similarity). Localization to focal adhesions depends on interaction with PTPRA. Abundantly expressed in the lung and brain, with lower expression in splenic lymphocytes and liver (at protein level) (PubMed:19365570). Expressed in splenic lymphocytes (at protein level) (PubMed:19365570). Expressed in the lymph node cortical region, periphery of the splenic white pulp and in alveolar lung fibroblasts (PubMed:19365570). Expressed in epithelial cells in the lens equatorial region and early stage nucleated cortical lens fiber cells (PubMed:19365570). Expressed in the thymus (PubMed:10438950). Expressed in B-cells (PubMed:12517963). Up-regulated by IL1A and LTA, in thymus cortical reticular cell lines. The SH2 domain mediates interaction with tyrosine-phosphorylated proteins (PubMed:10896938, PubMed:22801373). However, not involved in the binding to phosphorylated BCAR1 (PubMed:10896938). Required for cell cycle progression in response to INS/insulin (By similarity). Required for regulation of EGF-induced DNA synthesis (By similarity). The Ras-GEF domain appears to adopt a closed conformation rendering it incapable of carrying out canonical exchange factor function, this closed conformation is probably required for interaction with BCAR1. Phosphorylated on tyrosine residues. Knockout mice are generally normal and viable (PubMed:19365570). Retinal white circular lesions in anterior chamber derived from the lens cortex (PubMed:19365570). Retinal lens is partially opaque and irregular in structure, with rupture leading to cortical lens fragments floating in the aqueous humor (PubMed:19365570). Abnormally deep anterior chamber with anterior synechiae, ectropion uveae, mild to moderate retinal ganglion loss, and a small pigmented pre-retinal membrane overlying the optic nerve (PubMed:19365570). Reduced phosphorylation of AKT1 and BCAR1 in lens epithelial cells (PubMed:19365570). Retinal lens abnormalities develop progressively postnatally; at postnatal day 3 (P3) there is anterior lens vacuolization and liquefaction of lens cortical fibers (PubMed:19365570). At P24 there is evidence of extensive lens cortex vacuolation and early lens extrusion, progressing to extrusion of lens cortical material at P33 (PubMed:19365570). The guanine nucleotide exchange factor (GEF) activity is controversial. One study showed GEF activity towards RALA, RAP1A and RRAS (PubMed:10896938). However, in another study, a construct containing only the Ras-GEF domain lacks GEF activity towards RAP1 (By similarity). |
D3ZAZ5 | MAAGKFASLPRHMPVNHQFPLASSMDLLSSKSPLAEHRTEAYPDVSIHGTLPRKKKGPPPIRSCDSASHMGTLPHSKSPRQSSPLTQDLILEKPLPDWKGDSFAFRDPYLLDPTLEYVKFSKERHIMDRTPERLKKELEEELLLSSEDLRSHAWYHGRIPRQVSENLVQRDGDFLVRDSLSSPGNFVLTCQWKNLAQHFKINRTVLRLSEAYSRVQYQFEMESFDSIPGLVRCYVGNRRPISQQSGAIIFQPINRTVPLWCLEERYGTSPGRGREGSFAEGRPDVVKRLSLTTGGIQARDHSLPRGNLLRNKDKSGSQPACLDHVQDRKAATLKAHQSESHLPIGCKLPPQSPSVDTSPCPNSPVFRTGSEPTLSPALVRRFSSDARAGEALRGSDSQLCPKPPPKPCKVPFLKVPPSPSPWLNSEANYCELNPAFAVGCDRGAKLLSQALDSHEMLLTAKQNGASGPRNSGINYSILDGDDQGRHWDPLAVQTDEGQEDETKFVPPVMETVSSFRPNDFESKLLPPENKPLETAMLKHAKELFTNHDARVIAQHMLSVDCKVARILEVSEDMKRSMGVSSGLELITLPHGRQLRLDIIERHNTMAIGIAVDILGCTGTLENRAGTLNKIIQVAMELKDTMGDLYSFSAIMKALEMPQITRLEKTWTALRHHYTQTAILYEKQLKPFSKILHEGRESTYVPASSVSVPLLMPLVTLMERQAVTFEGTDMWEKNDESCEIMLSHLATARFMAEASESYRMNAERVLADFQPDEEMTEILKTEFQMRLLWGSKGAEVNQNERYDKFNQILTALSRKLEPPSGKQAEL | Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (By similarity). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (PubMed:24216110). Promotes insulin-mediated membrane ruffling (PubMed:24216110). In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1 (By similarity). Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity (By similarity). May inhibit TGFB/SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (By similarity). Regulates EGF-induced DNA synthesis (By similarity). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling (By similarity). Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA (By similarity). Positively regulates integrin-induced tyrosine phosphorylation of BCAR1 (By similarity). Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (By similarity). However, in a contrasting study, lacks GEF activity towards RAP1 (By similarity). Part of a complex comprised of PTPRA, BCAR1, BCAR3 and SRC; the formation of the complex is dependent on integrin mediated-tyrosine phosphorylation of PTPRA (By similarity). Within the complex, interacts (via SH2 domain) with PTPRA (when phosphorylated on 'Tyr-792') (By similarity). Interacts (via Ras-GEF domain) with BCAR1 (PubMed:24216110). Interacts (via Ras-GEF domain) with NEDD9 (By similarity). Interacts with PTK2/FAK1 (By similarity). Interacts with PTPN1. Interacts (via SH2 domain) with EGFR (when tyrosine-phosphorylated) (By similarity). Localization to focal adhesions depends on interaction with PTPRA. The SH2 domain mediates interaction with tyrosine-phosphorylated proteins (By similarity). However, not involved in the binding to phosphorylated BCAR1 (By similarity). Required for cell cycle progression in response to INS/insulin (By similarity). Required for regulation of EGF-induced DNA synthesis (By similarity). The Ras-GEF domain appears to adopt a closed conformation rendering it incapable of carrying out canonical exchange factor function, this closed conformation is probably required for interaction with BCAR1. Phosphorylated on tyrosine residues. The guanine nucleotide exchange factor (GEF) activity is controversial. One study showed GEF activity towards RALA, RAP1A and RRAS (By similarity). However, in another study, a construct containing only the Ras-GEF domain lacks GEF activity towards RAP1 (By similarity). |
Q6INP9 | MAAGKFASYHRNVQMNHPLVSSMDLLGSKSALGERRSDAFKNVCIHGTLPRKKKERVPIRSSDMFCHMGTLPHTKSHRLPNPLMQDIKEDYPFQERRTGIFNMREHYLDPAMEYVKFSKDRYIMDGGTPDKLKKELEEELKLNSEDLRSHAWYHGRIPRQVSESLVKRDGDFLIRDSLSSPGNLVLTCQWKNLSQHFKINKVVIRLNEAYCRIQYQLEHESFDSIPALVRFYVGNRKAVSQQSGAIIFQPINRTVPLRCIEEKYGTSPVRRLELGIMEVKSEPTKRLSLNFGQGISQEQSLVRGNLLRNKEKSGSQPACLDNMREKRRPLKAHQSESYLPLGSRQPCLSQGMDMKTSPKPHVFRTGSEPTLSPTEIRRFNHEVHPVEALRGSDSQLCPRPPPKPTKAPSIKQSQSPLVWQSSEANYCEFHPTPPEDCAWSDSHSSHNSYIEDQRTDEIETLSFSNSELSFPALDDSISQCSATDFCGNVEDDEFIRPVYETVSSFCPNDFQSVLLTAENKPLETSLLRRAKELFTNNDPRTIAKHILRMDCKVARILDVTPEVERMMGVSSGLELIILPYGHQLRLDLMERHSTMAIGIAVDILGCTGNLEERVATLHKIIQLAVEVKTLGDYFAFSAIMKALDMPQITRLEQTWTMLRHQYTQTAITYEKQLKPFSKYLHEGEALDAQEDVTVPLVMPLVTLLERQSVLFEGMDFWENNDRGCEILFNHLQTARQVAHNATVYKKNAQRILEGFKPDELMSEIFKTEFQMRLLWGSKGALLKQSERYHKFGQILTALSRKLEPPS | May act as an adapter protein. |
Q68CZ3 | MGNQMSVPQRVEDQENEPEAETYQDNASALNGVPVVVSTHTVQHLEEVDLGISVKTDNVATSSPETTEISAVADANGKNLGKEAKPEAPAAKSRFFLMLSRPVPGRTGDQAADSSLGSVKLDVSSNKAPANKDPSESWTLPVAAGPGQDTDKTPGHAPAQDKVLSAARDPTLLPPETGGAGGEAPSKPKDSSFFDKFFKLDKGQEKVPGDSQQEAKRAEHQDKVDEVPGLSGQSDDVPAGKDIVDGKEKEGQELGTADCSVPGDPEGLETAKDDSQAAAIAENNNSIMSFFKTLVSPNKAETKKDPEDTGAEKSPTTSADLKSDKANFTSQETQGAGKNSKGCNPSGHTQSVTTPEPAKEGTKEKSGPTSLPLGKLFWKKSVKEDSVPTGAEENVVCESPVEIIKSKEVESALQTVDLNEGDAAPEPTEAKLKREESKPRTSLMAFLRQMSVKGDGGITHSEEINGKDSSCQTSDSTEKTITPPEPEPTGAPQKGKEGSSKDKKSAAEMNKQKSNKQEAKEPAQCTEQATVDTNSLQNGDKLQKRPEKRQQSLGGFFKGLGPKRMLDAQVQTDPVSIGPVGKSK | Required for myelination. Homodimer (PubMed:14567997). Interacts with DYNLL1 and DYNLL2 (By similarity). Highly expressed in the brain and, more specifically, in oligodendrocytes (at protein level). Expressed in the prostate, and at lower levels in testis, intestine and colon. Overexpressed in most breast cancer cell lines and down-regulated in some colorectal tumors. |
Q9CVA1 | MGNQMSVPLRPGDQEHDPGADTCKVTSDNECVQNGNPVVLSTRVIQHYEEVDLGISSSKDNVATSSPKTMEAQAVGDASGKNLGKEAKTKAPAARSHFFLTLSRPVPGRPGDQGTDSSAASGRFDVSPSAAPENKDPSEHGALPVAAAPGQAPDKTPGCPEAKQQTLPATGPLAPSPPESQAEAPAQDKDFGFLNRFFKLDKGRESAPVNSQPKEAKGSEDPEQATEAPAVPGNPHGVSAGEDIVDSEQRGQDVDTLSYSVPGDPEVPGTTKEDPQVVDTTENSSSIMSFFKTLVSPNKTETKKDPEDTKATKADSVCDGHAAGQKMSETQAKSKKKRLDSPRLGLSFRKLFRHKDTENSPTTSANLKSDKANFTPQETRGKTKATKSCSPPPPPPEPTSEGRDSGKEKAGPTSLPLGKLFWKKSVKEDTLSTGAEENAVCESPVETVRLEEVESSLQTVDLSEETQPEPTDVKVKEESKPRKTPLMAFLRQMSVRSSEGIPRSEESNVKDSSCQTSNSVEKTPSPPEPEPAGTAQKNKETSSSKDKKSVDKKSATENSKQKNGKQEVREPAPCVQPPTVEANAMQTGDKTPKKSEKRRQSLGGFLKGLGPKRMSDAQVQTDPVSIGPVGKSK | Required for myelination. Homodimer. Interacts with DYNLL1 and DYNLL2. Highly expressed in the brain and, more specifically, in oligodendrocytes. Expressed in the Schwann cells (at protein level). Mice display hypomyelination, schizophrenia-like behavioral abnormalities and a tendency toward reduced anxiety-like behaviors and up-regulation of inflammatory genes in the brain. |
Q8K4U9 | MGNQMSVPLRPGDQEHDPEADTYKVTSDNECVQNGIPVVVSTRVIQHYEEVDLGINSLKDNVPASSPETMEAHAVADASGKNLGKGSKPKAPAARSHFFLTLSRPVPGRPGDQGTDSSAASGRLDVSPGTAPENKDPSEHGALPVAAAPGPAPDKTPGCTEAKQQTLPATSPLAPSPPESQAEAPSRPKDFSFLNRLFKLDKGRESAPADSPPEEGKGSKSQERAIEAPAVPGNPHGVSAGKDIVDSEERKQEVDTLSYSVPADPEVLGTTKEDPQVVDATENSNSIMSFFKTLVSPNKTETKKDPEDTDAENSPTTPANLKSDKADLTPQETQGTAKSSKGSSQPGQAPSAGTSDTAREGGKEKAGPTSLPLGKLFWKKSVKEDSLSTGAEENAVCEPPVETVRLEEVESTLQTVDLTEKETQTEPTDVKVKEESKPRRTPLMAFLRQMSVRGSEGITRSEESNGKDSSCQTSNSTEKTPSPPEPEPAGTAQKNKETSSKDKKSVDKKSAAESNKQKNGKPEAREPAPCVQQPTVEVNALQTGDKTPKRSEKRRQSLGGFLKGLGPKRMLDAQVQTDPVSIGPVGKSK | Required for myelination. Homodimer (By similarity). Interacts with DYNLL1 and DYNLL2 (PubMed:16133941). Expressed in cerebral cortex and cerebellum, but not in other organs. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. |
Q8SY41 | MSADSPRRHPSGVVGSGIGLGSGSGTGLGSGSTGGSKSGAAVPAIVPPQTVSDRSILDSAIGFINDVTLANQPVQDPKDTITWARFETCADVSDPRFGDDWELEGNAAPPLLLILGYGLGVQVWAIPANGEAVEVLSWRHGVVTALRVLPTPATAAALDENGRADEPVDSFAEKRPLVAFVDGGSAAASGLLAGSSGLGLGGGGGGVTTVGGSVGGVSGIGVSASAQFSAVNFMSLKTGVQVKTIKFKNAVLDIQANRSAVVITFHERIAVFDARTLEDRLTITTCYPSPGINPNPIALGPRWLAYAEHKLLHSKRSGGGCDGEGVPSYTATVLNAAKSLSKGLREFGEQVAAGLTGTTAGSGASSKSSSFDSASGGPDAKQSGVVTIIDVKHPVKDYSPTSGTPLSSTAGSQGGGDPIVAHFVAHSEALVAMEFDSSGMLLLTADRRGHDFHVFRVQPHPVGPSLAAVHHLYVLHRGDTSAKVQHIAFSLDSRWAAVSTLRGTTHVFPITPYGGAMGVRTHTSLHVVNKLSRFHRSAGLGADGRSSSPISHSESTTFVQSLQPYHNPTLPPYPRPSVVQPLAQLRQPFTLGSPPGSAGLGGGVGGGGVMGSGVSAGGHGVGVGVGSNSQRQRQRLSSLSDDSGKPLSVCSIFAKSRSWLLEPPMATREQPHRVQRKAVDSLFVMAGHGALIQYDLDTKLASHVAKEKICDDTPIELEVEARAQWNLGRRKDGSQEIAPPLGLDNWLIKDRHASLLLDSANQFDDPDERTESWLAQVEIITHAGPHRRLWMGPQFVFKNYNTPSGSNLNHVDAEAVEIGVSKTTTTTLPSTAASSALGLGTIIGKDRSSPLNMPLSAATSVGGAGIGSSAVTGRSGAGVPVLIESGSYSSIEQSPKLMDRFRHGHLDSDYGHGDTRLKEDLADAMRESPSTAAARRETTGNYFTTDQLDGLALNNNNNINNNIIPTKDNASPNPNTNTNPNAIPSSNKVQKAEVTDAVDYPIRHSYGDHGELSTVVNIEVFDDQLSMSSISTNSRLSLEGPPSQSSPPLSLTNGLMDTNLMHFSESVTGTGVAQAQVHGRGANRFEVDDDDEEEEEEEEELDEEAEPDDDEREDRPLGRRNL | Regulates macropinocytosis in pericardial cells. Expressed in all postembryonic pericardial cells, but not in cardioblasts. Also expressed in Garland cells in third instar larvae (at protein level). Not expressed during embryonic development and first instar larvae. Expression detected from second instar larval stage into adulthood (at protein level). Has been proposed to contain 7 WD repeats. This prediction could not be reproduced. RNAi-mediated knockdown of the protein in the hematopoietic system and pericardial cells causes a decrease in macropinocytic uptake by pericardial cells. Belongs to the BCAS3 family. |
Q9NXP4 | MNEAMATDSPRRPSRCTGGVVVRPQAVTEQSYMESVVTFLQDVVPQAYSGTPLTEEKEKIVWVRFENADLNDTSRNLEFHEIHSTGNEPPLLIMIGYSDGMQVWSIPISGEAQELFSVRHGPIRAARILPAPQFGAQKCDNFAEKRPLLGVCKSIGSSGTSPPYCCVDLYSLRTGEMVKSIQFKTPIYDLHCNKRILVVVLQEKIAAFDSCTFTKKFFVTSCYPCPGPNMNPIALGSRWLAYAENKLIRCHQSRGGACGDNIQSYTATVISAAKTLKSGLTMVGKVVTQLTGTLPSGVTEDDVAIHSNSRRSPLVPGIITVIDTETVGEGQVLVSEDSDSDGIVAHFPAHEKPVCCMAFNTSGMLLVTTDTLGHDFHVFQILTHPWSSSQCAVHHLYTLHRGETEAKVQDICFSHDCRWVVVSTLRGTSHVFPINPYGGQPCVRTHMSPRVVNRMSRFQKSAGLEEIEQELTSKQGGRCSPVPGLSSSPSGSPLHGKLNSQDSYNNFTNNNPGNPRLSPLPSLMVVMPLAQIKQPMTLGTITKRTGPYLFGAGCFSIKAPCKVKPPPQISPSKSMGGEFCVAAIFGTSRSWFANNAGLKREKDQSKQVVVESLYIISCYGTLVEHMMEPRPLSTAPKISDDTPLEMMTSPRASWTLVRTPQWNELQPPFNANHPLLLAADAVQYYQFLLAGLVPPGSPGPITRHGSYDSLASDHSGQEDEEWLSQVEIVTHTGPHRRLWMGPQFQFKTIHPSGQTTVISSSSSVLQSHGPSDTPQPLLDFDTDDLDLNSLRIQPVRSDPVSMPGSSRPVSDRRGVSTVIDAASGTFDRSVTLLEVCGSWPEGFGLRHMSSMEHTEEGLRERLADAMAESPSRDVVGSGTELQREGSIETLSNSSGSTSGSIPRNFDGYRSPLPTNESQPLSLFPTGFP | Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation (By similarity). Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin. Plays a regulatory role in autophagic activity. In complex with PHAF1, associates with the preautophagosomal structure during both non-selective and selective autophagy (PubMed:33499712). Probably binds phosphatidylinositol 3-phosphate (PtdIns3P) which would mediate the recruitment preautophagosomal structures (PubMed:33499712). Interacts with histone H3, ESR1, KAT2B and PELP1; the interactions occur in a estrogen-dependent manner. Interacts with beta-tubulin and VIM. Interacts (via C-terminal) with PHAF1; the interaction is requrired for the association with the phagophore (PubMed:33499712). Localizes in the cytoplasm in stationary cells. Translocates from the cytoplasm to the leading edge in motile cells. Colocalizes with microtubules and intermediate filaments in both stationary and motile cells (By similarity). Associates with chromatin. Recruited to estrogen receptor-induced promoters in a PELP1-dependent manner. The BCAS3:PHAF1 complex is recruited to the preautophagosomal structures adjacent to the damaged mitochondria upon mitophagy in a PRKN-PINK1 dependent manner (PubMed:33499712). Expressed in stomach, liver, lung, kidney, prostate, testis, thyroid gland, adrenal gland, brain, heart, skeletal muscle, colon, spleen, small intestine, placenta, blood leukocyte and mammary epithelial cells. Expressed in undifferentiated ES cells. Expressed in blood islands and nascent blood vessels derived from differentiated ES cells into embryoid bodies (BD). Expressed in endothelial cells. Not detected in brain. Expressed in brain tumors (at protein level). Expressed in brain. Highly expressed in breast cancers and in glioma cell lines. Fetal. By estrogen. Has been proposed to contain 7 WD repeats. This prediction could not be reproduced. A chromosomal aberration involving BCAS3 has been found in some breast carcinoma cell lines. Translocation t(17;20)(q23;q13) with BCAS4. The disease is caused by variants affecting the gene represented in this entry. Belongs to the BCAS3 family. Truncated N-terminus. Truncated N-terminus. |
Q9EPX3 | MNETMATDSPRRPSRCTGGVVVRPQAVTEQSYMESVVTFLQDVVPQAYSGSPLTEEKEKIVWVRFENADLNDTSRNLEFHELHSTGNEPPLLVMIGYSDGMQVWGIPISGEAQELFSVRHGPVRAARILPAPQLGAQKCDNFAEKRPLLGVCKSIGSSGTTPPYCCVDLYSLRTGEMVKSIQFKTPIYDLHCNKRILVVVLQEKIAAFDSCTFTKKFFVTSCYPCPGPNMNPIALGSRWLAYAENKLIRCHQSRGGACGDNIQSYTATVLSAAKTLKSGLTMVGKVVTQLTGTLPSGVTEDDVALHCNSRRSPLVPGIITVIDTETVGEGQVLVSEDSDSDGIVAHFPAHEKPVCCMAFNTSGMLLVTTDTLGHDFHVFQILTHPWSSSQCAVHHLYTLHRGETEAKVQDICFSHDCRWVVVSTLRGTSHVFPINPYGGQPCVRTHMSPRVVNRMSRFQKSAGLEEIEQELTSKQGGRCSPVPGLSSSPSGSPLHGKLTSQDSYNNFTNNNPGNPRLSPLPSLMVVTPLAQIKQPMTLGTITKRTGPYLFGAGCFSIKAPCKVKSPPQISPSKSMGGEFCVAAVFGTSRSWFANNAGLKREKDQSKQVVVESLYIISCYGTLVEHMIEPRPISTAPKISDDTPLEIMTSPRASWTLVRTPQWNELQPPFNANHPLLLAAEAVQYYQLLLAGSLPPGSPGPITRHGSYDSLASDHSGQEDEEWLSQVEIVTHTGPHRRLWMGPQFHFKTIQTSGQTTVISTSSSVLQSHGPSDTPQPLLDFDTDDLDLNSLRIQPVRSDPVSMPGSSRAVSDRRGVSTVTDAASGTFDRSVTLLEVCGSWPEGFGLRHMSSMEHSEEGLRERLADAMAESPSRDVVGSGTELQREGSIETLSNSSGSTSGSIPRNFDGYRSPLPTNESQPLSLFPTGFP | Functions synergistically with PELP1 as a transcriptional coactivator of estrogen receptor-responsive genes. Stimulates histone acetyltransferase activity. Binds to chromatin (By similarity). Plays a role in angiogenesis. Participates in the regulation of cell polarity and directional endothelial cell migration by mediating both the activation and recruitment of CDC42 and the reorganization of the actin cytoskeleton at the cell leading edge. Promotes filipodia formation. Plays a regulatory role in autophagic activity. In complex with PHAF1, associates with the preautophagosomal structure during both non-selective and selective autophagy. Probably binds phosphatidylinositol 3-phosphate (PtdIns3P) which would mediate the recruitment preautophagosomal structures (By similarity). Interacts with histone H3, ESR1, KAT2B and PELP1; the interactions occur in a estrogen-dependent manner. Interacts with beta-tubulin and VIM. Interacts (via C-terminal) with PHAF1; the interaction is requrired for the association with the phagophore (By similarity). Associates with chromatin. Recruited to estrogen receptor-induced promoters in a PELP1-dependent manner (By similarity). Localizes in the cytoplasm in stationary cells. Translocates from the cytoplasm to the leading edge in motile cells. Colocalizes with microtubules and intermediate filaments in both stationary and motile cells. The BCAS3:PHAF1 complex is recruited to the preautophagosomal structures adjacent to the damaged mitochondria upon mitophagy in a PRKN-PINK1 dependent manner (By similarity). Expressed in blood islands and yolk sac blood islands (at protein level). Highly expressed in mammary tumors. Expressed in eostrogen-induced epithelial cells of mammary glands. Expressed in brain, heart, kidney, lung, liver and spleen. Expressed in embryonic stem cells, embryoid bodies, endothelial cells and fibroblasts. Expressed in erythroid cells in the vessels at 9.5 and 10.5 dpc (at protein level). Expressed in embryo at 7.5 dpc and in the yolk sac at 10.5 dpc. Expressed in the heart and yolk sac mesoderm at 8.5 dpc. Expressed in the head mesenchyme, somitic mesoderm, otic vesicle, vessels and few blood cells at 9.5 to 11.5 dpc. Up-regulated by PELP1 in response to estrogen. Has been proposed to contain 7 WD repeats. This prediction could not be reproduced. 'Rudhira' stands for 'blood' in Sanskrit as this protein is strongly expressed in blood vessels. Due to an intron retention. Belongs to the BCAS3 family. Truncated C-terminus. |
Q9Y511 | MQRTGGGAPRPGRNHGLPGSLRQPDPVALLMLLVDADQPEPMRSGARELALFLTPEPGAEAKEVEETIEGMLLRLEEFCSLADLIRSDTSQILEENIPVLKAKLTEMRGIYAKVDRLEAFVKMVGHHVAFLEADVLQAERDHGAFPQALRRWLGSAGLPSFRNVECSGTIPARCNLRLPGSSDSPASASQVAGITEVTCTGARDVRAAHTV | Brain, thymus, spleen, kidney and placenta. Overexpressed in most breast cancer cell lines. A chromosomal aberration involving BCAS4 has been found in some breast carcinoma cell lines. Translocation t(17;20)(q23;q13) with BCAS3. Belongs to the cappuccino family. |
K0K750 | MGRPATPQQTAFHIPFPRAISPDVSAVHPGSMAWLRRHGMLRSDASARRVDGWRLTELAGRFFPDARGEDLRLGADVMGFFFLFDDQFDHPGGLRAEAVAVSKRLLHLTSLPAGPAPEGAGPVVAAWADLWNRSCQGMSSAWRVRAAREWRRYFVGNLEESVAREGMSGESVEDYLRLRAMTIGTTPVYDLCERTQHFEIPDEVLHSHHVQAMRDLATEIVVLCNDVASTIKESARGETLNAVLLLERHHEAERGPAVARVQRMVEARLAAFRRLRDRTSRTCAALDLTAEQCDRVDRYVRTALMSVVRGNYDWQQRSARFSADDARPGSLPGYLDDLVGHSGVVGPPPVDGS | Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) to yield the bicyclic sesquiterpene (2S,10R)-(-)-(E)-beta-caryophyllene via a probable 1,10-cyclization, which could involve the abstraction of the pyrophosphate from FPP to yield a (E,E)-germacradienyl cation. (2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene + diphosphate Binds 3 Mg(2+) ions per subunit. Secondary metabolite biosynthesis; terpenoid biosynthesis. The Asp-Asp-Xaa-Xaa-Asp (DDXXD) motif is important for the catalytic activity, presumably through binding to Mg(2+). Belongs to the terpene synthase family. |
O80597 | MALRRCLPQYSTTSSYLSKIWGFRMHGTKAAASVVEEHVSGAEREDEEYADVDWDNLGFSLVRTDFMFATKSCRDGNFEQGYLSRYGNIELNPAAGILNYGQGLIEGMKAYRGEDGRVLLFRPELNAMRMKIGAERMCMHSPSVHQFIEGVKQTVLANRRWVPPPGKGSLYLRPLLFGSGASLGVAAASEYTFLVFGSPVQNYFKEGTAALNLYVEEVIPRAYLGGTGGVKAISNYGPVLEVMRRAKSRGFSDVLYLDADTGKNIEEVSAANIFLVKGNTIVTPATSGTILGGITRKSIIEIALDLGYKVEERSVPVEELKEAEEVFCTGTAAGVASVGSITFKNTRTEYKVGDGIVTQQLRSILVGIQTGSIQDTKDWVLQIA | Converts 2-oxo acids to branched-chain amino acids. Acts on leucine, isoleucine and valine (By similarity). 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate 2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate Amino-acid degradation; L-leucine degradation; 4-methyl-2-oxopentanoate from L-leucine (aminotransferase route): step 1/1. Amino-acid degradation; L-valine degradation. A number of isoforms are produced. According to EST sequences. Branched-chain amino acids are synthesized in chloroplasts, whereas the degradation takes place in mitochondria. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. |
Q96MY9 | MKDCSNGCSAECTGEGGSKEVVGTFKAKDLIVTPATILKEKPDPNNLVFGTVFTDHMLTVEWSSEFGWEKPHIKPLQNLSLHPGSSALHYAVELFEGLKAFRGVDNKIRLFQPNLNMDRMYRSAVRATLPVFDKEELLECIQQLVKLDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPTKALLFVLLSPVGPYFSSGTFNPVSLWANPKYVRAWKGGTGDCKMGGNYGSSLFAQCEAVDNGCQQVLWLYGEDHQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRRCILDLAHQWGEFKVSERYLTMDDLTTALEGNRVREMFGSGTACVVCPVSDILYKGETIHIPTMENGPKLASRILSKLTDIQYGREESDWTIVLS | Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate 2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate Homodimer. During embryogenesis, expressed in the brain and kidney. Overexpressed in MYC-induced tumors such as Burkitt's lymphoma. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. |
K7QKH1 | MIHRGLWLHNLVQSYRVGSSSSSSTLFKLVYRYNSSTSLAKSSLKQSCELSCKSNTEPSNMDWDKLGFKLMPTDYVYSMKCSNEGNFEQGRLELHGNIELSPAAAVLNYGQGIFEGTKAYRKEDGSLLLFRPDQNGVRMRIGAERMCMPSPSVDQFVDAVKQTAIANRRWVPPSGKGSLYIRPLLMGTGAVLGVAPAPQYTFLAYASPVGNYFKEGLAPLRLYVEDEFDRASPGGTGFVKTIGNYSRCLAALSRAKNKGFSDVLFLDSVHKKYVEELSSCNIFIVQGNQISTPAANGTILSGVTRSSIIEIARDHGFKVEERKIAVDELMEAEEVFCTGTAVGVASVGSITYHNKRVEFKTGSQSVSQKFYSTLIGIQTGVVEDKKGWIVEID | Converts 2-oxo acids to branched-chain amino acids (BCAA). Shows no kinetic preferences corresponding to anabolic or catabolic functions, but likely involved in BCAA catabolism. 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate 2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4. Expressed specifically in lupulin glands. Branched-chain amino acids are synthesized in chloroplasts, whereas the degradation takes place in mitochondria. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. |
Q7TMT2 | MKDCSNGCSAPFAGERGSEEVAETFRAKDLIITPATVLKEKPDPDSLVFGATFTDHMLTVEWSSASGWEKPHIKPFGNLPIHPAASVLHYAVELFEGLKAFRGVDNKIRLFRPDLNMDRMCRSAVRTTLPMFDKEELLKCILQLLQIDQEWVPYSTSASLYIRPTFIGTEPSLGVKKPSKALLFVILSPVGPYFSSGSFTPVSLWANPKYIRAWKGGTGDCKMGGNYGASLLAQCEAVENGCQQVLWLYGKDNQITEVGTMNLFLYWINEDGEEELATPPLDGIILPGVTRQSILELAQQWGEFKVCERHLTMDDLATALEGNRVKEMFGSGTACVVCPVSDILYKGQMLHIPTMENGPKLASRILGKLTDIQYGRVESDWTIELP | Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. 2-oxoglutarate + L-leucine = 4-methyl-2-oxopentanoate + L-glutamate 2-oxoglutarate + L-isoleucine = (S)-3-methyl-2-oxopentanoate + L-glutamate 2-oxoglutarate + L-valine = 3-methyl-2-oxobutanoate + L-glutamate Homodimer. Expressed in brain and kidney. Overexpressed in MYC-induced brain tumors, lymphomas, as well as in a teratocarcinoma cell line. Highly expressed at day 9 of embryogenesis. Expression decreases to moderate levels through day 13. In the developing embryo, expressed in the brain, somites and mesenophric tubules. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. |
Q67FY3 | MHSENKLSNHGKQVTSGAQSQLPNVNQAQQQAPAGIQGSKGSVSGNHGVKANQISPGNPGLKSLNQTGGGGGMMKTKAKRERSVSIDTGDQRESLTPVLEPDAKVEGVMRSKRRCVLERKQPYSGDEWCSGAETEEEDEKPLSATHREHVMCPSQGHSGSSTTGHVSDPGGPGLGSGHGPGIRTDLHSRPPQQVVYVFTTSLANSAAEAVMHGHTDSILLYHQQNVPRTKLDQSTGVGKVSNLAEHISSSHSPPIGTPKSQSGTPRPASVGGVGHLPGTSTPSSTGHPDSEPAQTHRGGGTSSNNGRSAVHTLGLGNSGPQSVGVSGTEGVDRPGAIPHHGAGVSPSTSPSVLSALRQSELGQRVGPGNTDGLSKEQLEHRERSLQTLRDIERLLLRSGTGVAQEDPRGPNGNPNGTNVNNNNSNDGGRGLEDGEIGGGIPGNCHINNAGMPGMPPVGGMKKYEEPLQSIISQTQNLGGPGLDDSLMGPHHGMPPHSHHLSSPSGLDMGPLLGPEGVTPEQLAWRKLQEEYYQEKRRQHDMNPHQHPQHFRIMPEMGMPGGPPMLMRGPPPPYHSKPGDQQWGPGPMVGGGMGGNARMMDMNQEGPRGPRFLGQMRGPSGGGGYPESPGGVLGVEGLGPQRPPRPGMGWLEEIPPNMGGGGPFHGCCPPGGPGGPPQHFQGDLDRPMTREEIYRRIHRLDLQQMSRQQQQAGLGGPRMMDNPGGPGFPNPGMAGGPPSRGDPMDFPVSRTIMGSPIGGVGGDGGPTMRDIVDSPLGGNLNMNMGMNINQQQQLLAQKLRGGPGVLGEMLNAEDISRIRASQNGRGGANKAMIPGPEGPLQFPNQSSFPGGQVDGPYLQQPGPDMYGPDQPGPPHLSSTSRLSHIPMNTGSRVTDLGARHPPDLPISVNPMGSPAIPPSHQLKSPSLSQEPSPLMPSPSAAGLKSPSQLPQSGPTHPPLPAASGAGTPSSTSIKSPQVMGPSLGLRSPSGSPGHLKSPSMPVASPGWTASPKAAMPSPGGPPSVKVTGNGGSSSTDTGMSLPPRSSNSTPISQPSNSINPSMPFTSSPDAPPSQNPLSLIMSQMSKYAMPSSTPLYHDAIKTIATSDDEMLPDRPLQPGTNMSVGGMGNHQSAQMLLSSQGAMGPHSGPQSPMGMVLQGGPPLSHDHPGPMLPSPNPMGIPGMPSEIMGGGGGPPDGIGPCNVSPMHTQNQMGGFPRIQGPLHSPIGGMGQQFPPRPDDVLPPQQMHLLSKGMSHQRPPHQPDSFPPMPMGDGPDLSEVIRPTHRGIPEFDLSRIIPADKPSSTLQYFPKSETMSQPQQNPHQGQPPPQVSSAQLLKQLSSSGPPHSNIPSSNPHIANLQNMMAEQQLPLHPSHCGMRPGMGMPQIGSRGMGSGGGMGPMCHPGHMMGRTGMSPQQQLQQQHHHQQQQAMMANNLLQHPSHPPRGMLSPQQHPHNLIAQQNLMMMQAKQRGMALPGEHFGQQGALMSPQGPMMGPPHSQTGMMGPQSLRQRSMSLDSPLGYGPGSMANMPF | Transcriptional regulator that may act as an activator (By similarity). Plays a role for mesoderm patterning in early embryogenesis. Highly expressed during gastrulation. Severe defects of trunk and tail development. Belongs to the BCL9 family. |
Q6ZWK2 | MRILANKTRLPHPRRREAPGSPPLSPRGHCPPAPAKPMHPENKLTNHGKTGNGGAQSQHQNVNQGPTCNVGSKGVGAGNHGAKANQISPSNSSLKNPQAGVPPFSSLKGKVKRDRSVSVDSGEQREAGTPSLDSEAKEVAPRSKRRCVLERKQPYSGDEWCSGPDSEEDDKPIGATHNCNVADPAMAAPQLGPGQTTQLPLSESSVPGAPHGPPPGLRPDAPGGGGGGGGVPGKPPSQFVYVFTTHLANTAAEAVLQGRADSILAYHQQNVPRAKLDQAPKVPPTPEPLPLSTPSAGTPQSQPPPLPPPPPPAPGSAPPALPPEGPPEDSSQDLAPNSVGAASTGGGTGGTHPNTPTATTANNPLPPGGDPSSAPGPALLGEAAAPGNGQRSLVGSEGLSKEQLEHRERSLQTLRDIERLLLRSGETEPFLKGPPGGAGEGGPPAQAPPPPQQPPTAPPSGLKKYEEPLQSMISQTQSLGGPPLEHEVPGHPPGGDMGQQMNMMIQRLGQDSLTPEQVAWRKLQEEYYEEKRRKEEQIGLHGSRPLQDMMGMGGMMVRGPPPPYHSKPGDQWPPGMGAQLRGPMDVQDPMQLRGGPPFPGPRFPGNQIQRVPGFGGMQSMPMEVPMNAMQRPVRPGMGWTEDLPPMGGPSNFAQNTMPYPGGQGEAERFMTPRVREELLRHQLLEKRSMGMQRPLGMAGSGMGQSMEMERMMQAHRQMDPAMFPGQMAGGEGLAGTPMGMEFGGGRGLLSPPMGQSGLREVDPPMGPGNLNMNMNVNMNMNMNLNVQMTPQQQMLMSQKMRGPGDLMGPQGLSPEEMARVRAQNSSGVMGGPQKMLMPSQFPNQGQQGFSGGQGPYQAMSQDMGNTQDMFSPDQSSMPMSNVGTTRLSHMPLPPASNPPGTVHSAPNRGLGRRPSDLTISINQMGSPGMGHLKSPTLSQVHSPLVTSPSANLKSPQTPSQMVPLPSANPPGPLKSPQVLGSSLSVRSPTGSPSRLKSPSMAVPSPGWVASPKTAMPSPGVSQNKQPPLNMNSSTTLSNMEQGTLPPSGPRSSSSAPPANPPSGLMNPSLPFTSSPDPTPSQNPLSLMMTQMSKYAMPSSTPLYHNAIKTIATSDDELLPDRPLLPPPPPPQGSGPGISNSQPSQMHLNSAAAQSPMGMNLPGQQPLSHEPPPAMLPSPTPLGSNIPLHPNAQGTGGPPQNSMMMAPGGPDSLNAPCGPVPSSSQMMPFPPRLQQPHGAMAPTGGGGGGPGLQQHYPSGMALPPEDLPNQPPGPMPPQQHLMGKAMAGRMGDAYPPGVLPGVASVLNDPELSEVIRPTPTGIPEFDLSRIIPSEKPSSTLQYFPKSENQPPKAQPPNLHLMNLQNMMAEQTPSRPPNLPGQQGVQRGLNMSMCHPGQMSLLGRTGVPPQQGMVPHGLHQGVMSPPQGLMTQQNFMLMKQRGVGGEVYSQPPHMLSPQGSLMGPPPQQNLMVSHPLRQRSVSLDSQMGYLPAPGGMANLPF | Transcriptional regulator that acts as an activator. Promotes beta-catenin transcriptional activity. Plays a role in tumorigenesis. Enhances the neoplastic transforming activity of CTNNB1 (By similarity). Found in a complex with CDC73; CTNNB1 and PYGO1. Interacts with CTNNB1. Expressed in breast, ductal and invasive ductal carcinomas of the breast, sporadic colorectal adenomas and carcinomas (at protein level). Expressed in fetal brain. Expressed in lung, amygdala, eye, prostate, pancreatic and prostate cancers, head and neck tumors and embryonal tumor. Tne C-terminal domain is important for its transactivation activity. Belongs to the BCL9 family. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus. |
Q6I7B5 | MRILANKTRLPHPRRREAPGSPPLSPRGHCPPAPAKPMHPENKLTNHGKTGNGGAQSQHQNVNQGPTCNLGSKGVGAGSHGAKANQISPSNSSLKNPQAGVSPFSSLKGKVKRERSVSVDSGEQREAGTPSLDSEAKEVAPRSKRRCVLERKQPYSGDEWCSGPDSEEDDKPIAAAHNCNVADPAMVTPQLGPGQTAQLPLSESSAPGPQHGPQPGLRPDVPGGGGGGVPGKPPSQFVYVFTTHLANTAAEAVLQGRAESILAYHQQNVPRAKLDQAPKVPPTPEPLPLNTPSAGTPQSQPPPLPPPPPAPGSAPPALPPEGPPEDTSQDLAPNSVGAASTGGGTGGTHPNTPTAATANNPLPPGGDPGSAPGSALLGEATPTGNGQRNLVGSEGLSKEQLEHRERSLQTLRDIERLLLRSGETEPFLKGPPGGAGEGGPPAQAPSAAQPPPSAPPGGLKKYEEPLQSMISQTQSLGGPPLEHEVPGHPQGGDMGQQMNMMMQRLGQDSLTPEQVAWRKLQEEYYEEKRRKEEQIGLHGGRPLQDMVGMGGMMGRGPPPPYHSKPGDQWPPGMGAQLRGPMDVQDPMQLRPGPPFPGPRFPGNQMQRVPGFGGMQSMPMEVPMNAMQRPVRPGMAWNEDLPPIGGPSNFAQNAVPYPGGQGEAERFMTPRVREELLRHQLLEKRSMGMQRPLGMAGSGMGQSMEMERMIQAHRQMDPAMFPGQMTGGDGLAGTPMGIEFGGGRGLLSPPMGQSGLREVDPPMGPGNLNMNMNVNMNMNMNLNVQMTPQQQMLMSQKMRGPGDMMGPQGLSPEEMARVRAQNSSGMMGGPQKMLMPSQFPNQGQQGFSGGQGPYQAMPQDMGNTPDMFSPDQSSVPMGTVGTARLSHMPLPPASNPPGSVHLASNRGLGRRPSDLTISINQMGSPGMGHLKSPTLSQVHSPLVTSPSANLKSPQTPSQMVPLPSANPPGPLKSPQVLSSSLGVRSPTGSPSRLKSPSMAVPSPGWVASPKTAMPSPGVSQNKQPPLSINSSSTLGNVEQGALPPSAPRNSSSAPPANPSSGLMNPSLPFTSSPDPTPSQNPLSLMMSQMSKYAMPSSTPLYHNAIKTIATSDDELLPDRPLLPPPPPPQGSGPGISNNQPNQMHMNPAAAQSPMGMNLPGQQPLSHEPPPTMLPSPTPLGSNIPLHPNAQGTGGSSQNSMMMAPGGPDSLNAPCGPVPSSSQMMSFPPRLQQPHGAMAPTGAGGPGLQQHYPSGMALPPEDLPTQPPGPIPPQQHLMGKGMTGRMGDAYPPGVLPGVASVLNDPELSEVIRPTPTGIPEFDLSRIIPSEKPSSTLQYFPKSENQPPKAQPPNLHLMNLQNMMAEQTPSRPPNLPGQQGVQRGLSMSMCHPGQMSLLGRTGVPPQQGMVPHGLHQGVMSPPQGLMTQQNFMLMKQRGVGGEVYTQPPHMLSPQGSLMGPPPQQNLMVSHPLRQRSVSLDSQMGYLPTPGSMANLPF | Transcriptional regulator that acts as an activator. Promotes beta-catenin transcriptional activity. Plays a role in tumorigenesis. Enhances the neoplastic transforming activity of CTNNB1. Found in a complex with CDC73; CTNNB1 and PYGO1 (By similarity). Interacts with CTNNB1. localized also in punctate nuclear bodies as well in the cytoplasm. Colocalizes with CTNNB1. Expressed in kidney, liver, lung, testis, brain, spleen, heart and skeletal muscle. Highly expressed in numerous colorectal tumors compared to corresponding non-cancerous tissues. Expressed in embryo. Tne C-terminal domain is important for its transactivation activity. Belongs to the BCL9 family. |
Q9V4D2 | MLSTTMPRSPTQQQPQPNSDASSTSASGSNPGAAIGNGDSAASRSSPKTLNSEPFSTLSPDQIKLTPEEGTEKSGLSTSDKAATGGAPGSGNNLPEGQTMLRQNSTSTINSCLVASPQNSSEHSNSSNVSATVGLTQMVDCDEQSKKNKCSVKDEEAEISSNKAKGQAAGGGCETGSTSSLTVKEEPTDVLGSLVNMKKEERENHSPTMSPVGFGSIGNAQDNSATPVKIERISNDSTTEKKGSSLTMNNDEMSMEGCNQLNPDFINESLNNPAISSILVSGVGPIPGIGVGAGTGNLLTANANGISSGSSNCLDYMQQQNHIFVFSTQLANKGAESVLSGQFQTIIAYHCTQPATKSFLEDFFMKNPLKINKLQRHNSVGMPWIGMGQVGLTPPNPVAKITQQQPHTKTVGLLKPQFNQHENSKRSTVSAPSNSFVDQSDPMGNETELMCWEGGSSNTSRSGQNSRNHVDSISTSSESQAIKILEAAGVDLGQVTKGSDPGLTTENNIVSLQGVKVPDENLTPQQRQHREEQLAKIKKMNQFLFPENENSVGANVSSQITKIPGDLMMGMSGGGGGSIINPTMRQLHMPGNAKSELLSATSSGLSEDVMHPGDVISDMGAVIGCNNNQKTSVQCGSGVGVVTGTTAAGVNVNMHCSSSGAPNGNMMGSSTDMLASFGNTSCNVIGTAPDMSKEVLNQDSRTHSHQGGVAQMEWSKIQHQFFEERLKGGKPRQVTGTVVPQQQTPSGSGGNSLNNQVRPLQGPPPPYHSIQRSASVPIATQSPNPSSPNNLSLPSPRTTAAVMGLPTNSPSMDGTGSLSGSVPQANTSTVQAGTTTVLSANKNCFQADTPSPSNQNRSRNTGSSSVLTHNLSSNPSTPLSHLSPKEFESFGQSSAGDNMKSRRPSPQGQRSPVNSLIEANKDVRFAASSPGFNPHPHMQSNSNSALNAYKMGSTNIQMERQASAQGGSVQFSRRSDNIPLNPNSGNRPPPNKMTQNFDPISSLAQMSQQLTSCVSSMGSPAGTGGMTMMGGPGPSDINIEHGIISGLDGSGIDTINQNNCHSMNVVMNSMGPRMLNPKMCVAGGPNGPPGFNPNSPNGGLRENSIGSGCGSANSSNFQGVVPPGARMMGRMPVNFGSNFNPNIQVKASTPNTIQYMPVRAQNANNNNNNGANNVRMPPSLEFLQRYANPQMGAVGNGSPICPPSASDGTPGMPGLMAGPGAGGMLMNSSGEQHQNKITNNPGASNGINFFQNCNQMSIVDEEGGLPGHDGSMNIGQPSMIRGMRPHAMRPNVMGARMPPVNRQIQFAQSSDGIDCVGDPSSFFTNASCNSAGPHMFGSAQQANQPKTQHIKNIPSGMCQNQSGLAVAQGQIQLHGQGHAQGQSLIGPTNNNLMSTAGSVSATNGVSGINFVGPSSTDLKYAQQYHSFQQQLYATNTRSQQQQHMHQQHQSNMITMPPNLSPNPTFFVNK | Involved in signal transduction through the Wnt pathway. Binds to ARM and PYGO. Expressed both maternally and zygotically throughout development. Belongs to the BCL9 family. |
Q5T489 | MHSSNPKVRSSPSGNTQSSPKSKQEVMVRPPTVMSPSGNPQLDSKFSNQGKQGGSASQSQPSPCDSKSGGHTPKALPGPGGSMGLKNGAGNGAKGKGKRERSISADSFDQRDPGTPNDDSDIKECNSADHIKSQDSQHTPHSMTPSNATAPRSSTPSHGQTTATEPTPAQKTPAKVVYVFSTEMANKAAEAVLKGQVETIVSFHIQNISNNKTERSTAPLNTQISALRNDPKPLPQQPPAPANQDQNSSQNTRLQPTPPIPAPAPKPAAPPRPLDRESPGVENKLIPSVGSPASSTPLPPDGTGPNSTPNNRAVTPVSQGSNSSSADPKAPPPPPVSSGEPPTLGENPDGLSQEQLEHRERSLQTLRDIQRMLFPDEKEFTGAQSGGPQQNPGVLDGPQKKPEGPIQAMMAQSQSLGKGPGPRTDVGAPFGPQGHRDVPFSPDEMVPPSMNSQSGTIGPDHLDHMTPEQIAWLKLQQEFYEEKRRKQEQVVVQQCSLQDMMVHQHGPRGVVRGPPPPYQMTPSEGWAPGGTEPFSDGINMPHSLPPRGMAPHPNMPGSQMRLPGFAGMINSEMEGPNVPNPASRPGLSGVSWPDDVPKIPDGRNFPPGQGIFSGPGRGERFPNPQGLSEEMFQQQLAEKQLGLPPGMAMEGIRPSMEMNRMIPGSQRHMEPGNNPIFPRIPVEGPLSPSRGDFPKGIPPQMGPGRELEFGMVPSGMKGDVNLNVNMGSNSQMIPQKMREAGAGPEEMLKLRPGGSDMLPAQQKMVPLPFGEHPQQEYGMGPRPFLPMSQGPGSNSGLRNLREPIGPDQRTNSRLSHMPPLPLNPSSNPTSLNTAPPVQRGLGRKPLDISVAGSQVHSPGINPLKSPTMHQVQSPMLGSPSGNLKSPQTPSQLAGMLAGPAAAASIKSPPVLGSAAASPVHLKSPSLPAPSPGWTSSPKPPLQSPGIPPNHKAPLTMASPAMLGNVESGGPPPPTASQPASVNIPGSLPSSTPYTMPPEPTLSQNPLSIMMSRMSKFAMPSSTPLYHDAIKTVASSDDDSPPARSPNLPSMNNMPGMGINTQNPRISGPNPVVPMPTLSPMGMTQPLSHSNQMPSPNAVGPNIPPHGVPMGPGLMSHNPIMGHGSQEPPMVPQGRMGFPQGFPPVQSPPQQVPFPHNGPSGGQGSFPGGMGFPGEGPLGRPSNLPQSSADAALCKPGGPGGPDSFTVLGNSMPSVFTDPDLQEVIRPGATGIPEFDLSRIIPSEKPSQTLQYFPRGEVPGRKQPQGPGPGFSHMQGMMGEQAPRMGLALPGMGGPGPVGTPDIPLGTAPSMPGHNPMRPPAFLQQGMMGPHHRMMSPAQSTMPGQPTLMSNPAAAVGMIPGKDRGPAGLYTHPGPVGSPGMMMSMQGMMGPQQNIMIPPQMRPRGMAADVGMGGFSQGPGNPGNMMF | Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity (By similarity). Binds to beta-catenin (CTNNB1), PYGO1 and PYGO2; the interaction with PYGO1 increases PYGO1 affinity to histone H3 methylated at 'Lys 4'. Detected at low levels in thymus, prostate, testis, ovary and small intestine, and at lower levels in spleen, colon and blood. A chromosomal aberration involving BCL9 is found in a patient with precursor B-cell acute lymphoblastic leukemia (ALL). Translocation t(1;14)(q21;q32). This translocation leaves the coding region intact, but may have pathogenic effects due to alterations in the expression level of BCL9. Several cases of translocations within the 3'-UTR of BCL9 have been found in B-cell malignancies. Belongs to the BCL9 family. It is uncertain whether Met-1 or Met-27 is the initiator. |
Q8VE74 | MHPSNPKVRSSPSGNTQSSPKSKQEVMVRPPTVMSPSGNPQLDSKFSNQGKPGGSASQSQPSPCDSKSGGHTPKALPGPGGSMGLKNGAGNGAKGKGKRERSISADSFDQRDPGTPNDDSDIKECNSADHIKSQESQHTPHSMTPSTATAPRSSTPSHGQTPAPEPISAQKTPAKVVYVFSTEMANKAAEAVLKGQVETIVSFHIQNISNSKSERSTAPLNTQIPTLRNDPKPLPQQPPAPANQDQNSSQNARLQPTPPIQAPAPKPTAAPRPLDRESPGVENKLIPPVGSPGSSTPLPPDGTGPNSTPNNRAVTPVSQGSNSSSADPKAPPPPPVSGGEPPTLGENPDGLSQEQLEHRERSLQTLRDIQRMLFPDEKEFTAGQTGGPQQNTGVLDGPQKKPDGPIQAMMSQSQSLGKGPGPRTDVGAPFGPQGHRDVPFSPDEMVPPNMSSQSGPIGPDHLDHMTPEQIAWLKLQQEFYEEKRRKQEQVVVQQCSLQDMMVHQHGPRGVVRGPPPPYQMAPGEGWAPGAEPFPDGINISHSLPPRGMAPHPNMPGSQMRLPGFAGMINSEMEGPNVPNPASRPGLSGVSWPDDVPKIPDGRNFPPGQGVFSGPGRGERFPNPQGLSEEMFQQQLAEKQLALPPGMSMEGIRPGMEMNRMIPGSQRHMEPGSNPIFPRIPVEGPLSPSRGDFPKGMPPQIGPGRELEFGMVPGGMKGEVNLNVNMGSSSQMIPQKMREAGAGPEEMMKLRPGSSEMLPAQQKMVPLPFGEHPQQEYGVGPRPFLPMSQGPGSNSGLRNLREPIGPDQRTNSRLSHMPPLPLNPSSNPTSLSTAPPVQRGLGRKPLDISVAGSQVHSPGINPLKSPTMHQVQSPMLGSPSGNLKSPQTPSQLAGMLAGPAAAASIKSPPVLGSAAASPVHLKSPSLPAPSPGWTSSPKPPLQSPGIPPNHKAPLTMASPAMLGSVESGGPPPPTASQPASVNIPGSLPSSTPYPMPPEPTLSQNPLSIMMSRMSKFAMPSSTPLYHDAIKTVASSDDDSPPARSPNLPSMNSMPGMGINTQNPRISGPNPVVPMPTLSPMGMTQPLSHSNQMPSPNAMGPSIPPHGVPMGPGLMSHNPIMGHGSQEPPMVPQGRMGFPQGFPPVQSPPQQVPFPHNGPTGGQGNFPGGIGFPGEGPLGRPSNLPQSSADPALCKPGGPGAPDSFTVLGNSMPSVFTDPDLQEVIRPGATGIPEFDLSRIIPSEKPSQTLQYFPRGEVPGRKQPQGPGPGFSHMQGMMSDQAPRMGLALPGMGGPGPVGTPDIPLGTSPSMPGHNPMRPPAFLQQGMMGPHHRMMSPAQSTVPGPATLMTNPAAAVGMIPGKDRGPAGLYTHPGPVGSPGMMMSMQGMMGPQQNIMIPPQMRPRGMAADVGMGGFSQGPGNPGNMMF | Promotes beta-catenin's transcriptional activity. Involved in signal transduction through the Wnt pathway (By similarity). Binds to beta-catenin (CTNNB1), PYGO1 and PYGO2; the interaction with PYGO1 increases PYGO1 affinity to histone H3 methylated at 'Lys 4'. Belongs to the BCL9 family. Truncated N-terminus. |
Q95KQ6 | PMGMTQPLSHSNQMPSPNAMGPNIPPHGVPMGPGLMSHNPIMGHGSQEPPMVPQGRMGFPQGFPPVQSPPQQVPFPHNGPSGGQGNFPGGMGFPGEGPLGRPSNLPQSSADAALCKPGGPGGPDSFAVLG | Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity (By similarity). Binds to beta-catenin (CTNNB1), PYGO1 and PYGO2; the interaction with PYGO1 increases PYGO1 affinity to histone H3 methylated at 'Lys 4'. Belongs to the BCL9 family. |
Q8N1W7 | MARSRSRSPRWKHRSLSPVPRNAEHYKQRHSHGHYGCEYRKDPKRPVAWRMDSEKHGQSKPRIPSRGNIYYQSYEHRSPSPNIRNSLENVYMYKPHRGYSPGRGDSNRRAQYMPKYSEGIPYKEHERNSYPQKVQGGHSPDDHRVRGSGKGGKPPQRSIADSFRFEGKWHEDELRHQRIQEEKYSQSTRRGSEDFETRSSFQKRYPEDRDFRKYGHTSKRPKDVERYESREPARNPKWKPEHSLPPYQEDTDQWNLGPQTYRHAEREHPETSSATKVSYDYRHKRPKLLDGDQDFSDGRTQKYCKEEDRKYSFQKGPLNRELDCFNTGRGRETQDGQVKEPFKPSKKDSIACTYSNKNDVDLRSSNDKWKEKIKKEGDCRKESNSSSNQLDKSQKLPDVKPSPINLRKKSLTVKVDVKKTVDTFRVASSYSTERQMSHDLVAVGRKSENFHPVFEHLDSTQNTENKPTGEFAQEIITIIHQVKANYFPSPGITLHERFSTMQDIHKADVNEIPLNSDPEIHRRIDMSLAELQSKQAVIYESEQTLIKIIDPNDLRHDIERRRKERLQNEDEHIFHIASAAERDDQNSSFSKVKNVHTDGFQKPTHFIKSNFRKCIEKPYMNYTTQRKDIITHKPFEVEGNHRNTRVRPFKSNFRGGRCQPNYKSGLVQKSLYIQAKYQRLRFTGPRGFITHKFRERLMRKKKEYTDVATGI | Belongs to the BCLAF1/THRAP3 family. |
Q8BRL2 | MARSRSRSPRWKQRSLSPQSRNFEYHEERHFHGHYDPEYRHDQQRPFTWRMDDEKHGQNKPRIPPRVNSYHRSYVNRSPSPNVKPVEKFDTYKPHQEYFPGRGDDDRRSQYMPTYTESAATYMEHERDCYIPTVQGRYTPDDHRGRGRGSGRGEKPPQMSLGKPPKMSLGKPPQMSLADSLRFKEKWHEDELRHQRVQEESYPQSPRRGSEDFGTRNPFQKRYPEDHDFRKYGYTSKRPTDAARYENRDPARIPKWKPEHSFLPFQEKKEEWSFGAQGHRYTEREYPERSSTTRVSYDYRHKHHKLSESEQDFPDGRFHKHLKEEDRKYSSIKAPANRELDCFSTTRGREIENEQINGPFYLYNKNSVSYNHTNIKDADLEPCNDKWKKKISKEDCRKENASFSKQFDTSPKPEEKCYSLIKKKPLSVKVDRNKTDTFRSTSRYSAERQISHDLVAIGKTSDNFHPVFQHLDSTQNPENKPTEEFAQEIITLIHKVKADSFVTPDITLNERFSRIKNRQDADFNQTKSNSDPEFHRRIDMSLDDFQNKYTMVYEPDKTLVKVIEPNDLRHDIERRRKERLQNEDENIFHMASPTERNHQSPSFSKVKTIRADGFQKPPHFIKSNFRKFIQKPYINYTMQRKDAIDQKIFRVEENHQNRRGSKGSFKNFLGGRFQPHYKSHLVQKSMYIQAKYQRLRFAGPRGFITNKFRNRFLRKKKEYPVLPRTNNLELLQVEPTLYEDLTEHLIFVRNWN | Belongs to the BCLAF1/THRAP3 family. |
Q8GQN9 | MYTLSVADHSNTPPAIKIPERYNAADDLIGRNLLAGRGGKTVYIDDAGSYTYDELALRVNRCGSALRTTLGLQPKDRVLVCVLDGIDFPTTFLGAIKGGVVPIAINTLLTESDYEYMLTDSAARVAVVSQELLPLFAPMLGKVPTLEHLVVAGGAGEDSLAALLATGSEQFEAAPTRPDDHCFWLYSSGSTGAPKGTVHIHSDLIHTAELYARPILGIREGDVVFSAAKLFFAYGLGNGLIFPLAVGATAVLMAERPTPAAVFERLRRHQPDIFYGVPTLYASMLANPDCPKEGELRLRACTSAGEALPEDVGRRWQARFGVDILDGIGSTEMLHIFLSNRAGDVHYGTSGKPVPGYRLRLIDEDGAEITTAGVAGELQISGPSSAVMYWNNPEKTAATFMGEWTRSGDKYLVNDEGYYVYAGRSDDMLKVSGIYVSPIEVESALIAHEAVLEAAVVGWEDEDHLIKPKAFIVLKPGYGAGEALRTDLKAHVKNLLAPYKYPRWIEFVDDLPKTATGKIQRFKLRSA | Catalyzes the ligation of benzoate and CoA to form benzoyl-CoA at the expense of ATP. The enzyme also ligates 2-aminobenzoate and CoA. The enzyme shows activity toward a number of benzoate derivatives. ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate Optimum pH is 8.5. Monomer. By benzoate and 2-aminobenzoate. Belongs to the ATP-dependent AMP-binding enzyme family. Benzoate-CoA ligase subfamily. |
Q86WY0 | MGRSNSRSHSSRSKSRSQSSSRSRSRSHSRKKRYSSRSRSRTYSRSRSRDRMYSRDYRRDYRNNRGMRRPYGYRGRGRGYYQGGGGRYHRGGYRPVWNRRHSRSPRRGRSRSRSPKRRSVSSQRSRSRSRRSYRSSRSPRSSSSRSSSPYSKSPVSKRRGSQEKQTKKAEGEPQEESPLKSKSQEEPKDTFEHDPSESIDEFNKSSATSGDIWPGLSAYDNSPRSPHSPSPIATPPSQSSSCSDAPMLSTVHSAKNTPSQHSHSIQHSPERSGSGSVGNGSSRYSPSQNSPIHHIPSRRSPAKTIAPQNAPRDESRGRSSFYPDGGDQETAKTGKFLKRFTDEESRVFLLDRGNTRDKEASKEKGSEKGRAEGEWEDQEALDYFSDKESGKQKFNDSEGDDTEETEDYRQFRKSVLADQGKSFATASHRNTEEEGLKYKSKVSLKGNRESDGFREEKNYKLKETGYVVERPSTTKDKHKEEDKNSERITVKKETQSPEQVKSEKLKDLFDYSPPLHKNLDAREKSTFREESPLRIKMIASDSHRPEVKLKMAPVPLDDSNRPASLTKDRLLASTLVHSVKKEQEFRSIFDHIKLPQASKSTSESFIQHIVSLVHHVKEQYFKSAAMTLNERFTSYQKATEEHSTRQKSPEIHRRIDISPSTLRKHTRLAGEERVFKEENQKGDKKLRCDSADLRHDIDRRRKERSKERGDSKGSRESSGSRKQEKTPKDYKEYKSYKDDSKHKREQDHSRSSSSSASPSSPSSREEKESKKEREEEFKTHHEMKEYSGFAGVSRPRGTFFRIRGRGRARGVFAGTNTGPNNSNTTFQKRPKEEEWDPEYTPKSKKYFLHDDRDDGVDYWAKRGRGRGTFQRGRGRFNFKKSGSSPKWTHDKYQGDGIVEDEEETMENNEEKKDRRKEEKE | Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Interacts with Bcl-2 related proteins, EMD, with the adenovirus E1B 19 kDa protein and with DNA. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN. Component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3. Ubiquitous. Citrullinated by PADI4. Belongs to the BCLAF1/THRAP3 family. Contaminating sequence. Potential poly-A sequence. Contaminating sequence. Potential poly-A sequence. Contaminating sequence. Potential poly-A sequence. Contaminating sequence. Potential poly-A sequence. |
Q9CSW5 | MGRSNSRSHSSRSKSRSQSSSRSRSRSHSRKKRYSSRSRSRTYSRSRSRDRIYSRDYRRDYRNNRGMRRPYGYRGRGRGYYQGGGGRYHRGGYRPVWNRRHSRSPRRGRSRSRSPKRRSVSSQRSRSRSRRSYRSSRSPRSSSSRSSSPYSKSPVSKRRGSQEKQTKKAEGEPQEESPLKSKSQEEPKDTFEHDPSESIDEFNKSATSGDIWPGLSAYDNSPRSPHSPSPIATPPSQSSSCSDAPMLSTVHSAKNTPSQHSHSIQHSPERSGSGSVGNGSSRYSPSQNSPIHHIPSRRSPAKTITPQNAPREESRGRSSFYPEGDQETAKTGKFLKRFTDEESRVFLLDRGNIRDKEAPKEKGSEKGRADGDWDDQEVLDYFSDKESAKQKFHDSEGDDTEETEDYRQFRKSVLADQGKSFATSSHRNTEEEGPKYKSKVSLKGNRESDGFREEKNYKLKETAYIVERPSTAKDKHKEEDKGSDRITVKKEVQSPEQVKSEKLKELFDYSPPLHKSLDAREKSIFREESPLRIKMIASDSHRPEVKLKMAPVPLDDSNRPASLTKDRLLASTLVHSVKKEQEFRSIFDHIKLPQANKSTSESFIQHIVSLVHHVKEQYFKSPAVTLNERFTSYQKATEEHSTRQKSPEIHRRIDISPSALRKHTRLAGEERGFKEEIQKGDKKLRCDSADLRHDIDRRRKERSKERGDSKGSRESSGSRKQEKTPKDYKEYKPYKDDSKHKGRERDHSRSSSSSASPSSPSSREEKESKKEREEEFKTHHEMKDYSGFAGVSRPRGTFFRIRGRGRARGVFAGTNTGPNNSNTTFQKRPKEEEWDPEYTPKSKKYFLHDDRDDGVDYWAKRGRGRGTFQRGRGRFNFKKSGSSPKWTHDKYQGDGIVEDDEETMENNEEKKDRRKEEKE | Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA (By similarity). Interacts with Bcl-2 related proteins, EMD, with the adenovirus E1B 19 kDa protein and with DNA. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN (By similarity). Component of a MACOM-like complex, named WTAP complex, composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3 (By similarity). Citrullinated by PADI4. Belongs to the BCLAF1/THRAP3 family. |
M5AW86 | MGTVPANPFKIIQLAFKETVPKAHAELQKWHQEALKIEDVEIREQAAWTVNDKTFHCEGGSIFALLAGENKDNHIQFLVAYQTICDYLDTLCDKNDAHDPNDFRSIHQALLDCLTPDKPYGDYYQYRDRFEDNGYLRKLVDACREATASFPGFADMQTHMQEVSQFYIDFQVYKHVEEEKREPLLKDFYERNKHFAPTMRWYEFACGTASTLALYCMAAYAAAPVQTAQGQQIKEAYFTWVQGVHILLDYFIDQEEDRQENEMNFVAYYRDSKEMFERFKYIDEKATEKLQMLPDKKFHLLLKTGLYALYLSDKKVMSHPRLKAEAKQLIKLGGFPASLFYYNRWIFKRKIS | Catalyzes the conversion of geranylfarnesyl diphosphate (GFPP) and hexaprenyl diphosphate (HexPP) into beta-geranylfarnesene and beta-hexaprene, respectively (PubMed:23554321, PubMed:25882275). Also produces beta-heptaprene from heptaprenyl diphosphate (HepPP) as a minor product (PubMed:25882275). (2E,6E,10E,14E)-geranylfarnesyl diphosphate = beta-geranylfarnesene + diphosphate all-trans-hexaprenyl diphosphate = beta-hexaprene + diphosphate all-trans-heptaprenyl diphosphate = beta-heptaprene + diphosphate Belongs to the large terpene synthase family. |
P86393 | ATYYGNGLYCNKQKHYTWVDWNKASREIGKITVNGWVQH | Bacteriocin with antibacterial activity against C.jejuni. Stable from pH 3.0-9.0, inactivated at pH 10.0. Thermostable, activity is retained after incubation at 100 degrees Celsius for 15 minutes. Antimicrobial activity is lost upon treatment with beta-chymotrypsin, proteinase K and papain, but not when treated with lysozyme or lipase. Belongs to the bacteriocin class IIA/YGNGV family. |
C0HJE5 | NKPEALVDYTGVXNS | Has bactericidal activity against Gram-positive bacteria M.luteus, methicillin-resistant S.aureus, methicillin-sensitive S.aureus and B.stearothermophilus as well as against the Gram-negative bacteria E.coli and S.typhi. On the 2D-gel the determined pI of this protein is: 7.0, its MW is: 10.7 kDa. |
P85833 | KKIDTRTGKTMEKTEKKIELSLKNMKTAT | Has antibacterial activity against strains of L.monocytogenes, L.lactis, B.subtilis, S.typhi, S.aureus, C.perfringens, E.aerogenes and M.luteus but not against E.coli, S.sonnei, S.pneumoniae, S.faecalis, P.aeruginosa, K.pneumoniae or P.vulgaris. Activity is stable between pH 2 and 9 but decreases at a more basic pH. Thermostable. Activity remains unaffected even after incubation at 100 degrees Celsius for 30 minutes. |
P86395 | FVYGNGVTSILVQAQFLVNGQRRFFYTPDK | Bacteriocin with antibacterial activity against C.jejuni. Stable from pH 3.0-9.0, inactivated at pH 10.0. Thermostable, activity is retained after incubation at 100 degrees Celsius for 15 minutes. Antimicrobial activity is lost upon treatment with beta-chymotrypsin, proteinase K and papain, but not when treated with lysozyme or lipase. Belongs to the bacteriocin class IIA/YGNGV family. |
P08696 | MANNIIPNVSSGDLVGSTPTFPPNAVVRGDFLYLRDVDGNQIPGRTVSDGDEITVLFISNEKNIVLVQYPTSSGYRQGYVTNATSIIKYKDDYSWVNGSTPEPVYDFDKTTQIGTLDPRERAVVLYKVDGMTYVAYDTGKGKLTKSGLVHYEGSGSSTGGGSFNGVAPGEVVPGGFTYENNAEVVGDELYLRDANGNLIPGRSVSVGDKITVLDVGYTKQLALVQYPAGDVVRQGYVTNATNLIRYFNQYSWHNGSTSEEVLDENGGHLGSLNPYEAATLLYEKNGMKHVVYDTNKGPNTKSGYVKYEGAAATRVDIPYPSITNAQKIVYGISGRGRELAAYKVGNGSNSLVFVCAIHGWEDNWAADGIELTRIGNGLIEHFQNAGTNNWSLYIIPVANPDGLSEGFTNNGPGRCTIVGAVDCNRDFPLGFSPGGVPRYHSGSEPLSVSESKSLHDFIQGVKNRTSGEMCVIDLHGWEGAAIGNPEIGEYFRNQFGFGQRSGYGDNRGFMIGWAKSIGAKAALIELPGSTKSHSDVVNGRYLQKIINAVTNLIGGSGGSSSGGSSFSDVSYEATGEVINVQSFLNVREGAGLYTNSIGQLRQGNKVNIVAKNGDWYKIKYGSEYGYVNSGYIIILKNNTSVKLEDWQEDCIKFGWGPITKEKYLEYMDSTRLYKSIENDISQAIKNKSLINVINPLNFSVSEMIACTQIVFNNETTSFFRDEWYSKSNPNFIVKYKKLSNGQIIVLDRINIKKPEKLKTKIPKAAKGAFKDTIKFEFFKGIDGWFTAISGAISIGSDLSVFQSNGELKSNEDIAKALAAAVIVNGVETMFCAFLGGFIAQCIAPEFPIVAAVAGAIVSAIAAFAIGYFVDNHEKEKYLMNSFKGLIDYLF | May function as an ionophore. By UV irradiation. |
P86394 | VNYGNGVSCSKTKCSVNWGIITHQAFRVTSGVASG | Bacteriocin with antibacterial activity against C.jejuni. Stable from pH 3.0-9.0, inactivated at pH 10.0. Thermostable, activity is retained after incubation at 100 degrees Celsius for 15 minutes. Antimicrobial activity is lost upon treatment with beta-chymotrypsin, proteinase K and papain, but not when treated with lysozyme or lipase. Belongs to the bacteriocin class IIA/YGNGV family. |
Q9U5X3 | MSTRRQAITLYRNLLRESEKLPSYNFRMYAARKIRDTFRANRSTRDFAEIDRQMAEGQQNLELIRRQVIIGHLYSADKLVIENKKTLKPSDD | Interacts with Nfs1 (PubMed:29491838). Might form a complex with Nfs1, IscU and fh (Probable). Belongs to the complex I LYR family. |
P0DMY0 | MNKALFLCLVVLCAAVVFAAEDLQKAKHAPFKRGAAGAAICICPDKVGRGDLWLFRGDCPGGYGYTSDCYVWPNICCYPH | Blocks Kv3 voltage-gated potassium channels. Reduces blood pressure. Moderately expressed in the ectodermal tissue from the distal and proximal tentacles, body wall, and oral disk. Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. Opinions are divided on whether Anemonia viridis (Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate species. |
P86462 | GVPCKCGSKKGVYWFGQITGCPGGHGYKGSCNYLLGK | Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. |
P0DMY1 | MNKALFLCLVVLCAAVVFAAEDLQKAKHAPFKRAAPCFCSGKPGRGDLWILRGDCPGGYGYTSNCYKWPNICCYPH | Blocks Kv3 voltage-gated potassium channels. Reduces blood pressure. Moderately expressed in the ectodermal tissue from the distal and proximal tentacles, body wall, and oral disk. Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. Opinions are divided on whether Anemonia viridis (Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate species. |
P0DMY2 | MNKALFLCLVVLCAAVVFAAEDLQKAKHAPFKRGAAPCFCPGKADRGDLWILRGTCPGGYGYTSNCYNWPNICCYPH | Blocks Kv3 voltage-gated potassium channels. Reduces blood pressure. Experimental results show no expression in the ectodermal tissue from the distal and proximal tentacles, body wall, and oral disk. Since paralogs are expressed in this tissue, an expression of this toxin in this tissue is probable. The negative results could be explained by the very low abundance of EST sequences. Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. Opinions are divided on whether Anemonia viridis (Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate species. |
P0DMY4 | MNKALFLCLVVLCAAVVFAAEDLQKAKHAPFKRGAQVCFCPGKVDRGDLWILRGDCPGGYGYTSNCYTWPNICCYPQSFSGR | Blocks Kv3 voltage-gated potassium channels. Reduces blood pressure. Weakly expressed in the ectodermal tissue from the distal and proximal tentacles, body wall, and oral disk. Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. Opinions are divided on whether Anemonia viridis (Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate species. |
P0DMY3 | MNKALFLCLVVLCAAVVFAAEDLQKAKHAPFKRGAAGAAPCFCPDKVDRGDLWMFRGDCPGGYGYTSDCYVWPNICCYPH | Blocks Kv3 voltage-gated potassium channels. Reduces blood pressure. Weakly expressed in the ectodermal tissue from the distal and proximal tentacles, body wall, and oral disk. Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. Opinions are divided on whether Anemonia viridis (Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate species. |
P0DMY6 | MNKALFLCLVVLCAAVVFAAEDLQKAKHAPFKRAARCFCPGKPDRGDLWILRGTCPGGYGYTSNCYKWPNICCYPH | Blocks Kv3 voltage-gated potassium channels. Reduces blood pressure. Weakly expressed in the ectodermal tissue from the distal and proximal tentacles, body wall, and oral disk. Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. Opinions are divided on whether Anemonia viridis (Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate species. |
P0DMY7 | MNKALFLCLVVLCAAVVFAAEDLQKAKHAPFKRATACFCPGKADRGDLWILRGDCPDGYGYTTYCYKGPNICCYPH | Blocks Kv3 voltage-gated potassium channels. Reduces blood pressure. Weakly expressed in the ectodermal tissue from the distal and proximal tentacles, body wall, and oral disk. Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. Opinions are divided on whether Anemonia viridis (Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate species. |
P0DMY8 | MNKAFFLCLVVLCAAVVFAAEDLQKGKHAPFKRAAPCFCSGNPGRGDLWILRGPSPGGYGYTSNCYKWPNICCFPP | Blocks Kv3 voltage-gated potassium channels. Reduces blood pressure. Experimental results show no expression in the ectodermal tissue from the distal and proximal tentacles, body wall, and oral disk. Since paralogs are expressed in this tissue, an expression of this toxin in this tissue is probable. The negative results could be explained by the very low abundance of EST sequences. Lacks the conventional Cys residue at position 55. Thus, only 2 disulfide are possible present. Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. Opinions are divided on whether Anemonia viridis (Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate species. |
P0DQN7 | MNKALFLSLVVLCAAVVFAAEDLQKAKHAPFKLAAPCFCSGKPGRGDLWIFRGTCPGGYGYTSNCYKWPNICCYPH | Blocks Kv3 voltage-gated potassium channels (By similarity). Reduces blood pressure (By similarity). Experimental results show no expression in the ectodermal tissue from the distal and proximal tentacles, body wall, and oral disk. Since paralogs are expressed in this tissue, an expression of this toxin in this tissue is probable. The negative results could be explained by the very low abundance of EST sequences. Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. Opinions are divided on whether Anemonia viridis (Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate species. |
P0DQN6 | AAPCSCPGKPGRGDLWIFRGTCPGGYGYTSNCYKWPNICCYPH | Blocks Kv3 voltage-gated potassium channels (By similarity). Reduces blood pressure (By similarity). Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. Opinions are divided on whether Anemonia viridis (Forsskal, 1775) and Anemonia sulcata (Pennant, 1777) are separate species. |
P86470 | GTTCKCGSTLGIYWFAVTSCPPGRGYTTHCGYF | Potently and reversibly blocks mammalian Kv11/KCNH/ERG voltage-gated potassium channels. Acts as a gating-modifier toxin that shifts the voltage-dependence of ERG activation in the positive direction and suppresses its current amplitudes elicited by strong depolarizing pulses that maximally activate the channels. Belongs to the sea anemone type 3 (BDS) potassium channel toxin family. |
B6D9A8 | MEPLKNVNTGQPCSTVPFPVSDETVEHLNGLYEEINRRFGLDRDAIETILPCTPFQYDVLDCAANDARHAVGHAMYEISQHVHVQRFIAAWRETVRRTPALRACTFTSTTGESFQLVLRESFVLSRIYWSSSSSLQAAVLKDETTAAIAGPRCNRLVLLEDPDTRKQLLIWVFHLALVDSTVQEPILRRVLAAYKSEDDQLDSLPLTPDSSGGSDSDSPSTLKMPRAFDQEKATQFWQRQLSGLDASVFPPLSSHLTTPKADAKIEHYISWPASAAQHRWSSTTVCQAALAVLLSRYSHSSEALFGVVTEQVCMFEGQRLLINGPTRSVVPFRVHCGPEQSVTDLLKSIASDNHDMRQFAHVGLCNISRIGDDQSAACRFQTVLSVSNRRSSEDAASGEVLQILQESEGFAPCADRALLLRCETSRQGALLVARYDQGVIEPPQMARFLRQLGWLMEQLQSAADDALSVKQLDIVTREDRAEIDSWNSDALEVQESLLHSAFVKRAAESPSDPAVLSWDGAWTYSELDNVSSRLAAHIRSLDLSHEQLIVPVYFEKSKWVVASILAVLKAGHAFTLIDPKDPPARTTRIVQQTSAKVALTSKLHQDTVQAIIGRCIVVDDDFVQSLGSASQCQEKSELTVKPHNLAYAIFTSGSTGDPKGIMIEHQAFASCVAKFGPALIPHNARALQFASHGFGACLLEILPTLLRGGCVCIPSDLDRMHNIPDFIRRYNVNWMMATPSYMTTFKPEDVPGLQTLILVGEQMSASVNATWASRLGLFDGYGQSESCSICFIGKISPVSEANNIGRAVGAHSWIVHPDDPDRLAPVGAVGELLIESPGIARGYIAAPATDRNPFLETAPAWYAPRQPPTGVKFYRTGDLARYAADGTVVCLGRIDSQVKIRGQRVEMGAVETRLRQQVPSDITVVAEAVKRSGSSGSTVITAFLIDSSDKNNSSAASAKDARILDQTATQEMNAKLCQVLPPHSVPSCYICMHALPRTATGKVDRKTLRSIGSKLLEQQAYKKSPETMQKSKSAETLETGPEARLKEVWLQSFNLEPASPKCGASFFELGGDSITAIKMVNMARAAGLELKVSDIFQNPTLARLQAVMSGDSTPSTITTPFATIPASTWDGPVEQSYSQGRLWFLDQLDIGAVWYLIPYAVRMRGALNIDALRAALLALEQRHETLRTTFENQNGVGVQIVHQRLAKELKIIDASSHGDDGYLQPLEQEQTTPFDLTCEAGWRASLICVGEDHHVLSIVMHHIVSDGWSIDVLRQELGQLYAAVLHGDEDPLSAVSPLPIQYRDFSMWQRRQQVAEHDRQLQYWRKQLADCSPAKLPTDFPRPPLLSGDAGSVPVEISGELFQKLHRFCNVTSTTPFAVLLAAFRAAHYRLTGVDDAVVGTPIANRNRPELERLIGFFVNTQCMRITVDDDDTFEGLVRQVRRTTTEAFENEDVPFERVVSAMLPAGGGSRDLSQTPLAQLIFAVHSQENLGKFELEGLESEPVANKAYTRFDAEFHLFQTRDGLNGYLNFAAELFKLETMQNVVSVFLQILRHGLEQPKSLISVLPLTDGLKELDSMGLLKIHRGLEYQRDSSLVDIFRSQVATCPDTIAVIDSSARLTYAQLDHQSNLLEAWIRRKGLPAESLVGVLSPRSCETIIAFLGILKANLAYLPLDPKSPVSRMRDVLSDLPGHTIILLGSDVAAPDLELPCLELVRISDALKSGASAVNGSETTDLSAPSANSLAYVLYTSGSTGRPKGVMVEHRAIVRLVQRGVIPNFPPLRGAIMAHLFNTVFDGATYEIFLMLLNGGTLVCIDYLTTLSPKALETVFLREGINCAIMTPALLKLYLANARDGLKGLDMLMVAGDRFDPQDAVEAQTLVRGDCYNAYGPTENGVMSTLYKIDTSDSFINGVPLGRAIDNSGAYITDPNQQLVGPGVLGELIVTGDGLARGYTDPALDRDRFVQVVINGESVRAYRTGDRMRYRAGQDCLFEFFGRMDFQFKIRSNRIESAEVEAAILSHPLVRDAAIVVVGVQEEQEPEMVGFVVAADDAVEQEATDNQVEGWQELFESSMYNGIDAISPSALGKDFTGWTSMYDGSEIDKSEMQEWLDDTIHTLRDGHVPGHVLEIGTGTGMILFNLGSVESYVGLEPTKSAVEFVNKAIKTLPNLAGRAEVHTGTATDIDQLSGLRPDLVILNSVVQYFPTVEYLTRVVDALVRIRGVKRLFFGDVRSQALHRQFLAACAMHALGKTATRDDVRRYMAEREEREEELLVEPAFFTALMNRHPNLIQHVEILPKNIRATNELSAYRYAAVVHLRDPESAARPVYPIAADDWVDFQASQMRSDVLREYLRLSAGADTVAVCNIPYEKTIFERLIVESLDDNTGSDAPQSRLHGRSLDGAPWISAVRSDAESRASLSVPDLVQLAAESGFQVQVSAARQWSQSGALDAVFHRRHASSSQPTMRTLFQFPDDNALRASATLTNRPLQRLQRRRVAAQIRERLQTLVPSYMIPAKIVVLDQMPLNANGKVDRKELARRARTTTMTKKKKPQRLASEPACPISDIEVALCEEATATFGMQVGISDHFFKLGGHSLLATKLISRVGDRLKARLTVKDVFDHPIFSELAIVIREGLQNVVPVALNGGGQAKQGSAGVVAPRNEMETMLCEEFANVLGMDVGVTDNFFDLGGHSLMATKLAARIGRRLNTTISVKEVFEHPIVFQLANSLELGQLESDRVKHTMLADYTAFQLLSVEDLQGFLQNEISPQLECAHGGIQDVYPATHMQKAFLCDASTGHPKPLVPFYIDFPPDSDCSTLVEACSSLVKRFDMFRTVVVEAAGELYQVVLEHFDLQIDVVETEENVHAATNDFVDRILEVPVHLGQPLIQFTILKQASSVRVLLCLSHALYDGLSLEHVVRDLHMLYKGRSLLPANQFSRYMQYMDHTRKAGCDFWRDVIQDTPITVLGHVDAGGRELEVEAARTLHATKIISIPLQAVRSSIITQATVFNAACALVLSRETGAKDVVFGRIVSGRQGLPVSWQNIVGPCTNAVPVRARIIDDDDDNHRQMLRDMQDQYLLSLPFETLDFDEVRRSCTNWPATANNYACCVTYHDFSYHPESEMEQQRVEMGVLARKDALLKEEPVYDLGIAGEVEPDGVHLQVTVVAKTRLFSEERAAYLMEEVCRLFESLNSAL | Beauvericin nonribosomal cyclodepsipeptide synthetase; part of the gene cluster that mediates the biosynthesis of beauvericin (BEA), a non-ribosomal cyclic hexadepsipeptide that shows antibiotic, antifungal, insecticidal, and cancer cell antiproliferative and antihaptotactic activity (PubMed:18804027, PubMed:28534477). Ketoisovalerate reductase BEA2 catalyzes the NADPH-specific reduction of ketoisovaleric acid to hydroxyisovalerate, a precursor for beauvericin biosynthesis (PubMed:19105175, PubMed:27449895). The nonribosomal cyclodepsipeptide synthetase BEA1 then catalyzes the formation of beauvericin via condensation and cyclization of 3 dipeptidol monomers, each composed of one unit of hydroxyisovalerate and one unit of N-methyl-phenylalanine (PubMed:18804027, PubMed:28534477). 3 (R)-2-hydroxy-3-methylbutyrate + 6 ATP + 3 L-phenylalanine + 3 S-adenosyl-L-methionine = 6 AMP + beauvericin + 6 diphosphate + 6 H(+) + 3 S-adenosyl-L-homocysteine NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, additional domains required for further modifications are also present. Beauvericin synthetase has the C1-A1-T1-C2-A2-MT-T2a-T2b-C3 domain organization (PubMed:18804027, PubMed:28534477). During catalysis, C3 and C2 take turns to incorporate the two biosynthetic precursors into the growing depsipeptide chain that swings between T1 and T2a/T2b with C3 cyclizing the chain when it reaches the full length (PubMed:28534477). Impairs the production of beauvericin (PubMed:18804027). Belongs to the NRP synthetase family. |
S0EN43 | MTSLNTKSGTPVVPLLLRSDDASHTDTLVEEVSCSLGLGRDRIENILPSTAFQQDVIDCAGSEKQRSIGHVAYEISNDIDISKLAAAWKDTINRTPALRTCAFTSSSGETYQVILKDSFVFSWMFSTSADQKDAVVKDEAAAAASGPRCNRFVLLDDPIQKKILIWTFSHALVDTSFQERILGRVLKAYTHGHDELSNRPYTPESSDPEDDGLSLTPTDGSKTPETEGLHPATQYWKNYLSDLNASAFPHLTSPLAVPYPNAKSEHRITFTASSSSTWPSVAVCRTALAILLSRYTHSQEALFGVVTEQQQLLVNGPTRTVVPFRVHCASDQSLSDIIDVVNANDDAIRQFADVGLRSISSTGDDGVAASGFQTVLLVTEGDNEQSSSTFEILQKTEESELFMPCTNRALLLHCQIASDGLSIIARYDKSLIHSQQIARLLRQLGQLIQRLRGSPDKLPSAGELDISTSEDQAEIQSWNSHPIPSQPTLIHKEMLKTASLSPSKVAICAWNGEWTYSELDNITSRLAALIKFSTPDQEHAILPIYFEKSKWVVASMLAVIKAGHAFALIDPNDPPARVSQVVGQTGATVALTSKLYRSKVQGIIERCIIVDDDLVQSLICTCALKPDPTLAKVTPEDLAYVIFTSGSTGDPKGIMIEHRAFSSCALQFGSALGINSDTRALQFGSHAFGACLLEIMTTLIHGGCVCIPSDDDRMNNVPAFVNRANVNWMMATPSYMGTFQPDDVPGLKTLVLVGEQMSPSVNAIWAPRVQVLDGYGQSESSSICFVGKISSSGADPNNIGHSVGAHSWIIDPSDPNRLVPIGAIGELVIESPGIARDYIIPPPTENSPFFSTVPPWYPFKELPNGIKFYRTGDLARYASDGTVVCLGRMDSQVKIRGQRVELGAVETHLRQQLPDDMSIVVEAVKPSDLPTSTVLVAFLITEATKSVRDATILDLAATKAMSVKLEHVLPRHSIPSCYISMQHLPRTATGKVDRRKLRSIGRDMLAQQLQGTSFRPSQLSSTTTSSQSKLEEVWRQCLGLEPGAANINSTFFELGGHSITAIKMVNMARSAGIDLKVSDIYQNPTLAGLEAIVNGSAEPYAIIPTTTRDGPVEQSYSQGRLWFLDQLEVGALWYLIPYAVRMRGLVDIDALSRALMALEQRHETLRTTFEDCDGAGVQIIHKILSKKLRVVDAPDSDYLDLLKQEQTTPFDLTSEAGWRALLIRLNDTDYILSIVMHHIVSDGWSIDVLRHDLSQLYAAALQGRDLASAMNPLPIQYSDFAMWQKQEAQALEHEKQLDYWKRQLADCSPAKLPTDFPRPALLSGEAGVVPVSIDRQLYQNLRDFCNENNTTSFAVLLAAFRAAHYRLTGVDDAVIGTPIANRNRWELENIIGFFVNTQCMRITVDDQDTFGSLVSQVRATTTAAFENEDVPFERVVSTMLPGSRDLSRTPLAQLIFAVHSQKDLGRFELQGLESEVVASKAYTRFDIEFHLFQEADGLRGSCNFATDLFRPETVENMVSVFFQILRNGLEKPNIPISVLPLTDGIEELRRLDLLRIKKVEYPRDASLVDIFRTQVAAYPDSLAVVDSSSRLTYTELDLQSDRLAARLRRQGMPAETLVGVLAPRSCEAIVAIIGILKANLAYLPFDVKSPSARLEDILSSIPGQTIVLLGSDVPVPELSIPGLEFMRIVDAIECCDTNNLNGHAHVDNSNPTATSLAYVLFTSGSTGRPKGVMVEHRVIVRLMTSNIIPDFPVQPRSAHMFNIAFDGATYEIFFTLLNGGTLVCIDYMTTLDVKALQDVFLKEKINAACMAPALLKLYLTDARDALRGLDFLMAAGDRFDGQDAIEAQSLVRGQCYNGYGPTENGIMSTRYPIAVGDSFINGVPIGRAVNNSGAYVTDLNQQLVGVGVMGELVVTGDGLARGYFDPALNENRFIHIEVDGQRVRAYRTGDRVRYRVGDGLIEFFGRMDTQFKIRGNRIESAEVEAAMLGHGSVRDAAVVVQKDDGEKADLVGFVVIDHDHSLEGDANDNQVEGWQDHFETEMYADIGDIDPFTIGKDFKGWTSMYDGSEIDKVEMQEWLDDTIKTLRDGQAPGHVLEVGTGSGMILFNLGDGLQSYRGLEPSKSAAAFTNSVIKSVPSLASKAEVHVGTAQDVSQLTDLHPDLVVINSVAQYFPSPEYLAQVADTLIHIPGVKRLFFGDMRTNATNKHFLAARAIRTLGDTATKDFVRQKMAELEEREEELLVEPAFFTALQDRFPDLVHHVEILPKNMHATNELSAYRYAAVVHIRDSDSVPVHTIEKSTWVDFGASRMDRTSLLQFLRRSKGSPTVAISNIPFAKTIFERQIVESLEAEDESKLDGAVWISAVGSDADSRASLSVPDLRRLAEEAGFRLEVSAARQWSQSGALDAVFHHLPSPSDTRRTLIKFPNDNHLRSSATLSNRPLQGLQRRRATLQVRERLQSLLPSYMIPSSIVVLDQMPLNPNGKVDRKELARQARIMPKQQTALPVQAVPISDIEAILCDEATATFGMKVDISDDFFKLGGHSLLATKLISRVEQRFNVRVTVKDVFDNPVFANLAVVIREGLASRTTLTNSQDKQGWSARVAPRTETEITLCDEASKLLGIEVGITDNFFDLGGHSMMATKLAMRLGRRLDTTIVVKDIFDYPVLFQLSKKLESTDSGTDNEEVQVDDYTPFELLSLENPQDFIQRQICSQLNVSLESIQDMYQSTQMQKSFLFSPGTGSPRPLTPFYIDFPVDSDPPTLVNACHSLVQHIDMFRTVFVLASEQLYQVVLKHLEVPIETIVTNQNVNTATNDFLVEHAQDPIRLGESLIRIAILKQSSSVRVLLRLSHALYDGLSLEPIVRNLHILFNGMSLLPPTQFRRYMEYTANSQEKGFEFWRDVIGDSPMTILSDAGNGAYHREVSPSKALHLSKVVSVPSQAIRSSIATQATVFNSACALVLSKESRSSDVVFGRIVSGRQGLPVNCQDIIGPCTNAVPVRAHIGTDGNHHQMLRDMQDQYLRSLPFETLGFEEIKRNCTDWPDSTTNFACCVTYHNFEYHPESEVEQQRVEMGVLSKHVELRKDEPLYDLAIAGEVEPDGMSLKVTIIARAHLFEEERVQYFLEEVCNTFQTLNFSL | Beauvericin nonribosomal cyclodepsipeptide synthetase; part of the gene cluster that mediates the biosynthesis of beauvericin (BEA), a non-ribosomal cyclic hexadepsipeptide that shows antibiotic, antifungal, insecticidal, and cancer cell antiproliferative and antihaptotactic activity (PubMed:25543026, PubMed:27750383, PubMed:28125067). Ketoisovalerate reductase BEA2 catalyzes the NADPH-specific reduction of ketoisovaleric acid to hydroxyisovalerate, a precursor for beauvericin biosynthesis (By similarity). The nonribosomal cyclodepsipeptide synthetase BEA1 then catalyzes the formation of beauvericin via condensation and cyclization of 3 dipeptidol monomers, each composed of one unit of hydroxyisovalerate and one unit of N-methyl-phenylalanine (By similarity). 3 (R)-2-hydroxy-3-methylbutyrate + 6 ATP + 3 L-phenylalanine + 3 S-adenosyl-L-methionine = 6 AMP + beauvericin + 6 diphosphate + 6 H(+) + 3 S-adenosyl-L-homocysteine Expression is highly repressed by the histone deacetylase HDA1 and the beauvericin cluster-specific repressor BEA4 (PubMed:27750383). BEA biosynthesis is also repressed by the activity of the H3K27 methyltransferase KMT6 (PubMed:27750383). NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, additional domains required for further modifications are also present. Beauvericin synthetase has the C1-A1-T1-C2-A2-MT-T2a-T2b-C3 domain organization (PubMed:28125067). During catalysis, C3 and C2 take turns to incorporate the two biosynthetic precursors into the growing depsipeptide chain that swings between T1 and T2a/T2b with C3 cyclizing the chain when it reaches the full length (By similarity). Leads to complete loss of beauvericin biosynthesis (PubMed:27750383). Belongs to the NRP synthetase family. |
G3GBU7 | MTSLNTKSGTPVIPLLLRSDDASHTDTLVEEVSCSLGLGRDRIENILPSTAFQQDVIDCAGSEKQRSIGHVAYEISNDIDISKLAAAWKDTIHRTPALRTCAFTSSSGETYQVILKDSFVFSWMFSTSADQKDAVTKDEAAAAAYGPRCNRFVLLDDPIEKRKLLIWTFSHALVDTSFQERILERVLKAYTHGHDEVPNRPYTPESSDPEDDDLSLTPTDGSKTPETEGLHPATQYWKNYLSDLNASAFPHLTSPLAVPYPNAKSEHRFTFTASAQSTWPSLAICRTALAILLSRYTHSQEALFGVVTEQHQLLVNGPTRTVVPFRVHCASDQSLSDIIGAVYANDDAIRQFSDVGLRSISSTGDDGVAACGFQTVLSVTEGDNEQSSSCEILQKTGESELFMPCTNRALLLHCQMASDGLSMIARYDKSLIDSQQIARLLRQLGQLIQRLRVSPDELPSAGELDILTSEDQAEIQSWNSHPIPSQPTLIHKEMLKAASLSPSKVAICAWDGEWTYSELDNITSRLAALIRFSTPDQEHAILPIYFEKSKWVVASMLAVMKAGHAFTLIDPNDPPARVAQVVGQTGATVALTSKLYRKKVQGIIERCIIVDDDLVQSLICTCALKPDPTLAKVAPEDLAYVIFTSGSTGDPKGIMIEHRAFSSCALKFGSALGINSDTRALQFGSHAFGACLLEIMTTLIHGGCVCIPSDDDRMNNVPAFVNRANVNWMMATPSYMGTFQPDDVPGLKTLVLVGEQMSPSVNAIWAPRVQLLDGYGQSESSSICFVGKISSSGADPNNIGHSVGAHSWIIDPSDPNRLVPIGGIGELVIESPGIARDYIIPLPTEKSPFFSTVPPWYPFKELPNGIRFYRTGDLARYASDGTVVCLGRMDSQVKIRGQRVELGAVETYLRQQLPEDMSIVVEAIKPSDSPTSSVLVAFLIASEAAESIEDAAILDLAATKAMSVKLEQVLPRHSIPSCYISMQYIPRTATGKVDRRKLRSIGRDMLAQQLQGSSSRPSQSSSPTTSSPSRLEEVWCQCLGLETGAANVGSTFFELGGHSITAIKMVNMARSAGIDLKVSDIYQNPTLAGLEAIVNGSAVPYAIIPTTTRDGPVEQSYSQGRLWFLDQLEVGALWYLIPYAVRMRGMVDIYALSRALMALEQRHETLRTTFEDRDGAGVQIIHQTLFKDLRVVDTTDGNYLQLLKQEQTTPFNLTSEAGWRVLLIRLNDTDYVLSIVMHHIVSDGWSIDVLRHDLSALYAAALQGRDLASAMNPLPIQYSDFAMWQKQEAQALEHEKQLDYWKRQLADCSPAKLPTDFPRPALLSGEAGVVPVSIDGQLYQNLRDFCNENNTTSFAVLLAAFRAAHYRLTGVEDAVIGTPIANRNRWELENIIGFFVNTQCMRITVDDQDTFGSLVRQVRATTTAAFENEDVPFERVVSTMLPGSRDLSRTPLAQLIFAVHSQKDLGRFELQGLESEIVASKAYTRFDIEFHLFQEADGLKGSCNFATDLFKPETVENVVSVFFQILRNGLEKPNIPISVLPLTDGIEELRRLDLLRIKKVEYPRDASLVDIFRTQVAAYPDSLAVVDSSSRLTYTELDRQSDRLAARLRRQGMPAETLVGVLAPRSCEAIVAIIGILKANLAYLPFDVKSPFARLEDILSSIPGQTIVLLGSDVPVPELSIPGLEFMRIVDAIESYDTNDLNGHAHVDDSNPTATSLAYVLFTSGSTGRPKGVMVEHRVIVRLMTSNIIPDFPVQPRSAHMFNIAFDGATYEIFFTLLNGGTLVCIDYMTTLDVKALQDVFIKEQINAACMAPALLKLYLTDARDALRGLDFLMAAGDRFDGQDAIEAQSLVRGQCYNGLLALVSWGELVVTGDGLARGYFDPALNENRFIHIEVDGQRVRAYRTGDRVRYRVGDGLIEFFGRMDTQFKIRGNRIESAEVEAAMLSHGSVRDAAVVVQKDDGEKSDLVGFVVIDHDHSLEGDANDNQVEGWQDHFETEMYADIGDIDPSTIGKDFKGWTSMYDGSEIDKAEMQEWLDDTIKTLCDVQAPGHVLEVGTGSGMILFNLGDGLQSYRGLEPSKSAAAFTNSVIKSVPSLAGKAEVHVGTAQDISQLTNLHPDLVVINSVAQYFPSPEYLAQVADTLVHLSGVKRLFFGDMRTNATNKHFLAARAIRTLGDTATKDSVRQKMAELEEREEELLVEPAFFTTLQDRFPDLVHHVEILPKNMHATNELSAYRYAAVVHIRDHDSVPVHTIEKGSWVDFGASRMNRTSLLQFLRRSKGSSTVAITNIPFAKTVFERQIVESLEAEEDSKLDGAAWTSAVRSDAESRASLSVPDLHRLAEEAGFRLEISVARQWSQSGTLDAVFHHLPSPSNTGRTLIKFPTDNHLRSSATLANRPLQGLQRRRAALQVRERLQSLLPSYMIPSSIVVLDQMPLNPNGKVDRKELARQARIIPKQQTALPVQAVPISDIEAILCDEATATFGMKVDISDDFFKLGGHSLLATKLISRVEQRFNVRASVKDVFDNPVFAHLAVVIREGLASRTTLTNGQDKQGWSARVAPRTETEIILCDEASKLLGIEVGITDNFFDLGGHSMMATKLAMRLGRRLDTTIVVKDIFDYPVLFQLSKKLESAGSGADSEEVHVDDYNPFELLSLEDPKEFIQREICSQLNVSLESIQDMYKSTQMQNSFLFSPGTGSPRPLTPFYIDFPVDSDPPTLVNACHSLVQHIDMFRTVFVLASGQLYQVVLKHLDVPIETIVTNQNVNTATNDFLDEHAQDPIRLGESLIRVAILKQSSSVRVLLRLSHALYDGLSREPIVRNLHILFNGMSLLPPTQFRRYMEYTANSQEKGFEFWRDVIGDSPMTILSDANNGAYRREVSPSKALHLSKVVSVPSQAIRSSIATQATVFNSACALVLSKESGSSNVVFGRIVSGRQGLLVNCQDIIGPCTNAVPVRAHIGTDENHHQMLRDMQDQYLRSLPFETLGFEEIKRNCTDWPDSTTNFACCVTYHNFEYHPESEVEQQRVEMGVLSKHVELRKDEPLYDLAIAGEVEPDGMSLKVTIIARAHLFEEERVQYFLEEVCDTFQTLNFSL | Beauvericin nonribosomal cyclodepsipeptide synthetase; part of the gene cluster that mediates the biosynthesis of beauvericin (BEA), a non-ribosomal cyclic hexadepsipeptide that shows antibiotic, antifungal, insecticidal, and cancer cell antiproliferative and antihaptotactic activity (PubMed:23832252). Ketoisovalerate reductase BEA2 catalyzes the NADPH-specific reduction of ketoisovaleric acid to hydroxyisovalerate, a precursor for beauvericin biosynthesis (PubMed:23832252). The nonribosomal cyclodepsipeptide synthetase BEA1 then catalyzes the formation of beauvericin via condensation and cyclization of 3 dipeptidol monomers, each composed of one unit of hydroxyisovalerate and one unit of N-methyl-phenylalanine (By similarity). 3 (R)-2-hydroxy-3-methylbutyrate + 6 ATP + 3 L-phenylalanine + 3 S-adenosyl-L-methionine = 6 AMP + beauvericin + 6 diphosphate + 6 H(+) + 3 S-adenosyl-L-homocysteine NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, additional domains required for further modifications are also present. Beauvericin synthetase has the C1-A1-T1-C2-A2-MT-T2a-T2b-C3 domain organization (PubMed:23832252). During catalysis, C3 and C2 take turns to incorporate the two biosynthetic precursors into the growing depsipeptide chain that swings between T1 and T2a/T2b with C3 cyclizing the chain when it reaches the full length (By similarity). Impairs the production of beauvericin (PubMed:23832252). Belongs to the NRP synthetase family. |
B6D9A7 | MPSPEHPSWLSTLLADTRPPPKLFAWSPANLDSPTAVKPDRADRGDFDPGKYPVDAPITTASEPVKRIYIVGPGNVGRLYASYMSRQRDALPITLVVHRKELLSQWVTSEGVVLADRGGKVTKNKQFDVEWWTESRPRYGPVREVADGEKLHNVFISTKADAGLGEADRLRRYLGRCSSVVFAQNGVSKLWAPYGPLYVASRYHADDAPSFSACVVNHGISAAGLFYSIHTSPSDAFIGPIFKGSAAPAHGQNKRRRLDDDFFTTYISSTPFLDTKHVSSGQLWIIQLEKLVLNAAINPLTTLLRCKTGQLFASYDSHDALTRVLDQLLWQASAVIQALINHDANIDMLTSYAETVHRLVPGSDDYGRNFANIRRKLTVRFSQPILKAKLYAFGLNIREHRSSMLQDAEAGRKTEIRDVNGWIVDMAEYLGLDLDVGIHRGLIELIEECVVLDKEELARRLL | Ketoisovalerate reductase; part of the gene cluster that mediates the biosynthesis of beauvericin (BEA), a non-ribosomal cyclic hexadepsipeptide that shows antibiotic, antifungal, insecticidal, and cancer cell antiproliferative and antihaptotactic activity (PubMed:18804027, PubMed:19105175, PubMed:27449895). Ketoisovalerate reductase BEA2 catalyzes the NADPH-specific reduction of ketoisovaleric acid to hydroxyisovalerate, a precursor for beauvericin biosynthesis (PubMed:19105175, PubMed:27449895). The nonribosomal cyclodepsipeptide synthetase BEA1 then catalyzes the formation of beauvericin via condensation and cyclization of 3 dipeptidol monomers, each composed of one unit of hydroxyisovalerate and one unit of N-methyl-phenylalanine (PubMed:18804027, PubMed:28534477). (R)-2-hydroxy-3-methylbutyrate + NADP(+) = 3-methyl-2-oxobutanoate + H(+) + NADPH Environmental stimuli such as light and salt stress suppress activity through stimulation of calmodulin (CaM) that binds BEA2 and probably impairs its dimerization. Optimum pH is 7.5. Optimum temperature is 35 degrees Celsius. Homodimer (Probable). Binds to calmodulin in a calcium-independent manner (PubMed:27449895). Impairs the production of both beauvericin and bassianolide. Belongs to the ketopantoate reductase family. |
S0EGG0 | MASQEHPNWLTALLADTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCPSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWAACEGVGLADLTSGKIFLNKRFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLSEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRQPSDDFFIRHIATTPLVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRYKTGELFTSYGSDDPLARVIDKLLWQTSAVIQGLIDHETSHSVITSYAEQMSQPGTSCSVPKVRKKLTERFSQPILKAKLYAFGLKIFEHRSSMLQDIEAGRKTEIRDFNGWIVDTACFLGTGLDVSVHSGLTGLIERCERFDKMELGRALL | Ketoisovalerate reductase; part of the gene cluster that mediates the biosynthesis of beauvericin (BEA), a non-ribosomal cyclic hexadepsipeptide that shows antibiotic, antifungal, insecticidal, and cancer cell antiproliferative and antihaptotactic activity (PubMed:27750383). Ketoisovalerate reductase BEA2 catalyzes the NADPH-specific reduction of ketoisovaleric acid to hydroxyisovalerate, a precursor for beauvericin biosynthesis (By similarity). The nonribosomal cyclodepsipeptide synthetase BEA1 then catalyzes the formation of beauvericin via condensation and cyclization of 3 dipeptidol monomers, each composed of one unit of hydroxyisovalerate and one unit of N-methyl-phenylalanine (By similarity). (R)-2-hydroxy-3-methylbutyrate + NADP(+) = 3-methyl-2-oxobutanoate + H(+) + NADPH Expression is highly repressed by the histone deacetylase HDA1 and the beauvericin cluster-specific repressor BEA4 (PubMed:27750383). BEA biosynthesis is also repressed by the activity of the H3K27 methyltransferase KMT6 (PubMed:27750383). Decreases the production of beauvericin (PubMed:27750383). Belongs to the ketopantoate reductase family. |
G3GBU6 | MTSQEHPNWLTALLVDTRPPPKLFAWSPANIQPKLDEGIDMGSSNSDEEYDNDACVCQSTDSDQRIYIIGPGNIGRLYATHMARHPNALPITLVVHRKELLSQWVACEGVGLADITSGKLFLNKGFTVEWWTETRPPYGPVKEVADGKKLHNVFISTKAEAGLAEADRIRRYLGRCSSVVFAQNGVCKLWPPHGPLYISHRYPSGDTPTFSACVVSHGVASAGPFLSVHAAPADAYIGPVFWASDPESPWRHPSDDFFIRHIATTPHVNTKQVSSGEIWLLQLEKLVMNAAINPLTALLRCKTGELFTSYGSDDPLALVIDKLLWQTSAVIQGLVDHKTSHSVITSYAEHMSQPGTSCSVPKVRKKLMERFSQPILKAKLGWEEDRDTGL | Ketoisovalerate reductase; part of the gene cluster that mediates the biosynthesis of beauvericin (BEA), a non-ribosomal cyclic hexadepsipeptide that shows antibiotic, antifungal, insecticidal, and cancer cell antiproliferative and antihaptotactic activity (PubMed:23832252, PubMed:22916830). Ketoisovalerate reductase BEA2 catalyzes the NADPH-specific reduction of ketoisovaleric acid to hydroxyisovalerate, a precursor for beauvericin biosynthesis (PubMed:23832252, PubMed:22916830). The nonribosomal cyclodepsipeptide synthetase BEA1 then catalyzes the formation of beauvericin via condensation and cyclization of 3 dipeptidol monomers, each composed of one unit of hydroxyisovalerate and one unit of N-methyl-phenylalanine (By similarity). (R)-2-hydroxy-3-methylbutyrate + NADP(+) = 3-methyl-2-oxobutanoate + H(+) + NADPH The reductase activity is increased by Mg(2+) (195%), Ca(2+) (169%) and slightly increased by K(+) (123%) (PubMed:22916830). The reduction activity is inhibited by Fe(2+) and Co(2+), and almost totally inhibited by Cu(2+), Mn(2+), Zn(2+) and Fe(3+) (from 3% to 9% residual activity respectively) (PubMed:22916830). The chelating agent EDTA had little effect, suggesting Mg(2+) and Ca(2+) are not determining factors, though they could promote the reductase enzyme activity (PubMed:22916830). Optimum pH is 7.5. Optimum temperature is 35 degrees Celsius. Belongs to the ketopantoate reductase family. |
S0EGU4 | MGKRTAENSAANGEGEEKHPEIGVDGRPEKEPTFQDYMRVFKYASKWDLLAYTVGVIASIGVGITLPLLNIVFGQFASKFSDYAGTETLPGDEFRSKLSELCLYLLGLFLGRLVLGYITNFAFRMTGVRITSAIRQDYFTALFSQSVHVLDSMPPGYATTIITTTGNTLQLGISEKLGVFVEYNATMIASIIVAFIYSWQLSLVTFTAVVFITFSVSLVLPYITKGQTNQTKSEAMAMSVASEAMSGIRMIVAYGAESRIGSKYGRFVDEAKKHAQFAGPFIALQYGLVFFSSYAAFGLAFWYGTRLLLEDKINQLGAIIVVLFSVMMIVTAMERISTPLLAVSKATVAACEFFTVIDAPRPEPGHLTDPDVSATEDIILEDVTFAYPSRPHVKILDNLNLRIETGKVTAIVGPSGSGKSTIVGLVERWYGLKDQYVISKPVEKPTDKKNNGGKEEDEQELQELSFAGDETGPPVDLHGRISTCGHSLDDINVKWWRSQIGLVQQEPFLFNDTIYSNVLNGLIGTKWENEPDEKKREMVHEACKEAFADEFIEKLPEGYNTAVGEVGIKLSGGQRQRIAIARAIIRRPAILILDEATSAIDVRGERIVQAALDRASKNRTTIVIAHRLSTIKKADRIVVLRQGQVIQSGTHEGLLTDEAGLYYNLVNAQALSLGEQKEGNEVIAKEERPSSVHEKAHTESTIEEKPLEKKPKNKGLLSSFGRFFYETKSNWWMMALTLFFSACAGAAVPFQAWLFAKVIIVFGYLPDESKVRSESSFWSLMWTVLAISAGLAYCATFFLSTRTASTIRAKYQKQYFLYILHQKVAFFDHDDHSQGTMAARSAEDPRQLEELLGSNMASVFIALWTLMGTIAIALAFAWKLALVSLCVVVPILLAAGYWRMRYEIKFEEMNNAVFVDSSKFASEAIGAFRTVASFTLEVAICDQFRTLNSNHVKDAFKKARWVSLLYAFSDSATIGCQAIVLYYGGRLLLSGEYDLESFFVCFMSVLNAGETTGRALSFGPNVAQVRAAANRILGLRDSQVKDGPEATGEQFISHGDGIEIELENIYFKYPTRDVPVFDGLSLTIEKGQFAALVGASGSGKSSIVSLLERFYDPDHGRILCNGQDIATNNVYTYRRHLSLVAQESSLFQGTLRENILLGVEDTVDDAAVHRVCQEASIHEFIMSLPEGYQTQVGSRGVTLSGGQRQRVAIARALMRNPDILLLDEATSSLDSESEKLVQEAFERAGKGRTMVVVAHRLATVQNADVIFVLGEGKLIEKGSHRELLAARGVYWQMCQSQALDK | ABC transporter; part of the gene cluster that mediates the biosynthesis of beauvericin (BEA), a non-ribosomal cyclic hexadepsipeptide that shows antibiotic, antifungal, insecticidal, and cancer cell antiproliferative and antihaptotactic activity (PubMed:27750383). Functions as a regulator of beauvericin production, rather than in BEA transport out of the cell (PubMed:27750383). Beauvericin has low toxicity to the producing fungus and BEA3 does not play a role in detoxification and self-protection of the producing fungus (PubMed:27750383). Expression is highly repressed by the histone deacetylase HDA1 and the beauvericin cluster-specific repressor BEA4 (PubMed:27750383). BEA biosynthesis is also repressed by the activity of the H3K27 methyltransferase KMT6 (PubMed:27750383). Does not affect the production of beauvericin but increases the expression of BEA1 and BEA2 (PubMed:27750383). Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily. |
S0EFU6 | MTDESKRCRTKKVKARTGCSTCKRRKVKCDEQLPGCKRCAKIGVECPGYHKPVKWSVKYERHLVNSSPTAGNSFSCFDSGAGNLSNLMQPKSNPGSVETQNHNDNEVQAPGPLTRGSSSSLSDAREHLEDTLEMQPPSTLNSEQLSTLCDDVQADEEFPCALNALHDDSLCLTSYIPTLQTSLILDHYFTTVCHFNSSFDSANNPFRSEVSRMMADSPLLFGCVLSMSAAHLYQGDKSSSCIPLEFQTEAMSHLSRTLSELPTRNECEVDDNRPMALVSREKILNVSDDLLLSIIFLGMTAAWHDVSATGLPHLHGSRQLFRSWISLNNLTDIEKRRKMTRTQIFVVSSMVYWEAMSSALFDQQYEGLSHLTMFCDPHPPALVQPCPWTGVATPIFVFLAKTLTLVRNNQALKSLWVFESGEIHRRALYGELLAKANSLEREILRYRLPSLALIEDIGDPCTTPDHLLAISRCYRMAALLELYSAFPEITRTGGRPDSAIDLDRGDEKTHLIMGLAFSILEILEKIPDDSGTISIQLLSLLIAGSVLGPVPPRGEDEGPKRLETLRLRTFVRQRIHKMYAAVRLGPIGNAMAILEEVWARMDMLPAIQNANSAISSFHWINIMSQKKLETMFG | Transcription factor that specifically represses the expression of the gene cluster involved in the biosynthesis of beauvericin (BEA), a non-ribosomal cyclic hexadepsipeptide that shows antibiotic, antifungal, insecticidal, and cancer cell antiproliferative and antihaptotactic activity (PubMed:27750383). Leads to elevated expression of BEA1, BEA2 and BEA3 (PubMed:27750383). |
A0A0C6DUU3 | MMDLFKTDIMPDLQSSMMASIGSNWRFALFVAATLLTSYIVIVRPLKNVLFHPLRKYPGPKLFAGSSIPYGFWYMTGKWHTKIRQLHATYGPVVRIGPDELSYACPEAWEDIYGRYVPAKRKENPKPVWYCSPDAHDMVGASLGDHGRMRRVMTPGFTYSAMCKQEPLIKVHVDLFLEKLRGVCDDGNATVNMLEWFTYCTFDLIGDLSFGEPFGCLENSMLHPWLQLVFANIYVTHIILLCKRIPFFYLFLPIKTTLQLYRDFNRHVILLRQVVERRLSLTTPRNDFLDIMTSKKTSTLYLTNEEIFKNAILLTGGGAETTSSSLTGMAFILTTRPDVKKRIVEELHATFPNEEAINMRSVAQLTYTGAFIEEAMRYYPPGPNTMWRTTPAGGNTILGDYIPENTIIGIPHRVLYRSEAYWKHADEIHPERWLPDGQRPAEFDHDRREGFQPFSYGPRACIAMNLAYAEMRYILARFLWNFDIQETEQSKHWMDNQKAYLVWDKPGLFVRLKPVAKEEAQ | Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of betaenones, phytotoxic polyketides involved in leaf spot disease in sugar beets (PubMed:25530455). The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase bet1 and the enoyl reductase bet3 via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations (PubMed:25530455). The C-terminal reductase (R) domain of bet1 catalyzes the reductive release of the polyketide chain (PubMed:25530455). Because bet1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase bet3 (PubMed:25530455). The short-chain dehydrogenase/reductase bet4 then catalyzes reduction of dehydroprobetaenone I to probetaenone I (PubMed:25530455). The cytochrome P450 monooxygenase bet2 catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I (PubMed:25530455). The FAD-linked oxidoreductase (orf1) is probably responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A (By similarity). dehydroprobetaenone I + H(+) + NADPH + O2 = epoxybetaenone + H2O + NADP(+) dehydroprobetaenone I + 3 H(+) + 3 NADPH + 3 O2 = betaenone C + 3 H2O + 3 NADP(+) Mycotoxin biosynthesis. Belongs to the cytochrome P450 family. |
A0A0C6DWS6 | MPPTNGQTAIIQSKTCPTPTTLPLVVAHGRPLPPLPSSHHVRVRVLAVGLNPTDHKMVTHFFMQDNTTGCDFCGIIEEVGSASALPLGLRVCGADFPYRPSNPYNGAFAEYAVADSRHLLQIPDAISNIQAAAIGAIGWGTAALAMSDPTALNLPGTPSKPDARSLPVLVYGGATATGIIAIQMLKRSGYIPIAVCSAQSAPLCISLGAVGTACYTSTTCVQDIKALANGQSIKHALDCITDPESTTVCLASLARIGGRYACLEAVSDACITRRSVAVKVVMGFEGQNFDVDLGHPVYSRKANPALHAVAAQWAAELQPLLNAGIIKTQPLEEIEGRFEGVIKALEMLQGGHIKGKKLVVNISS | Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of betaenones, phytotoxic polyketides involved in leaf spot disease in sugar beets (PubMed:25530455). The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase bet1 and the enoyl reductase bet3 via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations (PubMed:25530455). The C-terminal reductase (R) domain of bet1 catalyzes the reductive release of the polyketide chain (PubMed:25530455). Because bet1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase bet3 (PubMed:25530455). The short-chain dehydrogenase/reductase bet4 then catalyzes reduction of dehydroprobetaenone I to probetaenone I (PubMed:25530455). The cytochrome P450 monooxygenase bet2 catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I (PubMed:25530455). The FAD-linked oxidoreductase (orf1) is probably responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A (By similarity). acetyl-CoA + 10 AH2 + 2 H(+) + 7 malonyl-CoA + 5 S-adenosyl-L-methionine = 10 A + 7 CO2 + 8 CoA + dehydroprobetaenone I + 6 H2O + 5 S-adenosyl-L-homocysteine Mycotoxin biosynthesis. Monomer. Belongs to the zinc-containing alcohol dehydrogenase family. |
Q9P6P5 | MSKSKIGEDVYKKVDKVNAELFVLTYGSIVAQLCKDMNYEKVNEELDKMGYNIGIRLIEDFLAKTEWPRCADFRETGETVAKVGFKVFLNFSPIISSVSDDGNTFVLTLDDNPLAEFVELPADARQKLWYSNILCGVIRGALEMLQMDVDAVFLRDILRGDEHTEIRVHLKRILKEEIPPGDE | Belongs to the TRAPP small subunits family. BET3 subfamily. |
D6VXC9 | MVSTTQSRSLKAMGEEIWKNKTEKINTELFTLTYGSIVAQLCQDYERDFNKVNDHLYSMGYNIGCRLIEDFLARTALPRCENLVKTSEVLSKCAFKIFLNITPNITNWSHNKDTFSLILDENPLADFVELPMDAMKSLWYSNILCGVLKGSLEMVQLDCDVWFVSDILRGDSQTEIKVKLNRILKDEIPIGED | Component of the TRAPP I, TRAPP II and TRAPP III complexes which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation. Required for sporulation. Has a role late in meiosis following DNA replication. Part of the multisubunit TRAPP (transport protein particle) I complex composed of BET3, BET5, TRS20, TRS23, TRS31 and TRS33. Part of the multisubunit TRAPP (transport protein particle) II complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65, TRS85, TRS120 and TRS130. Part of the multisubunit TRAPP (transport protein particle) III complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33 and TRS85. Present with 2370 molecules/cell in log phase SD medium. Belongs to the TRAPP small subunits family. BET3 subfamily. |
A0A0C6DRT7 | MTPAKAPSHAKKPEAGSQPISSMWTQMFPPKPTYTEEHMPDLSGKIYIVTGASSGVGKETSRMLYSKNAKVYMAMRSGAKAAAAMADIQRAVPKSSGALVILPLDLADLSAVKKAAEEFVSLESSLHGLINNAGVQVLDDTNGEARTAQGHEIHIGVNVLGPFLFTQLLRGVLAATAGRAQPDTVRIVWVSSMGTETIGEKGRGLSADYVDYWPLMSPLERYGLSKAGNWLQGAECAKRYAGDGILSFPINPGHLKSELYREGGTLFKLALRPVLFPPAYGSYVELFAALSPTLSTKDSGAWIVPWGRLYPIRSDLLDATKSAAEGGNGHASAFWDWCEEQVKAFL | Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of betaenones, phytotoxic polyketides involved in leaf spot disease in sugar beets (PubMed:25530455). The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase bet1 and the enoyl reductase bet3 via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations (PubMed:25530455). The C-terminal reductase (R) domain of bet1 catalyzes the reductive release of the polyketide chain (PubMed:25530455). Because bet1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase bet3 (PubMed:25530455). The short-chain dehydrogenase/reductase bet4 then catalyzes reduction of dehydroprobetaenone I to probetaenone I (PubMed:25530455). The cytochrome P450 monooxygenase bet2 catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I (PubMed:25530455). The FAD-linked oxidoreductase (orf1) is probably responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A (By similarity). AH2 + dehydroprobetaenone I = A + probetaenone I Mycotoxin biosynthesis. Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
A0A0C6E5D0 | MKSFATTVLLVTPGIYAAALSGRQGQAINSSCKVIPGDTAWPSRQIWSQLNDTLDGRLIQSTPQAAVCRPGGYGSISENGTECTTLKEDWDYAKAFLDSAVEIMNPWYQNTSCSPFYRVDQPCTLGNYVSYAIPVSGPEDVVTAINFTQTHNVRLVIKNTGHDYLGKSTGTGGLSLWTHNLQSKQIVNYTSPAYSGPAIKVGAGVTGGEALLHASQFGYRLVSGDCSTVGYAGGYSSGGGHSLLNSVHGMAADNVLEWEVVTADGRHLVASATQNSDLYWALSGGGAGNLAVVLSMTAKVHPDGLVGAATLSFNATSSPSNTSYISAINAWWTFLPTLIDAGASPSFNIYTNNFLIYNTTAPGKSAQDMSTLYAPYLSTLSSLSIPYTFQTYTAPSFLQHYNATDGPLPYGPYVASQLFNSRMIPRSLSSSPSNLTTAILSSVATDAPGIWQLGCLGINVNSTRISHPDNAVAPHWRTAMAVCLEFSLYDWAIPEEEMVARRQHLADVIHPAIVKVTPGSGAYLNEADPLVYPVGEDGWKDAFYGANYERLRGLKREWDPERVFYAYTAPGSEEWVSDAEGRLCRV | FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of betaenones, phytotoxic polyketides involved in leaf spot disease in sugar beets (PubMed:25530455). The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase bet1 and the enoyl reductase bet3 via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations (PubMed:25530455). The C-terminal reductase (R) domain of bet1 catalyzes the reductive release of the polyketide chain (PubMed:25530455). Because bet1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase bet3 (PubMed:25530455). The short-chain dehydrogenase/reductase bet4 then catalyzes reduction of dehydroprobetaenone I to probetaenone I (PubMed:25530455). The cytochrome P450 monooxygenase bet2 catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I (PubMed:25530455). The FAD-linked oxidoreductase (orf1) is probably responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A (By similarity). betaenone C = betaenone A Mycotoxin biosynthesis. Belongs to the oxygen-dependent FAD-linked oxidoreductase family. |
Q9P6L1 | MTIYAFYIYSRKCECVFAHRWKPSDRNSMETLVSQLEQNSIEDDMEKLIFGVVFSLRNMVKKITADQDQFMSYTTSKYKLHFYETPTNLRLIFITNPKIDSLTHVLQQIYTTLYVEFVVKHPLYTHVPPSAEEGGINCEIFRITLDRFVRTLSCF | May play a role in vesicular transport from endoplasmic reticulum to Golgi. Part of the multisubunit TRAPP (transport protein particle) complex composed of bet3, bet5, trs20, trs23, trs31, trs33, trs65, trs85, trs120 and trs130. Belongs to the TRAPP small subunits family. BET5 subfamily. |
D6W0K6 | MGIYSFWIFDRHCNCIFDREWTLASNSASGTINSKQNEEDAKLLYGMIFSLRSITQKLSKGSVKNDIRSISTGKYRVHTYCTASGLWFVLLSDFKQQSYTQVLQYIYSHIYVKYVSNNLLSPYDFAENENEMRGQGTRKITNRNFISVLESFLAPMVNQ | Component of the TRAPP I, TRAPP II and TRAPP III complexes which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation. Required for sporulation. Has a role late in meiosis following DNA replication. Part of the multisubunit TRAPP (transport protein particle) I complex composed of BET3, BET5, TRS20, TRS23, TRS31 and TRS33. Part of the multisubunit TRAPP (transport protein particle) II complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65, TRS85, TRS120 and TRS130. Part of the multisubunit TRAPP (transport protein particle) III complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33 and TRS85. Belongs to the TRAPP small subunits family. BET5 subfamily. |
P85983 | VQGMVYCDTCRSANALGFMR | Causes an allergic reaction in human. Binds to IgE. On the 2D-gel the determined pI of this protein is: 5.3, its MW is: 17 kDa. Belongs to the Ole e I family. |
Q1QXE1 | MTQAREYDYIIIGAGSAGNVLATRLTEDPDVQVLLLEAGGPDYRFDFRTQMPAALAYPLQGKRYNWAFETDPEPYMNNRRMECGRGKGLGGSSLINGMCYLRGNALDYDNWAKIPGLEDWNYLQCLPYFKRAETRDIGPNDYHGGDGPVSVATPKEGNNELYGAFIRAGIEAGYPATEDVNGYQQEGFGPMDRTTTPNGRRASTARGYLDIAKQRPNLTIETHATTDVIEFEGKRAVGVSYERKGQAQRVRARREVLLCAGAIASPQILQRSGVGNPEHLEEFDIPVVHELPGVGENLQDHLEMYIQYECKKPISLYPALKWYNQPKIGAEWLFFGKGIGASNQFEAAGFIRTNDQEEWPNLQYHFLPIAISYNGKSAVQAHGFQAHVGSMRSMSRGRIRLTSRDPKAAPSILFNYMSHDKDWQEFRDAIRITREIIEQPTMDEYRGREISPGPNVQSDAELDEFVRQHAETAYHPAGSCKMGSADDAMAVVDGAGRVHGLEGLRVIDASIMPVIATGNLNAPTIMIAEKMADKVRGRDPLPPAKVDYYVANGAPARRRA | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
Q9L4K0 | MSQATEFDYIIIGAGSAGNVLATRLTEDSDVSVLLLEAGGPDYRFDFRTQMPAALAYPLQGKRYNWAFETDPEPHMDNRRMECGRGKGLGGSSLINGMCYIRGNALDYDHWAKQPGLEEWDYLSCLPYFKKSETRDIGPNDYHGGDGPVSVTTPKAGNNPLYRTFIEAGKQAGYPETEDVNGYQQEGFGPMDRFVTPKGRRASTARGYLDTAKQRSNLTIETRAVTDVIEFEGKRAVGVRYEQKGQPKQARARREVLLCGGAIASPQILQRSGVGNPEWLKELGIPVVHELPGVGENLQDHLEMYIQYECKEPISLYPALKWYNQPKIGAEWLFKGTGVGASNQFESCGFIRSRDDEEWPNLQYHFLPIAISYNGKSAVQAHGFQAHVGSMRSESRGRIRLTSKDPHAAPSILFNYMAKEKDWEEFRDAIRLTREIIAQPAFDRYRGREISPGPDVQSDEELDNFVKQHAETAYHPCGSCRMGEGDMAVTDAQGRVHGLEGLRVVDASLFPVIPTGNLNAPTIMLAEKIADRIRGREPLPRASVDYYVANGAPAKQAS | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
Q6FDF9 | MTTQTFDYIIIGAGSAGNVLAARLTEDADVSVLLLEAGGPDYRLDFRTQMPAALAYPLQGRRYNWAYLTEPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDLEGWSKLKGLENWTYADCLPYYKKAETRDIGGNDYHGDHGPVSVATPKDNNNVLFHAMVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTKNGRRSSTARGYLDMAKERPNLTIITHAMTNKILFNGKQAIGVEYIQGADKRDLKKVMANKEVLLCAGAIASPQILQRSGVGESTFLKSMDIDVVHDLPGVGENLQDHLEMYLQYKCKQPVSLYPALKWYNQPAIGAEWLFLGKGIGASNQFEAGGFIRSSDEFEWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGHIKLKSKDPFEHPSILFNYMSTEQDWQEFRAAIRITREIMHQPALDPYRGEEISPGKQLSTDTQLDDFVRNHAETAYHPSCSCKMGEDDMAVVDHQGRVHGLQGLRVVDASIMPLIITGNLNATTIMMAEKIADQIRERAPLPRSDAPFYVASA | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
B7GYG5 | MNIKEYDYIIIGAGSAGNVLAARLTEDKDTTVLLLEAGGPDYRLDFRTQMPAALAYPLQGRRYNWAYLTDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDLEQWATHKGLENWTYADCLPYYKKAETRDIGGNDYHGDSGPVSVATPKNGNNVLFHAMVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRSSTARGYLDMAKGRPNLTILTHATTNKILFNQKQAIGVEYIIGADQNNLQRALVKREVLLCAGAIASPQILQRSGVGQSTFLKSMDIDVVHDLPGVGENLQDHLEMYLQYKCKQPVSLYPALKWYNQPAIGAEWLFNGTGIGASNQFEAGGFIRSSDEFKWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIKLKSKDPFAHPSILFNYMSTEQDWREFRDAIRITREIMHQPALDPYRGDEISPGKHLQTDAELDDFVRNHAETAYHPSCSCKMGEDEMAVVDGQGRVHGMNGLRVVDASIMPLIITGNLNATTIMIAEKIADQIRGREALPRSTAPFYVAS | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
B7I895 | MNIKEYDYIIIGAGSAGNVLAARLTEDKDTTVLLLEAGGPDYRLDFRTQMPAALAYPLQGRRYNWAYLTDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDLEQWATHKGLENWTYADCLPYYKKAETRDIGGNDYHGDSGPVSVATPKNGNNVLFHAMVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRSSTARGYLDMAKGRPNLTILTHATTNKILFNQKQAIGVEYIIGADQNNLQRALVKREVLLCAGAIASPQILQRSGVGQSTFLKSMDIDVVHDLPGVGENLQDHLEMYLQYKCKQPVSLYPALKWYNQPAIGAEWLFNGTGIGASNQFEAGGFIRSSDEFKWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIKLKSKDPFAHPSILFNYMSTEQDWREFRDAIRITREIMHQPALDPYRGDEISPGKHLQTDAELDDFVRNHAETAYHPSCSCKMGEDEMAVVDGQGRVHGMNGLRVVDASIMPLIITGNLNATTIMIAEKIADQIRGREALPRSTAPFYVAS | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
B2HV79 | MNIKEYDYIIIGAGSAGNVLAARLTEDKDTTVLLLEAGGPDYRLDFRTQMPAALAYPLQGRRYNWAYLTDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDLEQWATHKGLENWTYADCLPYYKKAETRDIGGNDYHGDSGPVSVATPKNGNNVLFHAMVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRSSTARGYLDMAKGRPNLTILTHATTNKILFNQKQAIGVEYIIGADQNNLQRALVKREVLLCAGAIASPQILQRSGVGQSTFLKSMDIDVVHDLPGVGENLQDHLEMYLQYKCKQPVSLYPALKWYNQPAIGAEWLFNGTGIGASNQFEAGGFIRSSDEFKWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIKLKSKDPFAHPSILFNYMSTEQDWREFRDAIRITREIMHQPALDPYRGDEISPGKHLQTDAELDDFVRNHAETAYHPSCSCKMGEDEMAVVDGQGRVHGMNGLRVVDASIMPLIITGNLNATTIMIAEKIADQIRGREALPRSTAPFYVAS | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
B0VST3 | MNIKEYDYIIIGAGSAGNVLAARLTEDKDTTVLLLEAGGPDYRLDFRTQMPAALAYPLQGRRYNWAYLTDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDLEQWATHKGLENWTYADCLPYYKKAETRDIGGNDYHGDSGPVSVATPKNGNNVLFHAMVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRSSTARGYLDMAKGRPNLTILTHATTNKILFNQKQAIGVEYIIGADQNNLQRALVKREVLLCAGAIASPQILQRSGVGQSTFLKSMDIDVVHDLPGVGENLQDHLEMYLQYKCKQPVSLYPALKWYNQPAIGAEWLFNGTGIGASNQFEAGGFIRSSDEFKWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIKLKSKDPFAHPSILFNYMSTEQDWREFRDAIRITREIMHQPALDPYRGDEISPGKHLQTDAELDDFVRNHAETAYHPSCSCKMGEDEMAVVDGQGRVHGMNGLRVVDASIMPLIITGNLNATTIMIAEKIADQIRGREALPRSTAPFYVAS | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
B0V945 | MNIKEYDYIIIGAGSAGNVLAARLTEDKDTTVLLLEAGGPDYRLDFRTQMPAALAYPLQGRRYNWAYLTDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDLEQWATHKGLENWTYADCLPYYKKAETRDIGGNDYHGDSGPVSVATPKNGNNVLFHAMVEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRSSTARGYLDMAKGRPNLTILTHATTNKILFNQKQAIGVEYIIGADQNNLQRALVKREVLLCAGAIASPQILQRSGVGQSTFLKSMDIDVVHDLPGVGENLQDHLEMYLQYKCKQPVSLYPALKWYNQPAIGAEWLFNGTGIGASNQFEAGGFIRSSDEFKWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIKLKSKDPFAHPSILFNYMSTEQDWREFRDAIRITREIMHQPALDPYRGDEISPGKHLQTDAELDDFVRNHAETAYHPSCSCKMGEDEMAVVDGQGRVHGMNGLRVVDASIMPLIITGNLNATTIMIAEKIADQIRGREALPRSTAPFYVAS | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
Q8UH55 | MQADYVIVGSGSAGSAIAYRLSEDGRYSVIVIEAGGSDFGPFIQMPAALAWPMSMKRYNWGYLSEPEPNLDNRRITAPRGKVIGGSSSINGLVYVRGHAEDFNRWEELGAQGWAYADVLPYFKRMEHSHGGEEGWRGTDGPLHVQRGPVSNPLFHAFIQAGAQAGFELTDDYNGSKQEGFGLMEQTIHNGRRWSAANAYLKPALKRGNVTLVNGFARKVIIENGRAVGVEIERRGRVETVKANREVIVSASSFNSPKLLMLSGIGPAAHLKDMGIEVKADRPGVGANLQDHMEFYFQQVSTKPVSLYSWLPWFWQGVAGAQWLLSKGGLGASNQFEACAFLRSAPGLKQPDIQYHFLPVAISYDGKAAAKSHGFQAHVGYNLSKSRGNVTLRSADPHDDPVIRFNYMSHPEDWEKFRHCVRLTREIFGQKAFDDFRGPEIQPGENIETDEQIDAFLREHLESAYHPCGTCRMGDRNDPMAVVDPECRVIGVEGLRVADSSIFPHVTYGNLNGPSIMTGEKAADHILGKTPLPRSNQEPWVNPRAAVSDR | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
B9JBA2 | MQADFVIIGSGSAGSAMASRLSEDGKHTVIVLEFGGSDVGPFIQMPAALAWPMSMDRYNWGYLSEPEPQLNNRRITAPRGKVIGGSSSINGMVYVRGHAEDFNRWEELGAQGWAYADVLPYFKRMEHSHGGEEGWRGTDGPLHVRRGDARNPLFHAFIEAGKQAGFEATEDYNGGKQEGFGLMEQTTWMGRRWSAATAYLKPALKRPNVELIRCFARKVVIENGRATGVEIERGGKIEIVKANSEVIVSASSFNSPKLLMLSGIGPGQHLQEMGIEVKIDRPGVGANLQDHMEFYFQQTSLKPVSLYSWLPWYMQGIVGAQWMFFKSGLGTSNQFEACAFLRSAPGVKQPDIQYHFLPVAISYDGKAAAKSHGFQAHVGYNLSKSRGAVTLRSSDPKADPVIRFNYMSHPEDWEKFRHCVRLTREIFGQKAFDDYRGPEIQPGPDVQTDDQIDAFLREHLESAYHPCGTCKMGSKDDPMAVVDPDTRVIGVEGLRVADSSIFPSLTYGNLNGPSIMTGEKAADHILGKPRLARSNQEPWINPRWEVSDR | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
A6X2G7 | MEADFVIIGSGSAGSAMAYRLSEDGRYSVIVIEYGVPDVGPLIQMPAALSFPMNMETYDWGFSTEPEPHIGGRSLVTPRGKVLGGSSSINGMVYVRGHARDYDHWSESGARGWAYADVLPYFKRMENSSGGQEGWRGTNGPLYIQRGKRDNPLFHAFVEAGHEAGFEVTEDYNGEKQEGFGPMEQTIHNGRRWSAANAYLKPALKRPNVKLVKGLARKIVLEGKRAVGVEIEAGRSFSTIRARREVIIAASSINSPKLLMLSGIGPAAQLKEHGIEVVADRPGVGQNLQDHLEVYIQQECTQPITLYSKLNLFSKAKIGAEWLFFKTGDGATNHFESAAFLRSKAGVEYPDIQYHFLPVAIRYDGKAAAQSHGFQAHVGPMRSKSRGSVTLRSANPREKPVIKFNYMSHEDDWADFRHCVRLTREIFGQAAFNPYRGAEIQPGAHVQSDDEIDNFIKEHVESAFHPCGTCKMGAVDDPMAVVDAECRVIGVEGLRVADSSIFPRITNGNLNGPSIMVGEKASDHILGRTPLARSDQEPWINPRWQVSDR | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
A7FKL6 | MEYDYIIIGAGSAGNVLAARLTEDADVTVLLLEAGGPDYRLDFRTQMPAALAFPLQGKRYNWAYETDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDFDHWASLSGLEDWSYLDCLPYFRKAETRDIGPNDFHGGEGPVNVTTPKIGNNPLFHAMVAAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRASTARGYLDQARPRNNLTIITHALTDRILFEGKRATGVRYLKGDAGTGQTAYARREVLLCGGAIASPQILQRSGIGPAELLQRLDIPLVQALPGVGENLQDHLEMYLQYSCKQPVSLYPALLWFNQPKIGIEWLFNGTGVGASNQFEAGGFIRSRDAFTWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIQVKSKDPRQHPSILFNYMSSEQDWHEFRDAIRITREIIAQPALDPYRGREISPGANVQNDDELDAFIREHAETAYHPSCSCKMGDDKMAVVDGQGRVHGVQGLRVVDASIMPQIITGNLNATTIMIAEKIADRIRGCQPLAKSNAAYFIAGDTPARTSPVRHSLPVTSYP | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
Q1C932 | MEYDYIIIGAGSAGNVLAARLTEDADVTVLLLEAGGPDYRLDFRTQMPAALAFPLQGKRYNWAYETDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDFDHWASLSGLEDWSYLDCLPYFRKAETRDIGPNDFHGGEGPVSVTTPKIGNNPLFHAMVAAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRASTARGYLDQARPRNNLTIITHALTDRILFEGKRATGVRYLKGDAGTGQTAYARREVLLCGGAIASPQILQRSGIGPAELLQRLDIPLVQALPGVGENLQDHLEMYLQYSCKQPVSLYPALLWFNQPKIGIEWLFNGTGVGASNQFEAGGFIRSRDAFTWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIQVKSKDPRQHPSILFNYMSSEQDWHEFRDAIRITREIIAQPALDPYRGREISPGANVQNDDELDAFIREHAETAYHPSCSCKMGDDKMAVVDGQGRVHGVQGLRVVDASIMPQIITGNLNATTIMIAEKIADRIRGCQPLAKSNAAYFIAGDTPARTSPVRHSLPVTSYP | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
B2K8U4 | MEYDYIIIGAGSAGNVLAARLTEDADVTVLLLEAGGPDYRLDFRTQMPAALAFPLQGKRYNWAYETDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDFDHWASLSGLEDWSYLDCLPYFRKAETRDVGPNDFHGGEGPVSVTTPKIDNNPLFHAMVAAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRASTARGYLDQARPRNNLTIITHALTDRILFEGKRATGVSYLKGDAGTGQTAHARREVLLCGGAIASPQILQRSGIGPAELLQRLDIPLVQALPGVGENLQDHLEMYLQYSCKQPVSLYPALLWFNQPKIGIEWLFNGTGVGASNQFEAGGFIRSRDAFTWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIQVKSKDPRQHPSILFNYMSNEQDWHEFRDAIRITREIIAQPALDPYRGREISPGANVQSDDELDAFIREHAETAYHPSCSCKMGDDKMAVVDGQGRVHGVQGLRVVDASIMPQIITGNLNATTIMIAEKIADRIRGCQPLAKSNAAYFIAGDTPARTSPVRHSLPVTSYP | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
Q0WHN4 | MEYDYIIIGAGSAGNVLAARLTEDADVTVLLLEAGGPDYRLDFRTQMPAALAFPLQGKRYNWAYETDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDFDHWASLSGLEDWSYLDCLPYFRKAETRDIGPNDFHGGEGPVSVTTPKIGNNPLFHAMVAAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRASTARGYLDQARPRNNLTIITHALTDRILFEGKRATGVRYLKGDAGTGQTAYARREVLLCGGAIASPQILQRSGIGPAELLQRLDIPLVQALPGVGENLQDHLEMYLQYSCKQPVSLYPALLWFNQPKIGIEWLFNGTGVGASNQFEAGGFIRSRDAFTWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIQVKSKDPRQHPSILFNYMSSEQDWHEFRDAIRITREIIAQPALDPYRGREISPGANVQNDDELDAFIREHAETAYHPSCSCKMGDDKMAVVDGQGRVHGVQGLRVVDASIMPQIITGNLNATTIMIAEKIADRIRGCQPLAKSNAAYFIAGDTPARTSPVRHSLPVTSYP | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
C4GWK6 | MEYDYIIIGAGSAGNVLAARLTEDADVTVLLLEAGGPDYRLDFRTQMPAALAFPLQGKRYNWAYETDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDFDHWASLSGLEDWSYLDCLPYFRKAETRDIGPNDFHGGEGPVSVTTPKIGNNPLFHAMVAAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRASTARGYLDQARPRNNLTIITHALTDRILFEGKRATGVRYLKGDAGTGQTAYARREVLLCGGAIASPQILQRSGIGPAELLQRLDIPLVQALPGVGENLQDHLEMYLQYSCKQPVSLYPALLWFNQPKIGIEWLFNGTGVGASNQFEAGGFIRSRDAFTWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIQVKSKDPRQHPSILFNYMSSEQDWHEFRDAIRITREIIAQPALDPYRGREISPGANVQNDDELDAFIREHAETAYHPSCSCKMGDDKMAVVDGQGRVHGVQGLRVVDASIMPQIITGNLNATTIMIAEKIADRIRGCQPLAKSNAAYFIAGDTPARTSPVRHSLPVTSYP | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
A4TNP2 | MEYDYIIIGAGSAGNVLAARLTEDADVTVLLLEAGGPDYRLDFRTQMPAALAFPLQGKRYNWAYETDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDFDHWASLSGLEDWSYLDCLPYFRKAETRDIGPNDFHGGEGPVSVTTPKIGNNPLFHAMVAAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRASTARGYLDQARPRNNLTIITHALTDRILFEGKRATGVRYLKGDAGTGQTAYARREVLLCGGAIASPQILQRSGIGPAELLQRLDIPLVQALPGVGENLQDHLEMYLQYSCKQPVSLYPALLWFNQPKIGIEWLFNGTGVGASNQFEAGGFIRSRDAFTWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIQVKSKDPRQHPSILFNYMSSEQDWHEFRDAIRITREIIAQPALDPYRGREISPGANVQNDDELDAFIREHAETAYHPSCSCKMGDDKMAVVDGQGRVHGVQGLRVVDASIMSQIITGNLNATTIMIAEKIADRIRGCQPLAKSNAAYFIAGDTPARTSPVRHSLPVTSYP | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
Q66D54 | MEYDYIIIGAGSAGNVLAARLTEDADVTVLLLEAGGPDYRLDFRTQMPAALAFPLQGKRYNWAYETDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDFDHWASLSGLEDWSYLDCLPYFRKAETRDVGPNDFHGGEGPVSVTTPKIDNNPLFHAMVAAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRASTARGYLDQARPRNNLTIITHALTDRILFEGKRATGVSYLKGDAGTGQTAHARREVLLCGGAIASPQILQRSGIGPAELLQRLDIPLVQALPGVGENLQDHLEMYLQYSCKQPVSLYPALLWFNQPKIGIEWLFNGTGVGASNQFEAGGFIRSRDAFTWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIQVKSKDPRQHPSILFNYMSNEQDWHEFRDAIRITREIIAQPALDPYRGREISPGANVQSDDELDAFIREHAETAYHPSCSCKMGDDKMAVVDGQGRVHGVQGLRVVDASIMPQIITGNLNATTIMIAEKIADRIRGCQPLAKSNAAYFIAGDTPARTSPVRHSLPVTSYP | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
B1JSR0 | MEYDYIIIGAGSAGNVLAARLTEDADVTVLLLEAGGPDYRLDFRTQMPAALAFPLQGKRYNWAYETDPEPHMNNRRMECGRGKGLGGSSLINGMCYIRGNAMDFDHWASLSGLEDWSYLDCLPYFRKAETRDIGPNDFHGGEGPVNVTTPKIGNNPLFHAMVAAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPKGRRASTARGYLDQARPRNNLTIITHALTDRILFEGKRATGVRYLKGDAGTGQTAYARREVLLCGGAIASPQILQRSGIGPAELLQRLDIPLVQALPGVGENLQDHLEMYLQYSCKQPVSLYPALLWFNQPKIGIEWLFNGTGVGASNQFEAGGFIRSRDAFTWPNIQYHFLPVAINYNGSNAVKEHGFQAHVGSMRSPSRGRIQVKSKDPRQHPSILFNYMSSEQDWHEFRDAIRITREIIAQPALDPYRGREISPGANVQNDDELDAFIREHAETAYHPSCSCKMGDDKMAVVDGQGRVHGVQGLRVVDASIMPQIITGNLNATTIMIAEKIADRIRGCQPLAKSNAAYFIAGDTPARTSPVRHSLPVTSYP | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Belongs to the GMC oxidoreductase family. |
P54222 | MRAQPKASHFIDGEYVEDAAGTVIESIYPATGEIIARLHAATPGIVEKAIAAAKRAQPEWAAMSPTARGRILKRAAELMRQRNRELSELETLDTGKPIQETIVADPTSGADSFEFFGGVAPAALNGDYIPLGGDFAYTKRVPLGVCVGIGAWNYPQQIACWKGAPALVAGNAMVFKPSENTPLGALKIAEILIEAGLPKGLFNVIQGDRATGPLLVNHPDVAKVSLTGSVPTGKKVAGAAAAELKHVTMELGGKSPLIVFDDADLESAIGGAMLGNFYSTGQVCSNGTRVFVQRKIKEPFLARLKERTEAIVIGDPLDEATQLGPMVSAAQRDKVFSYIGKGKAEGARLVTGGGIPNNVSGEGTYIQPTVFADVTDGMTIAREEIFGPVMCVLDFDDEVEVIARANATEFGLSAGVFTADLTRAHRVADRLEAGTLWINTYNLCPVEIPFGGSKQSGFGRENSVAALNHYTELKTVYVGMGPVEAPY | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Binds 2 potassium ions per subunit. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. Belongs to the aldehyde dehydrogenase family. |
Q92YD2 | MATPLCQPAASHFIDGTFIEDRTGPEILSVNPVDGEIIAKLHGATSCIIEKAIASAKRAQKEWARKEPAERGRVLSRAADIMRARNRELSVLETRDTGKPISETLVADAASGADCLEYFGAIAATLSGDSIQFGEDWVYTRREPLGVCLGIGAWNYPIQIAAWKAAPALACGNAMIFKPSEVTPLSALKLAEILTEAGLPPGVFNIVQGAGDVGAELATHPAIAKVSLTGSVKTGARVASAAMAGIRPVTMELGGKSALIVFDDADVEAAVSGAILGNFYSAGQICSNGTRVFLQRGIREAFLARLLARVAALKIGDPMDEETDIGPLVSAAHRNRVATYVARAEVEGAYQMAPPRKLPPGDAWHEPVVFTNVTDWMTLAREEVFGPVMAVLDFDDEQDVVARANATDFGLAAGIFTRDLVRAHRLAAELEAGTVWINAYNLTPAGMAFGGIKRSGIGRENGRVAIDHYTQLKSVFVSMQT | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Binds 2 potassium ions per subunit. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. Belongs to the aldehyde dehydrogenase family. Extended N-terminus. |
Q6FDF8 | MSDVKLHRLYIHGQYTDATSGKTFDSINPATGEVIATIQQASQTDIEAAVKSAAEGQKVWAAKTAVERSRILRRAVDILRERNDELAQLETLDTGKAFSETSTVDIVTGADVLEYYAGLATAIQGEQVPLRESSFFYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTAFKLAEIYSEAGLPAGVFNVVQGAGREIGQWLTEHAVIEKISFTGGVETGKKVMASAAGSTLKEVTMELGGKSPLIICEDANLDRAADIAVMANFFSSGQVCTNGTRVFIPQRLKAAFEQAVVERVKRIRMGDPQHTDTNFGPLVSFPHMEKVLSYIESGKQQGAKVLIGGERATTGLLAQGAYVQPTVFTDCHDDMKIVQEEIFGPVMSILTYDTIEEAIERANNTNFGLAAGVVTQNISQAHQIIHQLEAGICWINTWGESPAEMPVGGYKESGVGRENGISTLNHYTRTKSIQVELGDYQSVF | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Binds 2 potassium ions per subunit. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. Belongs to the aldehyde dehydrogenase family. |
B7GYG4 | MSDVQVHQLYIHGRYVEATSGKTFNSINPANGEIIATLQQASEQDIEAAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELARLETLDTGKAYSETSTVDIVTGADVLEYYAGLATAIQGEQVPLRESSFFYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSETTPLTALKLAEIYTEAGLPDGVFNVVQGAGREIGQWLTEHPVIEKISFTGGVETGKKVMASAAGSTLKEVTMELGGKSPLIICEDADLNRAADIAVMANFFSSGQVCTNGTRVFVPKSRLADFEKAVVERVKRIRVGDPMAEDTNFGPLTSFPHMEKVLSFIESGKQQGAKVLIGGGRATEGELAKGAYVLPTVFSDCTDQMAIVQEEIFGPVMSILSYETEEEVIQRANDTTFGLAAGVVTQDISRAHRIIHQIEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLGHYTRIKSIQVELGDYQSIF | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Binds 2 potassium ions per subunit. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. Belongs to the aldehyde dehydrogenase family. |
B7I896 | MSDVQVHQLYIHGRYVEATSGKTFNSINPANGEIIATLQQASEQDIEAAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELARLETLDTGKAYSETSTVDIVTGADVLEYYAGLATAIQGEQVPLRESSFFYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSETTPLTALKLAEIYTEAGLPDGVFNVVQGAGREIGQWLTEHPVIEKISFTGGVETGKKVMASAAGSTLKEVTMELGGKSPLIICEDADLNRAADIAVMANFFSSGQVCTNGTRVFVPKSRLADFEKAVVERVKRIRVGDPMAEDTNFGPLTSFPHMEKVLSFIESGKQQGAKVLIGGGRATEGELAKGAYVLPTVFSDCTDQMAIVQEEIFGPVMSILSYETEEEVIQRANDTTFGLAAGVVTQDISRAHRIIHQIEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLGHYTRIKSIQVELGDYQSIF | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Binds 2 potassium ions per subunit. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. Belongs to the aldehyde dehydrogenase family. |
B2HV80 | MSDVQVHQLYIHGRYVEATSGKTFNSINPANGEIIATLQQASEQDIEAAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELARLETLDTGKAYSETSTVDIVTGADVLEYYAGLATAIQGEQVPLRESSFFYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSETTPLTALKLAEIYTEAGLPDGVFNVVQGAGREIGQWLTEHPVIEKISFTGGVETGKKVMASAAGSTLKEVTMELGGKSPLIICEDADLNRAADIAVMANFFSSGQVCTNGTRVFVPKSRLADFEKAVVERVKRIRIGDPMAEDTNFGPLTSFPHMEKVLSFIESGKQQGAKVLIGGGRATEGELAKGAYVLPTVFSDCTDQMAIVQEEIFGPVMSILSYETEEEVIQRANDTTFGLAAGVVTQDISRAHRIIHQIEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLGHYTRIKSIQVELGDYQSIF | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Binds 2 potassium ions per subunit. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. Belongs to the aldehyde dehydrogenase family. |
B0VST2 | MSDVQVHQLYIHGRYVEATSGKTFNSINPANGEIIATLQQASEQDIEAAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELARLETLDTGKAYSETSTVDIVTGADVLEYYAGLATAIQGEQVPLRESSFFYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSETTPLTALKLAEIYTEAGLPDGVFNVVQGAGREIGQWLTEHPVIEKISFTGGVETGKKVMASAAGSTLKEVTMELGGKSPLIICEDADLNRAADIAVMANFFSSGQVCTNGTRVFVPKSRLADFEKAVVERVKRILIGDPMAEDTNFGPLTSFPHMEKVLSFIESGKQQGAKVLIGGGRATEGELAKGAYVLPTVFSDCTDQMAIVQEEIFGPVMSILGYETEEEVIQRANDTTFGLAAGVVTQDISRAHRIIHQIEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLGHYTRIKSIQVELGDYQGIF | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Binds 2 potassium ions per subunit. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. Belongs to the aldehyde dehydrogenase family. |
A3M365 | MSDVQVHQLYIHGRYVEATSGKTFNSINPANGEIIATLQQASEQDIEAAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELARLETLDTGKAYSETSTVDIVTGADVLEYYAGLATAIQGEQVPLRESSFFYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSETTPLTALKLAEIYTEAGLPDGVFNVVQGAGREIGQWLTEHPVIEKISFTGGVETGKKVMASAAGSTLKEVTMELGGKSPLIICEDADLNRAADIAVMANFFSSGQVCTNGTRVFVPKSLLVDFEKAVVERVKRIRIGDPMAEDTNFGPLTSFPHMEKVLSFIESGKQQGAKVLIGGGRATEGELAKGAYVLPTVFSDCTDQMAIVQEEIFGPVMSILSYETEEEVIQRANDTTFGLAAGVVTQDISRAHRIIHQIEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLGHYTRIKSIQVELGDYQSIF | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Binds 2 potassium ions per subunit. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. Belongs to the aldehyde dehydrogenase family. |
B0V944 | MSDVQVHQLYIHGRYVEATSGKTFNSINPANGEIIATLQQASEQDIEAAVKSAQQGQKIWAAMTAMERSRILRRAVDILRERNDELARLETLDTGKAYSETSTVDIVTGADVLEYYAGLATAIQGEQVPLRESSFFYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSETTPLTALKLAEIYTEAGLPDGVFNVVQGAGREIGQWLTEHPVIEKISFTGGVETGKKVMASAAGSTLKEVTMELGGKSPLIICEDADLNRAADIAVMANFFSSGQVCTNGTRVFVPKSRLADFEKAVVERVKRIRVGDPMAEDTNFGPLTSFPHMEKVLSFIESGKQQGAKVLIGGGRATEGELAKGAYVLPTVFSDCTDQMAIVQEEIFGPVMSILSYETEEEVIQRANDTTFGLAAGVVTQDISRAHRIIHQIEAGICWINTWGESPAEMPVGGYKQSGVGRENGLTTLGHYTRIKSIQVELGDYQSIF | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Binds 2 potassium ions per subunit. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. Belongs to the aldehyde dehydrogenase family. |
Q7D0K9 | MTIATPLKAQPKASHFIDGDYVEDNTGTPFESIFPATGEMIAKLHAATPAIVERAIASAKRAQKEWAAMSPMARGRILKRAADIMRERNDALSTLETLDTGKPIQETIVADPTSGADAFEFFGGIAPSALNGDYIPLGGDFAYTKRVPLGVCVGIGAWNYPQQIACWKAAPALVAGNAMVFKPSENTPLGALKIAEILIEAGLPKGLFNVIQGDRDTGPLLVNHPDVAKVSLTGSVPTGRKVAAAAAGHLKHVTMELGGKSPMIVFDDADIESAVGGAMLGNFYSSGQVCSNGTRVFVQKKAKARFLENLKRRTEAMILGDPLDYATHLGPLVSKAQQEKVLSYIEKGKAEGATLITGGGIPNNVAGEGAYVQPTVFADVTDDMTIAREEIFGPVMCVLDFDDEDEVLARANATEFGLAGGVFTADLARAHRVVDGLEAGTLWINTYNLCPVEIPFGGSKQSGFGRENSAAALEHYSELKTVYVSTGKVDAPY | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Binds 2 potassium ions per subunit. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. Belongs to the aldehyde dehydrogenase family. |
B9JBA3 | MRAQPKASHFIDGEYVEDTDGTVIESIYPATGEVIARLHAATPAIVEQAIAAAKRAQPEWAAMSPTARGRILKRAADIMRERNRELSELETLDTGKPIQETIVADPTSGADSFEFFGGIAAAGLNGSYIPLGGDFAYTKRVPLGVCVGIGAWNYPQQIACWKGAPALVAGNAMVFKPSENTPLGALKIAEILIEAGLPKGLYNVIQGDRETGPLLINHPDVAKVSLTGSVPTGRKVAAAAAGSLKHVTMELGGKSPLIVFDDADIDSAIGGAMLGNFYSTGQVCSNGTRVFVNRKIKAEFLKRLKARTEAMLIGDPMDEATQVGPMVSWAQREKVLSYIEKGKAEGATLVAGGGIPNNVSGEGYYVQPTVFADVTDDMTIAREEIFGPVMCVLDFDDEAEVIARANDTEFGLSGGVFTADLTRAHRVVDQLEAGTLWINAYNLAPVEIPFGGSKQSGFGRENSLAALEHYSELKTVYVGMGPVQAPY | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Binds 2 potassium ions per subunit. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. Belongs to the aldehyde dehydrogenase family. |
B2SA42 | MKAQPKASHFIGGAFVEDKAGKPLPVIYPATGEEIASLYSATPGIIEAAYAAALKAQGEWAALKPVERGRILRRTAEILREKNRKLSKLETLDTGKALQETLVADAASAADALEFFGGIISGFNGEFVELGGSFAYTRREALGICVGIGAWNYPIQIAAWKSAPALAMGNAFIFKPSENTPLSALALAEAYKEAGLPDGLFNVVQGYGDVGAALVNHRLTAKVSLTGSVPTGRRIMAQAGEQLKHVTMELGGKSPLIVFDDADLESAIGGAMLGNFYSTGQVCSNGTRVFVHKNIRERFIERLVERTRKIRIGDPFDEATQMGPLISAAQRDKVLSYIKKGKAEGATLACGGGVPKLQGFDKGFFIEPTVFADVTDTMTIAREEIFGPVMSVLEFSDEDEVIARANDSEFGLAAGVFTADLSRGHHVIGQIKAGTCWINAYNLTPVEVPFGGYKQSGIGRENGIAALAHYSQIKTVYVEMGKVDSPY | Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH Binds 2 potassium ions per subunit. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. Belongs to the aldehyde dehydrogenase family. |
P43177 | MGVFNYEIETTSVIPAARLFKAFILDGDNLVPKVAPQAISSVENIEGNGGPGTIKKINFPEGFPFKYVKDRVDEVDHTNFKYNYSVIEGGPVGDTLEKISNEIKIVATPDGGCVLKISNKYHTKGNHEVKAEQVKASKEMGETLLRAVESYLLAHSDAYN | May be a general steroid carrier protein. Causes an allergic reaction in human. Is a cause of type I allergic reactions in Europe, North America and USSR. Belongs to the BetVI family. |
P43178 | MGVFNYETEATSVIPAARLFKAFILDGDNLFPKVAPQAISSVENIEGNGGPGTIKKISFPEGIPFKYVKGRVDEVDHTNFKYSYSVIEGGPVGDTLEKISNEIKIVATPNGGSILKINNKYHTKGDHEVKAEQIKASKEMGETLLRAVESYLLAHSDAYN | May be a general steroid carrier protein. Causes an allergic reaction in human. Is a cause of type I allergic reactions in Europe, North America and USSR. Belongs to the BetVI family. |
P43179 | MGVFNYEIEATSVIPAARLFKAFILDGDNLFPKVAPQAISSVENIEGNGGPGTIKKISFPEGFPFKYVKDRVDEVDHTNFKYSYSVIEGGPVGDTLEKISNEIKIVATPNGGSILKINNKYHTKGDHEVKAEQIKASKEMGETLLRAVESYLLAHSDAYN | May be a general steroid carrier protein. Causes an allergic reaction in human. Is a cause of type I allergic reactions in Europe, North America and USSR. Belongs to the BetVI family. |
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