ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P31005 | MTNFFIPPASVIGRGAVKEVGTRLKQIGAKKALIVTDAFLHSTGLSEEVAKNIREAGLDVAIFPKAQPDPADTQVHEGVDVFKQENCDALVSIGGGSSHDTAKAIGLVAANGGRINDYQGVNSVEKPVVPVVAITTTAGTGSETTSLAVITDSARKVKMPVIDEKITPTVAIVDPELMVKKPAGLTIATGMDALSHAIEAYVAKGATPVTDAFAIQAMKLINEYLPKAVANGEDIEAREAMAYAQYMAGVAFNNGGLGLVHSISHQVGGVYKLQHGICNSVNMPHVCAFNLIAKTERFAHIAELLGENVSGLSTAAAAERAIVALERYNKNFGIPSGYAEMGVKEEDIELLAKNAFEDVCTQSNPRVATVQDIAQIIKNAL | Function: Catalyzes the oxidation of methanol to yield formaldehyde. It possesses a NADH-dependent formaldehyde reductase activity and cannot use NADP.
Catalytic Activity: methanol + NAD(+) = formaldehyde + H(+) + NADH
Sequence Mass (Da): 40045
Sequence Length: 381
Pathway: One-carbon metabolism; methanol degradation; formaldehyde from methanol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.244
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Q9F837 | MTTYVWSYLLEYERERADILDAVQKVFASGSLILGQSVENFETEYARYHGIAHCVGVDNGTNAVKLALESVGVGRDDEVVTVSNTAAPTVLAIDEIGARPVFVDVRDEDYLMDTDLVEAAVTPRTKAIVPVHLYGQCVDMTALRELADRRGLKLVEDCAQAHGARRDGRLAGTMSDAAAFSFYPTKVLGAYGDGGAVVTNDDETARALRRLRYYGMEEVYYVTRTPGHNSRLDEVQAEILRRKLTRLDAYVAGRRAVAQRYVDGLADLQDSHGLELPVVTDGNEHVFYVYVVRHPRRDEIIKRLRDGYDISLNISYPWPVHTMTGFAHLGVASGSLPVTERLAGEIFSLPMYPSLPHDLQDRVIEAVREVITGL | Function: Involved in the biosynthesis of the amino sugar dTDP-L-megosamine which is found in the macrolide antibiotic and antiparasitic megalomicin A. Catalyzes the reversible transfer of the amino group from L-glutamate to the C-3 position of dTDP-3-keto-4,6-deoxyglucose to yield dTDP-3-amino-3,4,6-trideoxyglucose.
Catalytic Activity: 2-oxoglutarate + dTDP-3-amino-3,4,6-trideoxy-alpha-D-glucose = dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucose + L-glutamate
Sequence Mass (Da): 41521
Sequence Length: 374
Pathway: Antibiotic biosynthesis.
EC: 2.6.1.106
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O32436 | MITRLVMIFSVLLLLSGCGQTPFKGKIEKVGMLFPDTINDLVWGTKGYKGLLNIQSKYNVDVYYKEGVKTEEDIINAIEDFHKRGVNLLYGHGSEYAEVFNLVGEDYPDMEFVISNAKAKADNVTSVHFSGEAMGFFGGMTAAHMSKTNQVGVIASFTWQPEVDGFIKGAKYENPDIEVNTKYTDHWDDDTTAVKLYQKMKNEGADVVYPAGDGYNVPVIQQIKKDGLYAIGYVTDQSDLGENTVLTSTVQNVDKAYEIIAEQFNKGTLEGGDHYYDLNTGVVEMGTFSPLVDQDFQQRIAKLIKTYNKTGELPKNE | Function: Positive activator of the comK gene.
Location Topology: Lipid-anchor
Sequence Mass (Da): 35311
Sequence Length: 317
Subcellular Location: Cell membrane
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Q5XVF0 | MICTECENDAFDEEDDGYYYCQRCGVQVENLIQTGVDDGDLIGEGGGTQGALYNPKHRRTEPQPITPSQPRFTDDTSRYSQFKSQFESENGNKELPREVKRAPDSYVDKEPTEPVDFAAETLSYENYYDEARDRYVKAFLMMITYQCDALVDKFNVTPLIIGLVGPISLRYVALSGVYHKDWANNAIRDSEHQSEDGEVKDAKRLKRHKAEPRNIDGKRAVTIWFGILKKTMPLSSSLVISFLACHQAGAPVLPTDIVRWAREGKLPYLSCFLDIREQMGERSAACPVKVSIMARPFQVISAQMLEARASVIADTIGLPLPPVNFYGIASNYIKQLSIPEDKILDLARLIQNWSLPPELYLSTNEQKLPSRVCVMSILIVAIRMLYNINGLGVWERSLGFVNASDGDSETNSGTAEKATEFDTQELLKNLEAKYHEVAAETLESEKDLVSYLSLGKNEFFAGLEEDSPDDTYRIVDNLWNGYPKDEDIECLPKRGRDWDDDVSLNQLSLYDSRFSDGNNPCSSSSRRNESVSIGLDLSSSEHRESSSPEKLKEIAIKRLITDMGDDLFCYIPPRVKVKRLDYLQYVRKKEDGALIYAAHADYYILLRVCAKVAEIDVRNMHRGVLSFERRLAWIEKRIDQVLHLTRPLMTCKHCCDDGNIGEDQDD | Function: Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during transcription initiation such as pre-initiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment (By similarity). Required for the development of the one-cell zygote and endosperm in embryos . Required for micropylar pollen tube guidance, but has no effect on ovule development and gametophytic cell fate specification . May regulate the transcription of secreted cysteine-rich peptide (CRP) genes in the embryo sac .
Sequence Mass (Da): 75475
Sequence Length: 666
Domain: Although it shares weak sequence similarity with GTF2B/TFIIB, displays a similar subdomain organization as GTF2B/TFIIB, with a N-terminal zinc finger, a connecting region (composed of B-reader and B-linker regions), followed by 2 cyclin folds.
Subcellular Location: Nucleus
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C0LGP2 | MKNLCWVFLSLFWFGVFLIIRFAEGQNQEGFISLDCGLPLNEPPYIESETGIQFSSDENFIQSGKTGRIPKNLESENLKQYATLRYFPDGIRNCYDLRVEEGRNYLIRATFFYGNFDGLNVSPEFDMHIGPNKWTTIDLQIVPDGTVKEIIHIPRSNSLQICLVKTGATIPMISALELRPLANDTYIAKSGSLKYYFRMYLSNATVLLRYPKDVYDRSWVPYIQPEWNQISTTSNVSNKNHYDPPQVALKMAATPTNLDAALTMVWRLENPDDQIYLYMHFSEIQVLKANDTREFDIILNGETINTRGVTPKYLEIMTWLTTNPRQCNGGICRMQLTKTQKSTLPPLLNAFEVYSVLQLPQSQTNEIEVVAIKNIRTTYGLSRISWQGDPCVPKQFLWDGLNCNITDISAPPRIISLNLSSSGLSGTIVSNFQNLAHLESLDLSNNSLSGIVPEFLATMKSLLVINLSGNKLSGAIPQALRDREREGLKLNVLGNKELCLSSTCIDKPKKKVAVKVVAPVASIAAIVVVILLFVFKKKMSSRNKPEPWIKTKKKRFTYSEVMEMTKNLQRPLGEGGFGVVYHGDLNGSEQVAVKLLSQTSAQGYKEFKAEVELLLRVHHINLVNLVGYCDEQDHFALIYEYMSNGDLHQHLSGKHGGSVLNWGTRLQIAIEAALGLEYLHTGCKPAMVHRDVKSTNILLDEEFKAKIADFGLSRSFQVGGDQSQVSTVVAGTLGYLDPEYYLTSELSEKSDVYSFGILLLEIITNQRVIDQTRENPNIAEWVTFVIKKGDTSQIVDPKLHGNYDTHSVWRALEVAMSCANPSSVKRPNMSQVIINLKECLASENTRISRNNQNMDSGHSSDQLNVTVTFDTDVKPKAR | Function: Receptor-like serine/threonine-kinase required during the endosperm development in seeds.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 98678
Sequence Length: 878
Subcellular Location: Membrane
EC: 2.7.11.1
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Q9W6U8 | MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCESPDADDYFEHSPLSEDRFSKLNEDSDFIFKRGPPGLPAQNFSMSVTVPVSNPNTLTYSNPGSSLVSPSLAASSSLTSTTMLSPPQTTLHRNVSPGAPQRPPSTGNAGGILGTTDLTVPNGAGTSPVGNGVWNSRASPSLLGTAGGGNGLGKVMPTKSPPPPGGGGLGMNNRKPDLRVVIPPSSKGMMPPLTEEDELELNTQRISSSQSTQPLATPVVSVTTPSFPPAGLVYSAMPTAYNTDYSLTSADLSAFEGFNSPGMLSLGQVSPWQQHHLGPATLSSLVSGSQLSQGSNLSINTNQNINIKSEPISPPRDRVNSSGFPQQQPPQQPQPPQPPQQPPQRQEMGRSPVDSLSSSSSSYDGSDREDPRSDFHSPVVLGRPPNSEDRESPSVKRMRMDTWVT | Function: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Mediates cellular functions in skeletal and cardiac muscle development,.
PTM: Sumoylation on Lys-402 is enhanced by PIAS1 and represses transcriptional activity. Has no effect on nuclear location nor on DNA binding. Sumoylated by SUMO1 and, to a lesser extent by SUMO2 and SUMO3 (By similarity).
Sequence Mass (Da): 53669
Sequence Length: 499
Subcellular Location: Nucleus
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Q02078 | MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLTDSSMLSPPQTTLHRNVSPGAPQRPPSTGNAGGMLSTTDLTVPNGAGSSPVGNGFVNSRASPNLIGATGANSLGKVMPTKSPPPPGGGNLGMNSRKPDLRVVIPPSSKGMMPPLSEEEELELNTQRISSSQATQPLATPVVSVTTPSLPPQGLVYSAMPTAYNTDYSLTSADLSALQGFNSPGMLSLGQVSAWQQHHLGQAALSSLVAGGQLSQGSNLSINTNQNISIKSEPISPPRDRMTPSGFQQQQQQQQQQQPPPPPQPQPQPPQPQPRQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPIVLGRPPNTEDRESPSVKRMRMDAWVT | Function: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter.
PTM: Constitutive phosphorylation on Ser-408 promotes Lys-403 sumoylation thus preventing acetylation at this site. Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation. Phosphorylation on Thr-312 and Thr-319 are the main sites involved in p38 MAPK signaling and activate transcription. Phosphorylated on these sites by MAPK14/p38alpha and MAPK11/p38beta, but not by MAPK13/p38delta nor by MAPK12/p38gamma. Phosphorylation on Ser-408 by CDK5 induced by neurotoxicity inhibits MEF2A transcriptional activation leading to apoptosis of cortical neurons. Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced by EGF.
Sequence Mass (Da): 54811
Sequence Length: 507
Subcellular Location: Nucleus
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A0QRG0 | MTNGVPALDDILERLHVVALPMRVRFRGITVRELALIDGPAGWGEFGAFVEYEPPEAAAWLSSALEAAYRPAPAALRDRVPINATVPAVSAERVPEVLARFPGARTAKVKVAEPGQSLADDVARVNAVRESVPVVRVDANGGWSVDDAVEAAAALTADGELEYLEQPCATVEELAALRARVDVPIAADESIRKAEDPLRVVRAHAADIAVLKVAPLGGVARMLDIAAQIDIPIVVSSALDSSVGIGRGLLAAAALPELRHACGLGTGGLFVDDVAEPRVPVDGCLAVEPAVPDPARLAALAAPEPRRQWWIDRVCACHALI | Function: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB).
Catalytic Activity: (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O
Sequence Mass (Da): 33686
Sequence Length: 321
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7.
EC: 4.2.1.113
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Q6D7W1 | MRQVTLYRYSVPMEAGVVLRNQRLKTRDGLIVRLQEDERLGWGEIAPLPEFSLETLAEAESAALEQLAAWAAGHAFSEDLPPSVAFGLSCAQAELDQHLPQAADYRKAPLCNGDPDELFEMLQAMPGEKVAKVKVGLYEAVRDGMIVNVLLEALPDLKLRLDANRSWTRAKADGFARYVAPSLRSRIAFLEEPCKTREESREFARETGINIAWDESVREADFRVEAEPGVSAIVIKPTLVGSLARCQQLVQETHQAGLTAVISSSIESSLGLTQLARLASWLTPDTIPGLDTLDLMQTQVIQRWPDSALPLLAAEQLDVVWQS | Function: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB).
Catalytic Activity: (1R,6R)-6-hydroxy-2-succinyl-cyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H2O
Sequence Mass (Da): 35674
Sequence Length: 323
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 4/7.
EC: 4.2.1.113
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Q2S2V6 | MAHQSWSVLDAPNPTYLWTQLLVEELVRNGVHTFFVAPGSRSTPLTVAIARHPEAESVLHVDERGAAFAALGVGRAARGPAAWVTTSGTAVANGLPAAVEASVDGVPMLLLTADRPPELRDTGANQTIDQVKIFGDYVRWQADVPPPSDEVDPAYVLTTADQALHQTLRAPAGPVHVNCMFRKPLEPVETEASVAVPTAVDAWARGTEPYTHYPTPAPSPPGPEVDALAETVRGTEHGLVVAGRLDSAAAADATRRLATHLGWPLIPDLTSRLRRGGREQPEQVPYGDLVLTSAAFREGHPPRAVLQVGGRFASKRLRLFLRDSAPEVWAVVRPDPSRIDPDHRVTHHVEAAVPAAVDALVARLEEGPRGTTWRDDWAGASERVGAVVQAHVQESDALTDPLVAALLTEEMPSEHALVAASSMPVRDLNRHAAPGGTGGPAFANRGASGIDGTVATAAGIAEGRDGPVTLLIGDLALQHDLNGLALLQDRPVVAIVVNNDGGGIFHFLPIRKHDEFDPYFTTPHGHDFEHAAALFDLPYHRPDSPSALRSAYAQACRSGESALIEVRTDRATNRQVHDRLEASVERAVEEG | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Mass (Da): 63081
Sequence Length: 591
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
EC: 2.2.1.9
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A1SE26 | MVRAELDKQPSDVRRMFDAVARRYDVTNDVLSMGQDRRWRRAVIAAVDPQPGERVLDLAAGTGTSSQPFADRGASVVPCDFSLGMLRVGKSALPHLPFTAGDGTRLPFADATFDAVTISFGLRNIVDPLSGLRELHRVTRPGGRLVVCEFSHPTFAPFRTVYLEYLMRALPSIARAVSSAPDAYVYLAESIRAWPDQEGLAAMVAEAGWRAPAWRNLSGGIVALHRATR | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25050
Sequence Length: 229
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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B2IUM7 | MTNEVQSIFNRIAPVYDQLNDWLSLGQHRIWKEMAVKWSAAKSGNTALDLCCGSGDLALRLARRVGATGYVYGVDFSCNLLETAKERSQKQYPQPAIAWVEADVLNLPFDDNQFDAATMGYGLRNVKDIPRSLQELHRVLKPGAKAAILDFHRPSNPQLRAFQQLYLNSFVVPVANYLGLKEEYAYISPSLDRFPIGKEQIELARQVGFAVATHYPIANGMMGVLVVSKF | Function: Methyltransferase required for the conversion of 2-phytyl-1,4-beta-naphthoquinol to phylloquinol.
Catalytic Activity: demethylphylloquinol + S-adenosyl-L-methionine = H(+) + phylloquinol + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25739
Sequence Length: 230
Pathway: Cofactor biosynthesis; phylloquinone biosynthesis.
EC: 2.1.1.329
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A1R990 | MNRASLEKRPDEVATMFDDVAPKYDVVNDVLSMGQTRRWRRIVVDAMDVKVGQKVLDLAAGTGTSSEPYADAGVDVVACDFSLGMLKVGKRRRPDIDFIAGDATNLPFADNSFDASTISFGLRNVVEPRKALEEMLRVTKPGGRLVIAEFSHPVVPLWRNLYTEYLMRALPAIATKVSSNPDAYVYLAESIRAWPDQDHLAQWLSDAGWTDITYRNLSGGIVAVHRAQKPDEHRESVPVAKLRRQIKPRHQAG | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28187
Sequence Length: 253
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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Q6MCB5 | MSTYNKNRPQTIQIMFNSIAKQYDRTNAVLSFCLHRRWNLELVKKVQSQQTSHTLLDLCAGTGDVAFSYLNQVSAPCQAYLVDFSSEMLACAEEKAKSFGKTPHSFQYVLADVQRLPFSNQTMDCATMAYGIRNIHHPLQSLQETYRVLKPGGCLGILELTRPENKFLQIGHQLYLKTLLPLLGKWLTANENAYQYLRKSIHTFIPPGELEELVKTAGFINTGRYSLAGGIATIITGFKPMK | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27301
Sequence Length: 242
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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A6L3D5 | MNYPQEKIKPYNADEKKSVQVEKMFDNIAPAYDQLNHALSWNIDKSWRRKAINWLEPFHPQHIMDVATGTGDFAIQACQTLHPQELIGTDISEGMMNVGREKVKAAGLDSRISFAKEDCTALTFPDKRFDAITVAFGVRNFEDLDKGLREMHRVLKDNGKLVILELSEPDWFPMKQLYAVYSKIVIPTLGKLLSKDRSAYTYLPQSIKAFPQGEIMTDIIRKAGFNQVSFKRLTLGICTLYLATK | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27935
Sequence Length: 245
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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B2RJE9 | MQSPEKITPYDTECPKNEQVEAMFNHIAGHYDRLNHLFSWGMDRVWRQKAIRMIEPFAPHTVLDVATGTGDLAIEICRHIPSVKQVTGVDLSLEMMRIGEQKVRSENLDNRITFMQKDCLDLPFADHSFDAVTVAFGLRNFQNIKLGLEEMYRVLNEGAPLMILELSRPVSFPWKQGYNFYASHVIPVVGRFLSQDAEAYTYLPESIAAMPQREELADLMLSVGFREAYYRSLSLEVATVYMGLK | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28057
Sequence Length: 245
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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P59912 | MSVPNVDPSHQSNASANEATRPSPAAEGLDKSGERVREMFRQIAPRYDVMNHLLSLNIDKWWRRKAVQTLKIKGDDPILDLCCGTGDLAIAIADSAGSDVQVIGSDFCHAMLEIARVKESKRTRDTAGGSGRHTIPFLEADSMALPFDDDAFQCVTVAFGLRNIADTDQGLSEMARVCKPGGQVLVLEFSQPTLPVLKQAYNFYFRHVLPRIGQWMARNDKSAYEYLPESVGKFPCGDALAGRMRDVGLQHVTFRPLTLGVATIYVGEKPGGKTDHAEMAAHREREALVAT | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 31929
Sequence Length: 291
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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A7NF26 | MNTNVLPPPDQKAEYVERMFSRIASGYDTMNGIMTLGLDRGWRTATVALAAPPSCGRALDIGTGTGDFLVELAQWMPDGLAVGVDFTLPMMRAGLPKIAGQRAVFVAGDALALPFDDESFDAITTGFTLRNVTDIAAAFREMWRVARVGGTVACLEVARPRQPLLRFGHWVYFQRIVPLMARALGADPEAYTYLPQSARVFPPPDELAQIMREAGWSDVTYRLVGLGAAAIHTGIKRG | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25873
Sequence Length: 238
Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
EC: 2.1.1.163
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P41948 | MSYNFTGTPTGEGTGGNSLTTDLNTQFDLANMGWIGVASAGVWIMVPGIGLLYSGLSRKKHALSLLWASMMASAVCIFQWFFWGYSLAFSHNTRGNGFIGTLEFFGFRNVLGAPSSVSSLPDILFAVYQGMFAAVTGALMLGGACERARLFPMMVFLFLWMTIVYCPIACWVWNAEGWLVKLGSLDYAGGLCVHLTSGHGGLVYALILGKRNDPVTRKGMPKYKPHSVTSVVLGTVFLWFGWMFFNGGSAGNATIRAWYSIMSTNLAAACGGLTWMVIDYFRCGRKWTTVGLCSGIIAGLVGITPAAGFVPIWSAVVIGVVTGAGCNLAVDLKSLLRIDDGLDCYSIHGVGGCIGSVLTGIFAADYVNATAGSYISPIDGGWINHHYKQVGYQLAGICAALAWTVTVTSILLLTMNAIPFLKLRLSADEEELGTDAAQIGEFTYEESTAYIPEPIRSKTSAQMPPPHENIDDKIVGNTDAEKNSTPSDASSTKNTDHIV | Function: Transporter for ammonium (both charged and uncharged NH3 and NH4) to use as a nitrogen source . The affinity of MEP2 is about twenty times higher than that of MEP1 . MEP3 has the lowest affinity . Under ammonium limitation acts as an ammonium sensor, generating a signal that leads to pseudohyphal (filamentous) growth .
PTM: Phosphorylated at Ser-457 by the TORC1 effector kinase NPR1 under nitrogen-limiting conditions which causes a conformational change in the C-terminal region (CTR) to form an open active conformation . Supplementation of nitrogen source leads to inactivation and instant Ser-457 dephosphorylation via plasma membrane PSR1 and PSR2 redundant phosphatases .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53401
Sequence Length: 499
Domain: Within the cytoplasmic CTD, an enhancer domain, limited to residues 428-441, upregulates substrate translocation via the MEP2 hydrophobic core, while an autoinhibitory domain, comprised within the 450-485 region and including the NPR1-target serine Ser-457, counteracts the action of the enhancer domain . In between, a linker domain, limited to residues 442-449, appears required for optimal activity when the kinase is present but dispensable when the kinase integrity is altered .
Subcellular Location: Cell membrane
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P06690 | MNNPERLPSETHKPITGYLWGGLAVLTCPCHLPILAVVLAGTTAGAFLGEHWVIAALGLTGLFLLSLSRALRAFRERE | Function: Broad mercury transporter that mediates the transport of both CH(3)Hg(I) and Hg(II) across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8410
Sequence Length: 78
Subcellular Location: Cell inner membrane
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Q7AKA4 | MNAPDKLPPETRQPVSGYLWGALAVLTCPCHLPILAAVLAGTTAGAFLGEHWGVAALALTGLFVLAVTRLLRAFRGGS | Function: Broad mercury transporter that mediates the transport of both CH(3)Hg(I) and Hg(II) across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 8069
Sequence Length: 78
Subcellular Location: Cell inner membrane
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Q24564 | MSPFGSKKNRSLSVRVSTFDSELEFKLEPRASGQDLFDLVCRTIGLRESWYFGLQYVDTRSNVSWLKMEKRVRDQRVELHASNNVYVFSFYAKFFPENVSEELIQEITQHLFFLQVKQSILSMDIYCRPEASVLLASYAVHVQYGPYDYETYKDGMLAGGELLPKGVTDQYQMTPEMWEERIKTWYMDHEPMTRDEVEMEYLKIAQDLDMYGVNYFPITNKNKTKLWLGVTSVGLNIYDERDKLTPKTTFQWNEIRHVSFDDKKFTIRLVDAKVSNFIFYSQDLHINKMILDLCKGNHDLYMRRRKPDTMEIQQMKAQAKEEKQRRQIERKKFIREKKLREKAEHERYELEKSMEHLQNEMRMANDALRRSEETKELYFEKSRVNEEQMQLTECKANHFKTEMDRLRERQMKIEREKHDLEKKIRDADFYVHQLTVENDKREAETEKLRKELICAKMAEREATARLLEFLNSGRKSSTDSLLTASSVSHAANTASSMAAISTPSLITSSSTNDLETAGGAELTTHSSHYLVQGDNSSGISDDFEPKEFILTDNEMEQITNEMERNHLDYLRNSKQVQSQLQTLRSEIAPHKIEENQSNLDILSEAQIKAGENKYSTLKKLKSGSTKARVAFFEEL | Function: Regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. Mer acts synergistically along with Ex and Kibra to regulate the Hippo signaling pathway.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74492
Sequence Length: 635
Subcellular Location: Cell junction
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P35240 | MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKIYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFAIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFNLIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHNENSDRGGSSKHNTIKKLTLQSAKSRVAFFEEL | Function: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex.
PTM: Phosphorylation of Ser-518 inhibits nuclear localization by disrupting the intramolecular association of the FERM domain with the C-terminal tail . The dephosphorylation of Ser-518 favors the interaction with NOP53 .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69690
Sequence Length: 595
Subcellular Location: Cell projection
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P46662 | MAGAIASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERTRDELERRLLQMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPPPLPPDIPSFDIIADSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDVLHSESSDRGGPSSKHNTIKKLTLQSAKSRVAFFEEL | Function: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex (By similarity). Plays a role in lens development and is required for complete fiber cell terminal differentiation, maintenance of cell polarity and separation of the lens vesicle from the corneal epithelium.
PTM: Phosphorylation of Ser-518 inhibits nuclear localization by disrupting the intramolecular association of the FERM domain with the C-terminal tail. The dephosphorylation of Ser-518 favors the interaction with NOP53.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69776
Sequence Length: 596
Subcellular Location: Cell membrane
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Q63648 | IASRMSFSSLKRKQPKTFTVRIVTMDAEMEFNCEMKWKGKDLFDLVCRTLGLRETWFFGLQYTIKDTVAWLKMDKKVLDHDVSKEEPVTFHFLAKFYPENAEEELVQEITQHLFFLQVKKQILDEKVYCPPEASVLLASYAVQAKYGDYDPSVHKRGFLAQEELLPKRVINLYQMTPEMWEERITAWYAEHRGRARDEAEMEYLKIAQDLEMYGVNYFTIRNKKGTELLLGVDALGLHIYDPENRLTPKISFPWNEIRNISYSDKEFTIKPLDKKIDVFKFNSSKLRVNKLILQLCIGNHDLFMRRRKADSLEVQQMKAQAREEKARKQMERQRLAREKQMREEAERSRDEPERRVLHMKEEATMANEALMRSEETADLLAEKAQITEEEAKLLAQKAAEAEQEMQRIKATAIRTEEEKRLMEQKVLEAEVLALKMAEESERRAKEADQLKQDLQEAREAERRAKQKLLEIATKPTYPPMNPIPAPLPPDIPSFDIIGDSLSFDFKDTDMKRLSMEIEKEKVEYMEKSKHLQEQLNELKTEIEALKLKERETALDILHSEHSDSGTSSKHNTIKKPQAQGRRPICI | Function: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in tumor suppression by restricting proliferation and promoting apoptosis. Along with WWC1 can synergistically induce the phosphorylation of LATS1 and LATS2 and can probably function in the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway. May act as a membrane stabilizing protein. May inhibit PI3 kinase by binding to AGAP2 and impairing its stimulating activity. Suppresses cell proliferation and tumorigenesis by inhibiting the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex Plays a role in lens development and is required for complete fiber cell terminal differentiation, maintenance of cell polarity and separation of the lens vesicle from the corneal epithelium.
PTM: Ubiquitinated by the CUL4A-RBX1-DDB1-DCAF1/VprBP E3 ubiquitin-protein ligase complex for ubiquitination and subsequent proteasome-dependent degradation.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 68712
Sequence Length: 586
Subcellular Location: Cell membrane
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Q7CWE8 | MPIKIPDTLPAFETLVHEGVRVMTETAAIRQDIRPLQIGLLNLMPNKIKTEIQMARLVGASPLQVELSLIRIGGHRAKNTPEEHLLSFYQTWEEVRHRKFDGFIITGAPIELLDYEDVTYWNEMQQIFEWTQTNVHSTLNVCWGAMAAIYHFHGVPKYELKEKAFGVYRHRNLSPSSIYLNGFSDDFQVPVSRWTEVRRADIEKHPELEILMESDEMGVCLAHEKAGNRLYMFNHVEYDSTSLADEYFRDVNSGVPIKLPHDYFPHNDPELAPLNRWRSHAHLFFGNWINEIYQTTPYDPQAIGKLAA | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 35691
Sequence Length: 308
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
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Q72X44 | MPIIIDKDLPARKVLQEENIFVMTKERAETQDIRALKIAILNLMPTKQETEAQLLRLIGNTPLQLDVHLLHMESHLSRNVAQEHLTSFYKTFRDIENEKFDGLIITGAPVETLSFEEVDYWEELKRIMEYSKTNVTSTLHICWGAQAGLYHHYGVQKYPLKEKMFGVFEHEVREQHVKLLQGFDELFFAPHSRHTEVRESDIREVKELTLLANSEEAGVHLVIGQEGRQVFALGHSEYSCDTLKQEYERDRDKGLNIDVPKNYFKHDNPNEKPLVRWRSHGNLLFSNWLNYYVYQETPYVL | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. Utilizes a ping-pong kinetic mechanism in which the acetyl group of acetyl-CoA is initially transferred to the enzyme to form an acetyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-acetylhomoserine. Cannot use succinyl-CoA as the acyl donor.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 35340
Sequence Length: 301
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
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Q5LSN6 | MPIKIPAHLPAYDILTREGVMVMSEDQAARQDIRPLRIGLLNLMPKKIQTETQFARLIGATPLQIELSLIRMTEHQTKTTASEHMEEFYRPFQEVRDEKFDGLIITGAPIEHLEFSDVTYWDELGEVFAWTQSNVHSTFGVCWGGMAMINHFHGIRKHMLDHKAFGCFRHRNLDPASPYLRGFSDDFVIPVSRWTEVKQAEVDAVPELVTLLGSDEVGPCLISDPGHRALYIFNHFEYDSDTLKQEYDRDVEGGTAINVPINYYPDDDPSRKPLNRWRSHAHLLYGNWISEIYETTPYDMARIGLESTDLRG | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 35866
Sequence Length: 312
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
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Q97PM9 | MPIRIDKKLPAVEILRTENIFVMDDQRAAHQDIRPLKILILNLMPQKMVTETQLLRHLANTPLQLDIDFLYMESHRSKTTRSEHMETFYKTFPEVKDEYFDGMIITGAPVEHLPFEEVDYWEEFRQMLEWSKTHVYSTLHICWGAQAGLYLRYGVEKYQMDSKLSGIYPQDTLKEGHLLFRGFDDSYVSPHSRHTEISKEEVLNKTNLEILSEGPQVGVSILASRDLREIYSFGHLEYDRDTLAKEYFRDRDAGFDPHIPENYFKDDDVNQVPCLCWSSSAALFFSNWVDHAVYQETPFDWRKIEDDASAYGYL | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 36927
Sequence Length: 314
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.31
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Q9AMV8 | MSPLSLPVATLGTPRIGPRRELKLALESYWAGKISEQQLHEDAFGLRAANWARQKSLGVTIIPSNDFSLYDQVLDTSVMVGAIPEIYAANGESVSLQTYFAMARGSQCGEQDASCAQSPRGSGVPAQEMTKWFDTNYHYMVPEFYRGQAFRLCSRKPVEEYEEARALGFQTRPVLIGPVTFLKLGKSTDSAFQPLSLLDDLIPVYIDLLHELAKRGASWVQFDEPCLVLDLDEAARNSLLHAYNRFAKEGPAIKIMLASYFGALGDNLDTALSLPISGLHVDLVRAPELLDQIVADGRSDLVMSLGVIDGRNVWRSNLPSLRQRLKPSIAKLGRHRVQLAPSCSLLHVPVDVELETGLASDVKSWLAFSVQKMRELAILARVLAGDQNVGLALAESECAATARRTSPKIHNANVAVRMRAIDQTMRQRATPFARRSEIQRERFGLPAFPTTTIGSFPQTTAVRNARAAHARGAMSEEQYDRFLKEEIARAVRWQEDIGLDVLVHGEFERNDMVQYFSEQLAGFAFTRNGWVQSYGSRCVRPPILFGDVVRPKPITVEWWRYAQSLTSKPMKAMLTGPVTILNWSFVRDDIPRSEVCRQLALAMRDEVRDLENAGAAMIQIDEAALREGLPLRRSDWKAYLDWAGDCFRICSSGVTDQTQIHTHMCYSEFNDIIGAIAAMDADVISIETSRSKMELLDAFRRYEYPNQIGPGVYDIHSPRVPETDEMKELIVLARTRLQDSQLWVNPDCGLKTRKWEEVRPALANMVAAARELRAASDPQIR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 87402
Sequence Length: 781
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
EC: 2.1.1.14
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P57142 | MTILNHTLGFPRIGLNRELKKAQEQYWSGELMIKDLLLVGSELRKKNWQKQKESGIDYIPVGDFAWYDHVLTTSMMLGNIPERHNNTVDSIDLDCLFRIARGCPPDISASEMTKWFNTNYHYIVPEFYKNKVLKYSWKQILDEVDEALLLGHKVKPILLGPITYLWLGKVKGEYFDRLDILKDIILIYKHVLKELSNRSIDFVQIDEPVLVLELPKKWKDAYHYAYKELSGITKLLLTTYFDSIEHNIEFIRDLPVQGIHIDLVHGKYNLKNFSSKIPSEWMLSLGVINGRNIWRSDLLKWFKSIKSISNHHRKILIGSSCSLLHTPIDLVAEKHLDKEVKRWFSFAVQKCEELRLLSSALNDNDIDSIKEWSLPIYERSVSKRVNKIEVENRLSNVLIDKHQRLSPYKTRSIEQNKKFNFPILPTTTIGSFPQTISIRKLRRDFKLGLVTEEEYTKIIKKNIKKVIKIQEELDIDVLVHGEAERNDMVEYFGEHLDGFAFTDNGWVQSYGSRCVKPPIIIGDISRPKPMTIEWSKYAQSLTKKPVKGMLTGPVTILLWSFPREDVSLKKIATQIALALYDEVLDLEKEKIEIIQIDEPALREGLPLRKSSWHEYLSWAVDVFRLSASGVKNTTQIHTHMCYCEFNDIMDSIALLDADVITIEAARSDMELLESFKKFKYPNEVGPGAYDIHSSNIPSVQSIISLLNKAMKYIPLKRIWVNPDCGLKTRNWNETILSLKNMVEATKILREKMKDSECD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 87916
Sequence Length: 758
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
EC: 2.1.1.14
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Q058E7 | MAIKNHILGFPRIGLNRELKFALEKYWSKKNTLEELLLIGKNIRKENWKNQIDSGMDYVTVGDFAWYDHVLNISMMINNIPERHNPNNHILNIDTLFKVARGSKGVDNNICSASEMTKWFNTNYHYIVPEFTSNQKFYFAWKQILEETDEALSLGYKVKPVLLGPLTYLWLGKVKNSKINKLDLLKKILPIYIQVFKELSSRNINWIQIDEPILVLDIPKNWKKEFQSTYKFLDGKIKILLATYFGDITHNLDIINKLSIQGLHIDLVSSKYDLLKLSKSINNNFLLSLGIINGRNIWKTNLLEWFYKLKDFMKINNNFWISSSCSLLHVPLDITIEENLTDFVKSWFSFGIQKCLEISLLSQVLQNNLDIKELKNWIKPIHEYKSSNIVNNTSVQKRTLKISSEQFIRKNEFSVRSKIQKETLCLPVLPTTTIGSFPQTSEIRKLRLDYKNKKINQLDYEKQIKIHIKKNIIQQEQLGLDVLVHGEPERNDMVEYFSEYLEGFVFTTYGWVQSYGSRCVKPPIIVGDISRITPMTVMWSKYAQSLTKKPVKAMLTGPVTILCWSFPREDISKEDICNQIAISLRDEVLDLENSGINIIQIDEPALREGLPLRTHEWNNYLRWAVKSFKICSSGVKNSTQIHTHMCYCEFNDIMPAIVDLDADVITIETSRSDMELLEFFKTFKYPNAIGPGVYDIHSPNIPSVQSIEKLLKKALKYISIQQLWVNPDCGLKTRNWTETSLALQNMLQATLNIRKEYFKK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): 88414
Sequence Length: 760
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1.
EC: 2.1.1.14
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O67422 | MKIGDILRKGVFSISFEFFPPKTEEGERQLFETIRKLEKLNPTFVSVTYGAGGSTRDRTRNIVQKIHEETNLTVMAHLTCIAHTREELIDILQDYKNIGIENILALRGDVPRDKPDWRPPKGACKYAKELVELIRKEFGDWFSIGVASYPEGHPESPNLEWEVKYFKEKVEAGADFSITQMFFVNDYYYRFVEMCKNAGIDISIIPGIMPITNFKQIRKFASLCGATIPQSLIEKLEKVEDKPEEVKKIGIEFAINQCLDLIEHGVPGLHFYTLNKSDATLKIYEAIKDKIPARST | Function: Catalyzes the NADH-dependent reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate. Is required to provide the methyl group necessary for methionine synthetase to convert homocysteine to methionine; the methyl group is given by 5-methyltetrahydrofolate.
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH
Sequence Mass (Da): 33871
Sequence Length: 296
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 1.5.1.54
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P0AEZ1 | MSFFHASQRDALNQSLAEVQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRTIARDYWNNGIRHIVALRGDLPPGSGKPEMYASDLVTLLKEVADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMTNVRIPAWMAQMFDGLDDDAETRKLVGANIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRPGL | Function: Catalyzes the NADH-dependent reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate . Is required to provide the methyl group necessary for methionine synthetase to convert homocysteine to methionine; the methyl group is given by 5-methyltetrahydrofolate. Can also use NADPH as the reductant, but much less effectively than NADH .
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH
Sequence Mass (Da): 33103
Sequence Length: 296
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 1.5.1.54
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G2IQS8 | MATATLDKAALSRLFTDYSLEITPKDVEALENAAHMIPPGTLISVTFLPGAEYEDRARAAKRIQELGFRPVPHLSARRLIDEADLRTYLDMLKGVIDLKHVFVIAGDPNEPLGIYEDALALIDSGILKEYGIEHCGISGYPEGHPDITDEKLAKAMHDKVASLKRQGIDYSIMTQFGFDAEPVLEWLKQIRSEGIDGPVRIGLAGPASIKTLLRFAARCGVGTSAKVVKKYGLSITSLIGSAGPDPVIEDLTPVLGPEHGQVHLHFYPFGGLVKTNEWIVNFKGKQGI | Function: Catalyzes the NADH-dependent reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate. Is required to provide the methyl group necessary for methionine synthetase to convert homocysteine to methionine; the methyl group is given by 5-methyltetrahydrofolate (By similarity). Is required for Sphingobium SYK-6 to grow on vanillate or syringate as the sole source of carbon (Ref.3).
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH
Sequence Mass (Da): 31367
Sequence Length: 288
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 1.5.1.54
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O54235 | MALGTASTRTDRARTVRDILATGKTTYSFEFSAPKTPKGEKNLWSALRRVEAVAPDFVSVTYGAGGSTRAGTVRETQQIVADTTLTPVAHLTAVDHSVAELRNIIGQYADAGIRNMLAVRGDPPGDPNADWIAHPEGLTYAAELVRLIKESGDFCVGVAAFPEMHPRSADWDTDVTNFVDKCRAGADYAITQMFFQPDSYLRLRDRVAAAGCATPVIPEVMPVTSVKMLERLPKLSNASFPAELKERILTAKDDPAAVRSIGIEFATEFCARLLAEGVPGLHFITLNNSTATLEIYENLGLHHPPRA | Function: Catalyzes the NADH-dependent reduction of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate. Is required to provide the methyl group necessary for methionine synthetase to convert homocysteine to methionine; the methyl group is given by 5-methyltetrahydrofolate.
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH
Sequence Mass (Da): 33268
Sequence Length: 307
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 1.5.1.54
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P54419 | MSKNRRLFTSESVTEGHPDKICDQISDSILDEILKKDPNARVACETSVTTGLVLVSGEITTSTYVDIPKTVRQTIKEIGYTRAKYGFDAETCAVLTSIDEQSADIAMGVDQALEAREGTMSDEEIEAIGAGDQGLMFGYACNETKELMPLPISLAHKLARRLSEVRKEDILPYLRPDGKTQVTVEYDENNKPVRIDAIVISTQHHPEITLEQIQRNIKEHVINPVVPEELIDEETKYFINPTGRFVIGGPQGDAGLTGRKIIVDTYGGYARHGGGAFSGKDATKVDRSAAYAARYVAKNIVAAELADSCEVQLAYAIGVAQPVSISINTFGSGKASEEKLIEVVRNNFDLRPAGIIKMLDLRRPIYKQTAAYGHFGRHDVDLPWERTDKAEQLRKEALGE | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 44043
Sequence Length: 400
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
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Q8A2T6 | MGYLFTSESVSEGHPDKVADQISDAVLDKLLAYDPSSKVACETLVTTGQVVLAGEVKTKAYVDLQLIAREVIKKIGYTKGEYMFESNSCGVLSAIHEQSPDINRGVERQDPMEQGAGDQGMMFGYATNETENYMPLSLDLAHRILQVLADIRREEKVMTYLRPDAKSQVTIEYDDNGTPVRIDTIVVSTQHDDFIQPADDSAEAQLKADEEMLSIIRRDVIEILMPRVIASIHHDKVLALFNDQIVYHVNPTGKFVIGGPHGDTGLTGRKIIVDTYGGKGAHGGGAFSGKDPSKVDRSAAYAARHIAKNMVAAGVADEMLVQVSYAIGVARPINIFVDTYGRSHVNMTDGEIARVIDQLFDLRPKAIEERLKLRNPIYQETAAYGHMGREPQVVSKTFFSRYEGNKTVEVELFTWEKLDYVDKIKAAFGL | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 47565
Sequence Length: 430
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
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O43938 | MSVHSILFSSEHVTEGHPDKLCDQVSDAVLDACLAGDPFSKVACESCAKTGMVMVFGEITTKAVLDYQKIVRNTIKDIGFDSADKGLDYESCNVLVAIEQQSPDICQGLGNFDSEDLGAGDQGMMFGYATDETETLMPLTYELARGLAKKYSELRRSGSLEWARPDAKTQVTVEYDYDTREGKQVLTPKRVAVVLISAQHDEHVTNDKISVDLMEKVIKAVIPANMLDAETKYWLNPSGRFVRGGPHGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDPSKVDRSAAYAARWIAKSIVAGGLARRCLVQLAYAIGVAEPLSMHVETYGTGKYDDAKLLEIVKQNFKLRPYDIIQELNLRRPIYYDTSRFGHFGRKDELGTGGFTWEVPKKMVE | Cofactor: Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 43084
Sequence Length: 392
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
EC: 2.5.1.6
|
Q72SM5 | MSLKDFIFTSESVGEGHPDKVCDQISDAVLDAYLEQDPKSRVACETLVTTNLVVIAGEITSKGKVDAQEIARNVIRDIGYNDITMGFDADFAVVSAHVHAQSPDISQGVTEGEGLFKEQGAGDQGLMFGFAINETPELMPMPIYYSHELVKHLAGLRHGNKLKFLRPDAKSQVTVEYKDGKPVRIDTVVISTQHSPDVTHKQIEEALIEECIKKVIPANLLNNTKYFINPTGQFIIGGPHGDAGLTGRKIIVDTYGGYGRHGGGAFSGKDPSKVDRSAAYMGRYIAKNVVASGLADKCEVQLAYAIGVAEPVSVHVDTFGTGKISEEELVKRIRANFKLTPRGIIESLKLLEKGRKYRETASYGHFGRKGSTFTWEETDKASALKG | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 42034
Sequence Length: 386
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
|
A9EXT3 | MRRYQFTSESVTEGHPDKVCDQISDAILDGILEKDPTARVACETLVKTGMAVVAGEITTSAWVDMPVVVRNTIKDIGYTDAAMGFDYETCAVLTAIEKQSPDISRGVTEGEGLFKEQGAGDQGLMFGYATDETSELMPSPISYAHRLARKLADLRKSKKLDWLRPDGKTQVTIEYEDQTPVRVSAVVVSTQHSPEVKHKTIVDAVRSLIIEKCIPAKLMDKSTKIYVNPTGRFVVGGPFGDAGLTGRKIIVDTYGGMGRHGGGAFSGKDPTKVDRSACYYARYVAKNVVASKLAARCEVQIAYAIGVAQPVGVHVNTFGTGRVGEDVLEKYIMQNFDMRPKAIIEQLDLLKPIYRKTAAYGHFGRDEFTWEKTDRAAKLAEDLLRPTLAAVPATTNGAGSKNGSGSKKEPKRKGKKETGAQA | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 45876
Sequence Length: 422
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
|
Q1GND0 | MRNSFLFTSESVSEGHPDKVADQISDSIVDLFLAKDPEARVACETLTTTQLVVLAGEIRCKGVFEDGEWAPGALDEIEATVRRTVREIGYEQAGFHWNRFRFENNLHGQSPQIAQGVDEGAGKDEGAGDQGIMFGYASDETPDFMPATLDYSHKILERMASDRKAGIAPFLEPDAKSQVTLRYANERPVEATAIVVSTQHAPGYYFHNGEGDEAKYTELRKYVLGVIADVLPAELLTANTVYHINPTGRFEIGGPDGDAGLTGRKIIVDTYGGASPHGGGAFSGKDPTKVDRSAAYITRYLAKNIVAAGLARRCTIQLSYAIGVAEPLSIYVDLHGTGTVDEGRIEAVLPQLVRLTPKGIRTHLGLNKPIYRQTAAYGHFGRQADGDAFPWERTDLVDKLKAALAV | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
Catalytic Activity: ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine
Sequence Mass (Da): 44100
Sequence Length: 406
Pathway: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.6
|
A0K5N5 | MIELRNLSQRFPGPGGWVEALHNVNLTIPQGEVFGIIGRSGAGKSTLVRTINLLTRPTEGNVVVGGRDLTLLSAGALREARREIGMIFQHFNLLSSRTVFDNVALPLELAGASRADIEAAVLPLLDLVGLSAQKDRYPSQISGGQKQRVGIARALASQPKVLLSDEATSALDPETTRSILDLLKRINRELGLTIVLITHQMEVIKQVCDRVAVLDAGRVVEEGRVIDVFLQPHHEVTRALIGDVIAQELPPALKARVAERLKTGRGHLLRLAFTGSGVDQPILSETIRRYELDFNILHGQIDEIQGQAFGSLAVLAGGEPGKVGQALAFLREQGVVVEELSYVE | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37260
Sequence Length: 344
Subcellular Location: Cell inner membrane
EC: 7.4.2.11
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Q832Y6 | MIELKNISVTFQQKKQEIQAVQDVSLTIDKGDIYGIVGYSGAGKSTLVRVINLLQRPTAGTVIINKENILTFSKKELRQQRKKIGMIFQHFNLMKERTIFSNIDFSLKYSGLSKSERRQKISHLLELVGLSEKRDAYPSQLSGGQKQRVAIARALANDPEILLCDEATSALDPKTTGQILALLKKLNQELNLTIVLITHEMQVVKEICNKVAVMENGCVVESNDIVSIFSQPQQPLTKDFIRTATHIDQALTTILEHPKLADLDKNQELIEFSYVGDQTNEPLIAQLYSQYQVYTNILYGNVEIVQNVPIGHLIVVLSGDEAQRQQALTYLAKQGVRTNVLKTYQQTKQKQNLQVI | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40091
Sequence Length: 356
Subcellular Location: Cell membrane
EC: 7.4.2.11
|
Q88WA5 | MTEAIIDLKDIAVTFDDGHQVVHAVQDVNLQIQTGDIYGIIGYSGAGKSTLVRVINLLQSPTTGQVVVNGQALQTLSPAALRQARKHVGMIFQHFNLMQSRTVMGNVIYPLLGQKISKQNRRAKALRLLKLVGLTDYAQTYPDKLSGGQKQRVAIARALVTDPQILISDEATSALDPKTTTAILELLQRVNRELGITIVLITHEMQVIKSICHHVAVMADGRIIERGPVAEVFTAPKAPLTVDFVETSTNVRAAIQRITKTIKLSELAAGQELIAFKFVGQSTKQGIVSQLSQTLGVDVNILFANIDQIDGQNVGDMIAIITGDLTAFNAAVTNMSAQGVHTRIINEEVVKGMVD | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38431
Sequence Length: 355
Subcellular Location: Cell membrane
EC: 7.4.2.11
|
Q8YA75 | MIELHQVSKSFNVNGKTVEAVKNVSITVEKGEIFGVVGYSGAGKSTLVRCINLLERPDAGQVVIDGKNLSTLSSKELRVARRKIGMIFQGYNLLKTATVYDNIAKPLKLEGVPKNEIETRVNKYLSIVGLEDKRNNYPSQLSGGQKQRVAIARALAHEPEILLSDEATSALDPETTEAILQLLLKINAELGITIFLITHELDVIQRICDRVAVMENGHLVEQGTVLDIFTKAKHATTKRFVGSEASFDIPQDLLEKYVATGKLVSLHFIGDEADEPALALVSRKFDVLPSILAGGIDHLKNGTLGKLLVHLKGDEVEYSKAISYLKESGVVVEEVELL | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36979
Sequence Length: 338
Subcellular Location: Cell membrane
EC: 7.4.2.11
|
Q8EPK1 | MIQLENIEKHYESKKRRVIGVDQVSLDIKKGEIYGIVGYSGAGKSTLLRCMNVLERPTKGRVFVDGIDLLELNNKQLRKARQSIGMIFQGFYLVSSKTVVENVSFALKAAGVGKLERNKRALELLNLVGIEDKANQYPSQLSGGQKQRVSIARALANNPKVLLCDEATSALDPSTTKSILKLLKKINEQIGITIVIITHEMEVVKEICDRCAVMQNGKVIENGKTYDIFSDPNEKLTKDFIHTVLDFQLPEALLKQCNGTLLKLQFRGDIAAESVVSDMLQQHKVKGNILHGKVEYIKDKPLGVFIMEVSGDPSEISSAISYLEERIKQVEVIQHVSY | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37699
Sequence Length: 338
Subcellular Location: Cell membrane
EC: 7.4.2.11
|
Q47RE8 | MINAVDLHKVYQLKGREVVALRGVSLHVPQGEIYGVVGPSGAGKSTLLRCINLLERPDRGEIWVDGRNLTALPPPQLRAARRGIGMIHQHFALLSSRTVAGNVAFPLEIAGVPRAERRRRVAELLELVGLADKAAAYPAQLSGGQKQRVGIARALAPRPTVLLSDEATSALDPATTASILDLLRDLNRELGLTILLITHEMDVVKRICDAVAIMDRGSVVETGRTVDLLRTPGSLLARSLFAPPPVSGDGVVTLTWVDQAEEPLISQLTRLFDVDVSILGGALEEVAGHAVGRLTVRITGERSAEALTYLTDRNVLVEEVP | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34480
Sequence Length: 321
Subcellular Location: Cell membrane
EC: 7.4.2.11
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O32168 | MFEKYFPNVDLTELWNATYETLYMTLISLLFAFVIGVILGLLLFLTSKGSLWQNKAVNSVIAAVVNIFRSIPFLILIILLLGFTKFLVGTILGPNAALPALVIGSAPFYARLVEIALREVDKGVIEAAKSMGAKTSTIIFKVLIPESMPALISGITVTAIALIGSTAIAGAIGSGGLGNLAYVEGYQSNNADVTFVATVFILIIVFIIQIIGDLITNIIDKR | Function: Part of the ABC transporter complex MetNPQ involved in methionine import. Responsible for the translocation of the substrate across the membrane (Probable). It has also been shown to be involved in methionine sulfoxide transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23756
Sequence Length: 222
Subcellular Location: Cell membrane
|
O32167 | MKKLFLGALLLVFAGVMAACGSNNGAESGKKEIVVAATKTPHAEILKEAEPLLKEKGYTLKVKVLSDYKMYNKALADKEVDANYFQHIPYLEQEMKENTDYKLVNAGAVHLEPFGIYSKTYKSLKDLPDGATIILTNNVAEQGRMLAMLENAGLITLDSKVETVDATLKDIKKNPKNLEFKKVAPELTAKAYENKEGDAVFINVNYAIQNKLNPKKDAIEVESTKNNPYANIIAVRKGEEDSAKIKALMEVLHSKKIKDFIEKKYDGAVLPVSE | Function: Part of the ABC transporter complex MetNPQ involved in methionine import. Binds the methionine and transfers it to the membrane-bound permease. It has also been shown to be involved in methionine sulfoxide transport (Probable).
Location Topology: Lipid-anchor
Sequence Mass (Da): 30355
Sequence Length: 274
Subcellular Location: Cell membrane
|
P28635 | MAFKFKTFAAVGALIGSLALVGCGQDEKDPNHIKVGVIVGAEQQVAEVAQKVAKDKYGLDVELVTFNDYVLPNEALSKGDIDANAFQHKPYLDQQLKDRGYKLVAVGNTFVYPIAGYSKKIKSLDELQDGSQVAVPNDPTNLGRSLLLLQKVGLIKLKDGVGLLPTVLDVVENPKNLKIVELEAPQLPRSLDDAQIALAVINTTYASQIGLTPAKDGIFVEDKESPYVNLIVTREDNKDAENVKKFVQAYQSDEVYEAANKVFNGGAVKGW | Function: This protein is a component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system.
Location Topology: Lipid-anchor
Sequence Mass (Da): 29432
Sequence Length: 271
Subcellular Location: Cell membrane
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P31728 | MKLKQLFAITAIASALVLTGCKEDKKPEAAAAPLKIKVGVMSGPEHQVAEIAAKVAKEKYGLDVQFVEFNDYALPNEAVSKGDLDANAMQHKPYLDEDAKAKNLNNLVIVGNTFVYPLAGYSKKIKNVNELQDGAKVVVPNDPTNRGRALILLEKQGLIKLKDANNLLSTVLDIVENPKKLNITEVDTSVAARALDDVDLAVVNNTYAGQVGLNAQDDGVFVEDKDSPYVNIIVSRTDNKDSKAVQDFIKSYQTEEVYQEAQKHFKDGVVKGW | Function: This protein is a component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system.
Location Topology: Lipid-anchor
Sequence Mass (Da): 29828
Sequence Length: 273
Subcellular Location: Cell outer membrane
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Q88CT3 | MSTVFPEDSVGLVVPQTARFDEPLALACGRSLASYELVYETYGTLNASASNAVLICHALSGHHHAAGYHAATDRKPGWWDSCIGPGKPIDTNRFFVVSLNNLGGCNGSTGPSSVNPATGKPYGADFPVLTVEDWVHSQVRLGERLGIQQWAAVVGGSLGGMQALQWTISYPERVRHCVDIASAPKLSAQNIAFNEVARQAILTDPEFHGGSFQDQGVIPKRGLMLARMVGHITYLSDDSMGEKFGRELKSDKLNYDFHSVEFQVESYLRYQGEEFSGRFDANTYLLMTKALDYFDPAATHGGDLAATLAHVTADYCIMSFTTDWRFSPARSREIVDALMAARKNVCYLEIDSPYGHDAFLIPTPRYMQGFSNYMNRIAI | Function: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
Catalytic Activity: L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine
Sequence Mass (Da): 41659
Sequence Length: 379
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-succinyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.46
|
Q4ZZ78 | MPTVFPHDSVGLVTPQTAHFSEPLALACGRSLPAYDLIYETYGQLNAARSNAVLICHALSGHHHAAGFHSADDRKPGWWDSCIGPGKPIDTTKFFVVSLNNLGGCNGSTGPSSIDPDTGKPFGANFPVVTVEDWVNSQARLADLLGIDTWAAVIGGSLGGMQALQWTISYPNRVRHCLAIASAPKLSAQNIAFNEVARQAILTDPEFHGGSFQERGVIPKRGLMLARMVGHITYLSDDSMGEKFGRGLKSEKLNYDFHSVEFQVESYLRYQGEEFSGRFDANTYLLMTKALDYFDPAANFNDDLAKTFANATARFCVMSFTTDWRFSPARSRELVDALMAARKDVCYLEIDAPQGHDAFLIPIPRYLQAFGNYMNRISL | Function: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
Catalytic Activity: L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine
Sequence Mass (Da): 41691
Sequence Length: 379
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-succinyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.46
|
Q8P6V8 | MVRIVPSARRTRAPAKLDGRSTPDIAMSLVTTASPLTTADTYTPAADSDAPPAVRGELVINLPMRHAGQRELRLRYELVGAEQAPVVFVAGGISAHRHLAASAVFPEKGWVEGLVGAGRALDPASRRLLAFDFLGADGSLDAPIDTADQADAIAALLDALGIARLHGFVGYSYGALVGLQFASRHAARLHTLVAVSGAHRAHPYAAAWRALQRRAVALGQLQCAEHHGLALARQFAMLSYRTPEEFSERFDAPPELINGRVRVAAEDYLDAAGAQYVARTPVNAYLRLSESIDLHRIDPAAVAVPTVVVAVEGDRLVPLADLVSLVEGLGPRGSLRVLRSPFGHDAFLKEIDRIDAILTTALRTTGETA | Function: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
Catalytic Activity: L-homoserine + succinyl-CoA = CoA + O-succinyl-L-homoserine
Sequence Mass (Da): 39292
Sequence Length: 369
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-succinyl-L-homoserine from L-homoserine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.3.1.46
|
Q5SK88 | MRFETLQLHAGYEPEPTTLSRQVPIYPTTSYVFKSPEHAANLFALKEFGNIYSRIMNPTVDVLEKRLAALEGGKAALATASGHAAQFLALTTLAQAGDNIVSTPNLYGGTFNQFKVTLKRLGIEVRFTSREERPEEFLALTDEKTRAWWVESIGNPALNIPDLEALAQAAREKGVALIVDNTFGMGGYLLRPLAWGAALVTHSLTKWVGGHGAVIAGAIVDGGNFPWEGGRYPLLTEPQPGYHGLRLTEAFGELAFIVKARVDGLRDQGQALGPFEAWVVLLGMETLSLRAERHVENTLHLAHWLLEQPQVAWVNYPGLPHHPHHDRAQKYFKGKPGAVLTFGLKGGYEAAKRFISRLKLISHLANVGDTRTLAIHPASTTHSQLSPEEQAQAGVSPEMVRLSVGLEHVEDLKAELKEALA | Function: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway. Has weak activity with O-acetyl-L-serine, O-phospho-L-serine, L-serine, O-succinyl-L-homoserine and L-homoserine. Shows low CTT beta-lyase activity and very low CTT gamma-synthase activity.
Catalytic Activity: hydrogen sulfide + O-acetyl-L-homoserine = acetate + L-homocysteine
Sequence Mass (Da): 46088
Sequence Length: 421
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from O-acetyl-L-homoserine: step 1/1.
EC: 2.5.1.-
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Q5SJ58 | MEYTTLAVLAGLPEDPHGAVGLPIYAVAAYGFKTLEEGQERFATGEGYVYARQKDPTAKALEERLKALEGALEAVVLASGQAATFAALLALLRPGDEVVAAKGLFGQTIGLFGQVLSLMGVTVRYVDPEPEAVREALSAKTRAVFVETVANPALLVPDLEALATLAEEAGVALVVDNTFGAAGALCRPLAWGAHVVVESLTKWASGHGSVLGGAVLSRETELWRNYPQFLQPDLKGQIPWEALRARCFPERVRTLGLSLCGMALSPFNAYLLFQGLETVALRVARMSETARFLAERLQGHPKVKALRYPGLPEDPAHRNARKYLASGGPILTLDLGDLERASRFLGAIRLLKAANLGDARTLLVHPWTTTHSRLKEEARLQAGVTPGLVRVSVGLEDPLDLLALFEEALEAV | Function: Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway. Has weak activity with O-acetyl-L-serine, O-phospho-L-serine, L-serine, O-succinyl-L-homoserine and L-homoserine. Shows a very low CTT gamma-synthase activity.
Catalytic Activity: hydrogen sulfide + O-acetyl-L-homoserine = acetate + L-homocysteine
Sequence Mass (Da): 44184
Sequence Length: 412
EC: 2.5.1.-
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Q503U3 | MAEVNRIHYELEYTEGISQQMRIPERLKIASGSSEEPPGLLNASHSTMMLVPERIVIAGDDNDARFGRPRDLDLIQSTPLETVELKTPPRVLTLNDQPLDFLEPEPAANSTAQPREEMKSHFRSRREQCRSENSTMRRNGQINKHDFASPSPSRAPVRVCPPLISPEDSQNLNSASGVLNYIKSTTRRAYQQVLEVLDDSQRGRASLVTFDASVENTPDDAGLTDAASLRRQIIKLNRRLQLLEHENKERAKREMVMYSLTVAFWLVNSWIWLRR | Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 31360
Sequence Length: 275
Subcellular Location: Mitochondrion outer membrane
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Q7SZQ4 | MSGAAFPSPTAEIAEMNRIHYELEYTEGISQRMRIPEQLKVAPYGSEDQELPDHELLHTAMMHVPERIIVAGHSDDMPFPRDLDLIQSTPQESTLSLKTPPRVLTLSDRPLDFLEMEQTSSVSHPSEEVRTQTKTRRERSVSENAGVHHNGPLARNDSAFALATLDSTLEGGTDDMAVVDATSLRRQIVKLNRRLQLLEEENKERAKREMVMYSITVAFWLVNSWVWFRR | Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 26253
Sequence Length: 230
Subcellular Location: Mitochondrion outer membrane
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Q6GQI8 | MAEINRMQYEREYTEGISQSMRVPEKLKVAPSNSGVDPKTQPDMPIPGVFMEVPERIVIAGHSEESLFSRPSNLDFIPGANIAALALKTPPRVLTLSERPLDFLDLEGPAPATPHSKEVRSSGHLKRDGLASENSLRQNGQLVRHDSMPILRCGSSTSVPVTHHDNPRSAMSTLDTTLDSTPDDLALADAASLRRQIIKLNRRLLLLEEENKERVKHEMTMYSIIIIFGLLNSWLWFRR | Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 26799
Sequence Length: 239
Subcellular Location: Mitochondrion outer membrane
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Q9GZY8 | MSKGTSSDTSLGRVSRAAFPSPTAAEMAEISRIQYEMEYTEGISQRMRVPEKLKVAPPNADLEQGFQEGVPNASVIMQVPERIVVAGNNEDVSFSRPADLDLIQSTPFKPLALKTPPRVLTLSERPLDFLDLERPPTTPQNEEIRAVGRLKRERSMSENAVRQNGQLVRNDSLWHRSDSAPRNKISRFQAPISAPEYTVTPSPQQARVCPPHMLPEDGANLSSARGILSLIQSSTRRAYQQILDVLDENRRPVLRGGSAAATSNPHHDNVRYGISNIDTTIEGTSDDLTVVDAASLRRQIIKLNRRLQLLEEENKERAKREMVMYSITVAFWLLNSWLWFRR | Function: Plays a role in mitochondrial and peroxisomal fission . Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface . May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 38465
Sequence Length: 342
Subcellular Location: Mitochondrion outer membrane
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Q6PCP5 | MAEISRIQYEMEYTEGISQRMRVPEKLKVAPPNADLEQEFQDGVPNASVIMQVPERIVVTGNNEDISFSRPADLDLIQSTPFKPLALKTPPRVLTLSERPLDFLDLERPLPTPQSEESRAVGRLKRERSMSENAVRQNGQLVRNDSIVTPSPPQARVCPPHMLPEDGANLSSARGILSLIQSSTRRAYQQILDVLDENRRPVLRGGSAAATSNPHHDNVRYGISNLDAAIEGASDDMTVVDAASLRRQIIKLNRRLQLLEEENKERAKREMVMYSITVAFWLLNSWLWFRR | Function: Plays a role in mitochondrial and peroxisomal fission . Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface . May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 32931
Sequence Length: 291
Subcellular Location: Mitochondrion outer membrane
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Q5R795 | MAEISRIQYEMEYTEGISQRMRVPEKLKVAPPNADLEQGFQEGVPNASVIMQVPERIVVAGNNEDVSFSRPADLDLIQSTPFKSLALKTPPRVLTLSERPLDFLDLERPPTTPQNEEIRAVGRVKRERSMSENAVRQNGQLVRNDSLYGISNIDTTTEGTSDDLTVVDAASLRRQIIKLNRRLQLLEEENKERAKREMVMYSITVAFWLLNSWLWFRR | Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface. May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 25031
Sequence Length: 218
Subcellular Location: Mitochondrion outer membrane
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Q6DD53 | MAEINRMQYEIDYTEGISQRMRVPEMLKVAPGNLGANLKAQQDMPIPGVVMEVPERIVVAGQSEESPFSRPSDLDFISGTNIGTLALKTPPRVLTLSERPLDFLDLEGLTPATPQSEEIRSSGHLKRDKFSSENALRQNGQLVRHDSMSAMSTLDTTLDATADDLALADAASLRRQIIKLNRRLLLLEEENKERVKHEMTMYSIIIIFGLLNSWLWLRR | Function: Plays a role in mitochondrial and peroxisomal fission. Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface (By similarity).
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 24673
Sequence Length: 219
Subcellular Location: Mitochondrion outer membrane
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Q95114 | MPCPRLLAALFCSSGLFAASGDFCDSSLCLHGGTCLLNEDRTPPFYCLCPEGFTGLLCNETEHGPCFPNPCHNDAECQVTDDSHRGDVFIQYICKCPLGYVGIHCETTCTSPLGMQTGAIADSQISASSMHLGFMGLQRWAPELARLHQTGIVNAWTSGNYDKNPWIQVNLMRKMWVTGVVTQGASRAGSAEYLKTFKVAYSTDGRQFQFIQVAGRSGDKIFIGNVNNSGLKINLFDTPLETQYVRLVPIICHRGCTLRFELLGCELNGCTEPLGLKDNTIPNKQITASSYYKTWGLSAFSWFPYYARLDNQGKFNAWTAQTNSASEWLQIDLGSQKRVTGIITQGARDFGHIQYVAAYRVAYGDDGVTWTEYKDPGASESKIFPGNMDNNSHKKNIFETPFQARFVRIQPVAWHNRITLRVELLGC | Function: Contributes to phagocytic removal of apoptotic cells in many tissues. Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity). Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction.
PTM: The two O-linked glycans consist of Gal, GlcNAc and Fuc, with probably Fuc as reducing terminal sugar.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47411
Sequence Length: 427
Domain: The F5/8 type C 2 domain mediates high-affinity binding to phosphatidylserine-containing membranes.
Subcellular Location: Membrane
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P85297 | DFGHIQYVAAYR | Function: Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction. Contributes to phagocytic removal of apoptotic cells in many tissues. Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 1440
Sequence Length: 12
Subcellular Location: Membrane
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C0HJR4 | ASGPCFPNPCQNDGECHVIDDSHR | Function: Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction. Contributes to phagocytic removal of apoptotic cells in many tissues. Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 2599
Sequence Length: 24
Subcellular Location: Membrane
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Q08431 | MPRPRLLAALCGALLCAPSLLVALDICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKGYAGNHCETKCVEPLGLENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTPSSNDDNPWIQVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHKEFVGNWNKNAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNSIPDKQITASSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHSHKKNLFETPILARYVRILPVAWHNRIALRLELLGC | Function: Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity). Contributes to phagocytic removal of apoptotic cells in many tissues. Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction.
PTM: Medin has a ragged N-terminus with minor species starting at Pro-264 and Gly-273.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 43105
Sequence Length: 387
Domain: The F5/8 type C 2 domain mediates high-affinity binding to phosphatidylserine-containing membranes.
Subcellular Location: Membrane
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P21956 | MQVSRVLAALCGMLLCASGLFAASGDFCDSSLCLNGGTCLTGQDNDIYCLCPEGFTGLVCNETERGPCSPNPCYNDAKCLVTLDTQRGDIFTEYICQCPVGYSGIHCETETNYYNLDGEYMFTTAVPNTAVPTPAPTPDLSNNLASRCSTQLGMEGGAIADSQISASSVYMGFMGLQRWGPELARLYRTGIVNAWTASNYDSKPWIQVNLLRKMRVSGVMTQGASRAGRAEYLKTFKVAYSLDGRKFEFIQDESGGDKEFLGNLDNNSLKVNMFNPTLEAQYIKLYPVSCHRGCTLRFELLGCELHGCSEPLGLKNNTIPDSQMSASSSYKTWNLRAFGWYPHLGRLDNQGKINAWTAQSNSAKEWLQVDLGTQRQVTGIITQGARDFGHIQYVASYKVAHSDDGVQWTVYEEQGSSKVFQGNLDNNSHKKNIFEKPFMARYVRVLPVSWHNRITLRLELLGC | Function: Contributes to phagocytic removal of apoptotic cells in many tissues. Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction (By similarity). Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization.
PTM: N-glycosylated. Isoform 1 also exists in both an O-glycosylated and a non-O-glycosylated form.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51241
Sequence Length: 463
Domain: The F5/8 type C 2 domain mediates high-affinity binding to phosphatidylserine-containing membranes.
Subcellular Location: Membrane
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Q9HE09 | MIVLRDSSDYSDSEVDLPSIEVNGERGNVPTSVLCNVEGSLLNSNPALRQPNLKCIKHNQDVENTTFQLDLRGCRVPSSQPQVITELENNIDIPKNIDAMQNWIFPQTQQYRNYQKEFCEQALFHNLLLALPTGLGKTFIAAVVMLNYFRWFPESKIIFLAPTKPLLLQQRVACSNVAGMSPGATAELNGEVSPDRRLFEYNTKRVFFMTPQTLQNDLKEHLLDAKSIICLIFDEAHRATGNHSYAQVMRAVLRSNSHFRVLGLTATPGSSTASVQKVVDCLHISKLIVRNEESIDIRSYVFHKKIQLIKVTISSEMNILKSDFANLYRPYFNFLRQKKLIPINCECLNIKAYTLFVSLRKYSFSSKNVQSKEKSKIMSCFTLLISCAHITYLLDCHGIIQFYQKLVETKNKAEGKGSGQSFWLFTSKPFAFYLEHLHNKIQGLSLNHPKMNHLLELLKEHFKDTSEGYQNQRVMIFTEFRNTAEYITTTLLAIRPMVRASLFIGQANSAYSTGMNQMQQKETIDQFRAGVINTLVATSIGEEGLDIGDTDMIICYDASSSPIRTIQRMGRTGRKKSGKVFVLLTEDCEDSKWERSQVSYRRVQKVIESGKKIALKKDVPRLIPSNIQPIFKFQALQNNADATLILNSYNNNSSSLSPVNTLANQAHSRSKRYLPFIVDDVFEDMESNLRVPTEDAKIKRFKSDYRSCIYNARRNVFSKPTYMGDKLTKFAKVPHSLLTLSIYRRGRLLQQCSPSSVTKYLKYEEKFKRKRMKKTSNALFQST | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 89463
Sequence Length: 783
Subcellular Location: Nucleus
EC: 3.6.4.12
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A4QN56 | MSPAEAAPRKKHVRFARMEGDVDHDDQEENTLFDKQKDVKEGLKSVLKGGKGILSQGSGQVDVVRPGRSKTGTCWRWLVSLALCASFLGLGMAISVLGPTFEDLAINVNKNISNLSYIFVGRASGYIGGSLLGGILFDFVNPHLLLGFALLTTAFGMSGTPFCKKAWVLTVLMSSVGVSMGVLDTGGNVLILNTWGEQAGPHMQALHFSFAAGAFASPIIAKLLFGHHNSSTNTSLMSGHASKTIDAVLPFSHPKGTSTIDLPWMWAYIVIGAFVLLVSLLFFSLYFCISTNSNRTKTASGKQQFSKHHNTLIILLSMFFFFYVGSEVAYGSFIFTYGKDYVHMEETEAAGLNSLFWGAFAAGRGLAIFFAACLHPGTLILLSLVGTTVSSLLLCLFSQNYPMLWACTALYGISMSTTFPSGISWVEQYTTVTGRSAAIFVVGAALGEMVLPALLGFLLGHVQNYPLLMYLTLCTATFTSILFPVLYKLASPEGNVTLRKSSGKCTIKDADDSEYRQALLENMEEQEENESEADLCNDADFEVIEMDDASLLSSPKSSPPADVAASVPDVHLVASPLSEPNMLSFSTDSPRSKL | Function: May function as a sodium-dependent glucose transporter. Potential channels for urea in the inner medulla of kidney.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64081
Sequence Length: 594
Subcellular Location: Apical cell membrane
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Q5TF39 | MLCASFLGLGLSVAIVGPTFQDLATNVNRNISSLSFIFVGRALGYLSGSVIGGFLVDVMNYFLLLGISMSATTVGLYLVPFCKTAILLTVMMSIFGVSIGILDTGGNVLILAIWGDKGAPHMQALHFSFALGAFLAPLLAKLALGPTASAENHTESDFHPALNQSSDADSEALFGVPNDKNLLWAYAVIGTYMFLVSVIFFCLFLKNSSKQEKARASAETFRRAKYHNALLCLLFLFFFFYVGAEVTYGSYVFSFATTHAGMKESEAAGLNSIFWGTFAACRGLAIFFATCLQPGTMIVLSNIGSLTSSLFLVLFDKNPICLWIATSVYGASMATTFPSGVSWIEQYTTIHGKSAAFFVIGASLGEMAIPAVIGILQGKYPDLPVVLYTSLGASIATGILFPVLYKLATSPLDRQRKEDRKSEDQKALLSSSGLNEYEEENEEEDAEKWNEMDFEMIETNDTMRHSIIETSRSSLTEPTAEVYNQYPSNALVFESSPFNTGSAHVKHLPETRTKGTNV | Function: May function as a sodium-dependent glucose transporter. Potential channels for urea in the inner medulla of kidney.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56218
Sequence Length: 518
Subcellular Location: Apical cell membrane
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Q80T22 | MEFRGSGATAVEQHLLQSETPGKNGLQATSSDQVGRTLRWFTTVVLNAAFLGMGVSAAVLGPTFPDLARNVNRNISSLSEIFVGRALGYLGGSVVGGVLFDCMNHFLLLGLSHLLTAAGLYLTPFCKTAALLTAMMSITGVSFGVLDTGGNVLILDLWGDKGAPHIQALHFSFALGAFLAPLLAKLAWGTTASAQNHTEPQLDRSALNRSFEAASDSVLAVPDDMNLLWAYASIGTYVLVLSVFLFAPFFKKRSKQKKSAASAQGARRAKYHRALLCLLFLFFFFYVGAEVTYGSYVFSFATTHVGMEESEAAGLNSIFWGTFAACRGLAIFFATLLQPGTMMVLCNIGSLASSFFLVLFDKSPLCLWIASSVYGASMAATFPSGISWIEQYTTLTGKSAAFILVGAALGLMATPALSGILQGHYPDLPVILYMCLGSAVLTTVLFPVMYKVATLPLDRKQEKSINSEGQKILLSSSRLIKEAK | Function: May function as a sodium-dependent glucose transporter . Potential channels for urea in the inner medulla of kidney .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51775
Sequence Length: 484
Subcellular Location: Apical cell membrane
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Q569T7 | MAIAVLGPTFLDLAENVESSVANISFIFVGRSMGYLGGSVLGGILFEQINQHLLLGISMLATAAGLFVVPWCKKAVLLTAVMSVVGMSMGFLDTGGNIIILNTWEDQAGPHIQALHFSFALGAFVAPILAKLALEFLPLDKKSFNVSEPFLEQSALPFGIKKSMLSYIVIGTYILLVSLFLFILFSKSRPRQSSGKASDDKFRTARYHNAVIFLLFLFFFCYVGAEVAYGSYIFTYAITYITNIENNYAAGLNSLFWGVFAAVRGLAICFATCLYPGTMLLLSVIGCTLSSLILVLFSRNHLLLWVGTAVYGASMATTFPSGFSWVQQYTTIGGKSASLFVVGAALGEMAIPASVGYLQGMFPNFPVLMYTALASSTMTAILFPVMYKLATAQQDQAQYNRVESDDRRALLSSSGMEEEDEDEAQNWNEADFETIEMNDQMKNSVTVISEDTPGNSAPSEILKHSTKSNGAEAAANKSPSRKHNTDREKND | Function: May function as a sodium-dependent glucose transporter. Potential channels for urea in the inner medulla of kidney.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53397
Sequence Length: 491
Subcellular Location: Apical cell membrane
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A0A4Q4NMP3 | MKEGVVTPPDSEKDLQNVEGSLNTEEEKAEEAHIQLSKGRFVLVLVGLVLAIFLASLDFTIISTAIPKITDEFHSLQDIGWYGSAFFITTAATTAHWGRLYTFFPLKWTYLTSIFFFELGSVICGAAPSSTALIIGRAICGIGAAGLFSGSYTIIAVLVPSADRPKYSGLMGASYGLASVVGPLIGGAFTSHVSWRWCFYINLPVGGVSCLFILLFFANEPPKSRPDWRGMLRQLDMLGLVLIVGAITCFILALQWGGVSKAWDSGAVIGTLVAFVVCMILFVIEQWWLGENAMVHSVMIKRRTIWVGSMFSFLINSAFLVTFYYLPIYFQSVQGVSASTSGVRTVPFILAVTFCVVIVGQIITKTGYAFPWMIVGAAITTIGSGMIYTFDTHSPAGKWIGYQILCGIGVGVSFQVPVMLIQATTKDADVPLATATLLFIQTLGGAFGVSSAQAAFQNTLLKQLAITAPGLNPQIVLDAGASELKRVIPEQFLQGVLEAYVSGFRECLIVGIAFGGAAFLAAFGFRFTNIKRTAAAEA | Function: MFS-type efflux pump involved in the modulation susceptibility to various compounds including the xenobiotics 2,3,5-triiodobenzoic acid (TIBA) and 2-chloro-5-hydroxypyridine (CHP), CuCl(2) several fungicides (clotrimazole, fludioxonil, vinclozolin, and iprodione), potassium superoxide KO(2), and the singlet oxygen-generating compound hematoporphyrin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57832
Sequence Length: 538
Subcellular Location: Cell membrane
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A0QWU7 | MSSRGNRNIAISAGSLAVLLGALDTYVVITIIVDIMADVGIAINQIQQVTPIITGYLLGYIAAMPLLGRASDRFGRKMLIQVGLAGFAVGSVVTALSSDLTMLVIGRIIQGSASGALLPVTLALAADLWSARSRASVLGGVGAAQELGAVLGPMYGIALVWLFNHWQAVFWVNVPLAVIAMVMIHFSLPARQQVDEPERVDVIGGVLLAIALGLTVVGLYNPEPDGKQVLPSWGLPVLAGALVAAVAFFAWEKVAKTRLIDPAGVRFRPFLAALAASLCAGAALMVTLVNVELFGQGVLGQDQDHAAFLLLRFLIALPIGALIGGWLATRIGDRLVVLIGLLIAAGGFVLISHWSVDVLADRHNLGLFTLPVLDTDLAIVGLGLGLVIGPLTSATLRAVPAAEHGIASAAVVVARMIGMLIGIAALGAWGFYRFNQHLATLAARAAGDAGSPMSLAERLTAQAVRYREAYVMMYGDIFLSAAVVCVIGALLGLLISGKHEHAEEFEPAYAPTYGGGGAIDPYDAGDADDAPTEMLDLPTQVLSAPPSDPGDERPGRHRAP | Function: In association with lipoprotein LprG probably transports triacyglycerides (TAG) across the inner cell membrane into the periplasm; TAG probably regulates lipid metabolism and growth regulation (By similarity). Confers resistance to ethidium bromide, possibly acting as an efflux pump, requires LprG lipoprotein for normal function . Export of ethidium bromide can be complemented by the equivalent operon from M.tuberculosis (lprG-Rv1410c) .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58286
Sequence Length: 560
Subcellular Location: Cell inner membrane
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Q4WC50 | MWTTTSGLSGRSLRLSITFAAVVGFSLFGYNQGMMAGLLNGDEFVNSFPILKMPDNPTAGEKHYIDVIRGAVTSCYELGCFFGALFSMFCGNRLGRTRLIFMGASILIVGALLTTVCYTGKWEVGQFVIGRVVSGIGNGMNTATIPVWQSECSGAHNRGFLVCFEGAMIAGGTFIAYWVVFGISHAADSVQWRFPVALQIFFALVVATGALMLPDSPSWFVSRGLDNEACEVLGKIKGTSPDSDQVLHDFNLIKTDMESTKSEQSNWKTVFTFGKTQEFQRLLIGCSGQFFQQFTGCNAAIYYSTLLFQENLHMEKYLSLIMGGVFASVYALATIPSFFMIERVGRRKLYLIGFLGQGLSFVITFACLIKETEENSKGAAVGIFLFITFFAFTLLPLPWIYPPEINPLRTRTVGASASTCTNWMCNFAVVMFTPLFAGQSPWGVYLFFALFNFVGLIFGYFFYVETAGRELEEVDIIYAKAHVEGKMPFRVAHDLPKLSFEEIVQQSRELGLDTNDHVMLEKKELGLSSDSAQETEEVYEKQ | Function: Major facilitator superfamily transporter that may be involved in A.fumigatus adaptation to azoles such as vorizonazole.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60110
Sequence Length: 542
Subcellular Location: Membrane
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P23905 | MNKKVLTLSAVMASLLFGAHAHAADTRIGVTIYKYDDNFMSVVRKAIEKDGKSAPDVQLLMNDSQNDQSKQNDQIDVLLAKGVKALAINLVDPAAAGTVIEKARGQNVPVVFFNKEPSRKALDSYDKAYYVGTDSKESGVIQGDLIAKHWQANQGWDLNKDGKIQYVLLKGEPGHPDAEARTTYVVKELNDKGIQTEQLALDTAMWDTAQAKDKMDAWLSGPNANKIEVVIANNDAMAMGAVEALKAHNKSSIPVFGVDALPEALALVKSGAMAGTVLNDANNQAKATFDLAKNLAEGKGAADGTSWKIENKIVRVPYVGVDKDNLSEFTQK | Function: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import (By similarity). In addition, binds D-galactose and D-glucose and plays a role in the chemotaxis towards these two sugars by interacting with the Trg chemoreceptor (Probable).
Sequence Mass (Da): 35814
Sequence Length: 332
Domain: The calcium-binding site is structurally similar to that of EF-hand proteins, but is in two parts, with the last calcium ligand provided by Glu-228.
Subcellular Location: Periplasm
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Q08255 | MKENSCTACSRRLALFVGAAVLVVGCSSKTDVTLNRDKPLVFFNRQPSDPLTGKVDMAAMNWNDKTYYVGFDAKFGGSIQGKMILDFLASSESSVDRNGDGIIGYVLCIGDVGHNDSKVRTEGIRRALGTWTGSSDPGQAKEGQAVVGGKSYKVVELEGKAMTGTDGSTWNTNSATESMGSWVAKFADKIDLVISNNDGMAMGCLQASNYPRGLPIFGYDANADAVESVGKGELTGTVSQNVDAQAVAVLQIIRNLLDGSSGEDVVANGISRPDAHGNKISAPVQYWEDVKAIMADNSEVTSANWKEYTRGARDAGVRQVSAPTKKVLLTVHNASNDFLASAYLPALKHYAPLLNVDLTVVQGDGQNELSCLDKFTNLDMFDAFAVNMVKTNSGADYTDKLKY | Function: May be involved in the transport of sugars. May have a role in chemotaxis.
Location Topology: Lipid-anchor
Sequence Mass (Da): 43052
Sequence Length: 403
Subcellular Location: Cell membrane
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P23200 | MSALNKKSFLTYLKEGGIYVVLLVLLAIIIFQDPTFLSLLNLSNILTQSSVRIIIALGVAGLIVTQGTDLSAGRQVGLAAVVAATLLQSMDNANKVFPEMATMPIALVILIVCAIGAVIGLINGLIIAYLNVTPFITTLGTMIIVYGINSLYYDFVGASPISGFDSGFSTFAQGFVALGSFRLSYITFYALIAVAFVWVLWNKTRFGKNIFAIGGNPEAAKVSGVNVGLNLLMIYALSGVFYAFGGMLEAGRIGSATNNLGFMYELDAIAACVVGGVSFSGGVGTVIGVVTGVIIFTVINYGLTYIGVNPYWQYIIKGAIIIFAVALDSLKYARKK | Function: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35550
Sequence Length: 336
Subcellular Location: Cell inner membrane
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Q57321 | MRDRTQCVAVPTQAFNEILDQDGQLTAYAQRLEQLRERGSHRVALLRGELARIRQDQVLGMPEKRVQVAAHRLKISEAQAVARQCKTEETQLVRKAVARVRGLFRDFDCSVRDAMREQRLLLKQVATVQHTSASSDQREHCLAQLRQCKEARHHAYRSLVEKSAALRNGKMTFIERVVRALREYSFNFDATQFFLANGLYIAIAVFFIACIVVAPFSGNGNLLTIPNILTILEQSSVRMFYAVGVAGIILLAGTDLSIGRMVAMGSVVTGIILHPGQNIVTFFGLGPWDFTPVPMAVRVVMSLAVSVALCVSFSLFAGFFSARLKIHPFISTLATQLIIYGVLFFGTSGTPVGSIDPYIKDLFGGRWILGTMQGTLVTFPKLIIPATIAVAIAWFIWNKTILGKNMYAVGGNAEAANVSGISVFGVTMSVFAMAAVFYGFGAFFETFKANASAGTGQGYELDAIASCVVGGISFNGGIGKLEGAVVGVIIFTGLTYCLTFLGIDTNLQFVFKGLIIIAAVALDSVKYLKRR | Function: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57875
Sequence Length: 531
Subcellular Location: Cell membrane
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Q99685 | MPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEELARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLGHSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPIDSSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADRLCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTASPP | Function: Converts monoacylglycerides to free fatty acids and glycerol . Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain . Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth .
Catalytic Activity: Hydrolyzes glycerol monoesters of long-chain fatty acids.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33261
Sequence Length: 303
Pathway: Glycerolipid metabolism; triacylglycerol degradation.
Subcellular Location: Cytoplasm
EC: 3.1.1.23
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O35678 | MPEASSPRRTPQNVPYQDLPHLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTLGRIDSSVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRIAAAGAGCPP | Function: Converts monoacylglycerides to free fatty acids and glycerol . Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain . Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth (By similarity).
Catalytic Activity: Hydrolyzes glycerol monoesters of long-chain fatty acids.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33388
Sequence Length: 303
Pathway: Glycerolipid metabolism; triacylglycerol degradation.
Subcellular Location: Cytoplasm
EC: 3.1.1.23
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O07427 | MTTTRTERNFAGIGDVRIVYDVWTPDTAPQAVVVLAHGLGEHARRYDHVAQRLGAAGLVTYALDHRGHGRSGGKRVLVRDISEYTADFDTLVGIATREYPGCKRIVLGHSMGGGIVFAYGVERPDNYDLMVLSAPAVAAQDLVSPVVAVAAKLLGVVVPGLPVQELDFTAISRDPEVVQAYNTDPLVHHGRVPAGIGRALLQVGETMPRRAPALTAPLLVLHGTDDRLIPIEGSRRLVECVGSADVQLKEYPGLYHEVFNEPERNQVLDDVVAWLTERL | Function: Involved in the hydrolysis of exogenous host lipids during chronic infection (Probable). Catalyzes the hydrolysis of both monoacylglycerols (MAG) and diacylglycerols (DAG), with a preference for MAG. It hydrolyzes 2-MAG, 1-3-MAG and MAG with short, medium and long chain fatty acids such as 1-monobutyroyl-rac-glycerol (MC4), 1-mono-octanoyl-rac-glycerol (MC8), 1-monodecanoyl-rac-glycerol (MC10), 1-monolauroyl-rac-glycerol (MC12), 1-monomyristoyl-rac-glycerol (MC14) and 1-mono-oleyl-rac-glycerol (MC18:1) . Also able to hydrolyze DAG with short (DiC6) and medium (DiC10) fatty acid chains, but not with longest fatty acid chains . Can also hydrolyze vinyl laurate (VC12), vinyl butyrate (VC4) and vinyl propionate (VC3) .
Catalytic Activity: a 1-acylglycerol + H2O = a fatty acid + glycerol + H(+)
Sequence Mass (Da): 30262
Sequence Length: 279
Subcellular Location: Secreted
EC: 3.1.1.23
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Q8R431 | MPEASSPRRTPQNVPYQDLPHLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAQMLKRLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDLLQHVNTVQKDYPEVPVFLLGHSMGGAISILAAAERPTHFSGMILISPLILANPESASTLKVLAAKLLNFVLPNISLGRIDSSVLSRNKSEVDLYNSDPLICHAGVKVCFGIQLLNAVSRVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSPSQDKTLKMYEGAYHVLHKELPEVTNSVLHEINTWVSHRIAVAGARCLP | Function: Converts monoacylglycerides to free fatty acids and glycerol . Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain . Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth (By similarity).
Catalytic Activity: Hydrolyzes glycerol monoesters of long-chain fatty acids.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33500
Sequence Length: 303
Pathway: Glycerolipid metabolism; triacylglycerol degradation.
Subcellular Location: Cytoplasm
EC: 3.1.1.23
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O94305 | MADLYTKDWTDVKDKPVARVVFIHGFGEHVNAYPEFFEALNERNIEVYTFDQRGFGHSRKGGPKKQGCTGGWSLVFPDLDYQILRASDTELPLFLWGHSMGGGLALRYGISGTHRHKLAGVIAQAPMLRCHPDTEPNFLLRKALTLVSKVHPNFLFDSDVQSQHITRDEAVNQRLQDDPLVSSVGSLQVFSDMLNRGTKTIELAPQFFLPLLITHGTDDNVTCSDSSKEFYENAGTKDKTYQSYPGFYHSLHIEKKPEVYEYLDKVAAWIYEHSKPSETVKSEQETAVEHPKPTATTSAPSASPTGVPVEEESHKATSDAVPPAEAKPEPVPASAAERAPTSESTTVPETIVASTTKVISEPAPRVTTAATADIVTNK | Function: Converts monoacylglycerides (MAG) to free fatty acids and glycerol. Has a strong preference for monounsaturated monoglycerides. Required for efficient degradation of MAG, short-lived intermediates of glycerolipid metabolism which may also function as lipid signaling molecules. Controls inactivation of the signaling lipid N-palmitoylethanolamine (PEA). Involved in fatty acid ethyl ester (FAEE) catabolism. FAEEs are non-oxidative metabolites of ethanol that are transiently incorporated into lipid droplets (LDs). Their mobilization by LD-resident FAEE hydrolases facilitates a controlled metabolism of these potentially toxic lipid metabolites.
Catalytic Activity: Hydrolyzes glycerol monoesters of long-chain fatty acids.
Sequence Mass (Da): 41624
Sequence Length: 378
Pathway: Glycerolipid metabolism; triacylglycerol degradation.
Subcellular Location: Lipid droplet
EC: 3.1.1.23
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P28321 | MAPYPYKVQTTVPELQYENFDGAKFGYMFWPVQNGTNEVRGRVLLIHGFGEYTKIQFRLMDHLSLNGYESFTFDQRGAGVTSPGRSKGVTDEYHVFNDLEHFVEKNLSECKAKGIPLFMWGHSMGGGICLNYACQGKHKNEISGYIGSGPLIILHPHTMYNKPTQIIAPLLAKFLPRVRIDTGLDLKGITSDKAYRAFLGSDPMSVPLYGSFRQIHDFMQRGAKLYKNENNYIQKNFAKDKPVIIMHGQDDTINDPKGSEKFIQDCPSADKELKLYPGARHSIFSLETDKVFNTVFNDMKQWLDKHTTTEAKP | Function: Converts monoacylglycerides (MAG) to free fatty acids and glycerol . Has a strong preference for monounsaturated monoglycerides . Required for efficient degradation of MAG, short-lived intermediates of glycerolipid metabolism which may also function as lipid signaling molecules. Controls inactivation of the signaling lipid N-palmitoylethanolamine (PEA) . Involved in fatty acid ethyl ester (FAEE) catabolism. FAEEs are non-oxidative metabolites of ethanol that are transiently incorporated into lipid droplets (LDs). Their mobilization by LD-resident FAEE hydrolases facilitates a controlled metabolism of these potentially toxic lipid metabolites .
Catalytic Activity: Hydrolyzes glycerol monoesters of long-chain fatty acids.
Sequence Mass (Da): 35563
Sequence Length: 313
Pathway: Glycerolipid metabolism; triacylglycerol degradation.
Subcellular Location: Lipid droplet
EC: 3.1.1.23
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P82597 | MSEQYPVLSGAEPFYAENGPVGVLLVHGFTGTPHSMRPLAEAYAKAGYTVCLPRLKGHGTHYEDMERTTFHDWVASVEEGYGWLKQRCQTIFVTGLSMGGTLTLYLAEHHPDICGIVPINAAVDIPAIAAGMTGGGELPRYLDSIGSDLKNPDVKELAYEKTPTASLLQLARLMAQTKAKLDRIVCPALIFVSDEDHVVPPGNADIIFQGISSTEKEIVRLRNSYHVATLDYDQPMIIERSLEFFAKHAG | Function: Hydrolyzes monoacylglycerols, with the highest activity occurring with 1-monolauroylglycerol.
Catalytic Activity: Hydrolyzes glycerol monoesters of long-chain fatty acids.
Sequence Mass (Da): 27359
Sequence Length: 250
EC: 3.1.1.23
|
A6TAC8 | MHAYLHCLSHTPLVGFVDPEQAVLDEVNRVIADARRRIAEFDPELVVLFAPDHYNGFFYDVMPPFCLGIGATAIGDFASAAGDLPVPAELAEACAHAILNSGIDLAVSYNMQVDHGFAQPLEFLLGGLDRVPVLPVFINGVAAPLPGFQRTRLLGEAMGRFLNTLNKRVLILGSGGLSHQPPVPELAKADAHLRDRLLGGGKQLPPDERERRQQRVISAARRFTEDPHSLHPLNPVWDNRFMSLLEQGRLSELDAIGNDELSAMAGKSTHEIKTWVAAFAALSAFGRWRSEGRYYRPIPEWIAGFGSLSATTEI | Function: Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively.
Catalytic Activity: 3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-dienedioate + H(+)
Sequence Mass (Da): 34404
Sequence Length: 314
Pathway: Aromatic compound metabolism; 3-phenylpropanoate degradation.
EC: 1.13.11.16
|
A0R1T3 | MPLALCCMSHSPLLNLPGPSAELLDQITDAIADARKFVEQFDPELVVTFSPDHYNGFFYRLMPPFCIGTAAAGVGDYGTYQGPLPVDADIANACAESLWESGVDIAISTAMDVDHGTVQPLQELFGDATARPVVPIFINSVATPLGPLSRSRALGAAVGTFLATLDKRVLIVGSGGLSHDPPVPTLATAPPAALDRIVHGAPMTPEQRMARQEAVIKAAHDFAHGQSPLRSLNPDWDRSLLEIFDEGRLSDLDGWTNTFITGEGGNSAHEIRTWVAAFAALAAHGEYQTGNHFYRAAPELIAGFAIRTAVPST | Function: Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively.
Catalytic Activity: 3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-dienedioate + H(+)
Sequence Mass (Da): 33282
Sequence Length: 313
Pathway: Aromatic compound metabolism; 3-phenylpropanoate degradation.
EC: 1.13.11.16
|
B2JQV7 | MPIHLECMSHTPLHGYFDPAPEVVAEVERVQRVARERVDAFDPELVIVFAPDHYNGFFYDVMPQFCIGVRATAIGDFNSAAGPLPVARDVALALADAALASDIDVAVSYRMQVDHGCAQALDVLTGGIDRYPVVPVFINSVAPPMASCRRARLLGDAIGRAAARMNRRVLLIGSGGMSHEPPVPEIAAADDVVAERLIAGRNPSPESRNARQSRTIAAAKAFAAGDSRLHPLNPAWDRALLELLERGEIAAADGLTNEAITRDAGKSAHEIRTWVAAFGALAASGPYAASIDYYRAIPEWIAGFGAMHAHEQTLSRR | Function: Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively.
Catalytic Activity: 3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-dienedioate + H(+)
Sequence Mass (Da): 34021
Sequence Length: 317
Pathway: Aromatic compound metabolism; 3-phenylpropanoate degradation.
EC: 1.13.11.16
|
Q7N4V6 | MTVKLICTSHTPLMGFGSPPEATEKHVRQVFQQLAEQIKDYDPQLIVIFAPDHFNGFFYDLMPAFCVGVRANAVGDWDIGKGPLNVPENTAKDLISALYDSGIDVAHSWRMQVDHGFTQPLMLLCQNLQRYPTIPIFINCAAKPLPTCRRAVELGRAVGQFLFTTDQRVLLLGSGGLSHDPPIPQMGQVPPEVEEGLIAGRNPTKEARQKRQIRVIEVGKSLARGENIVAPLNPQWDDELLRIFCSGDIRRLASLTEGGIAIQGGKGGQEIRCWIAAFAALSVYGEYKAQRHYYQPIKEWLAGMAMVSAQPVTQIGA | Function: Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively.
Catalytic Activity: 3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-dienedioate + H(+)
Sequence Mass (Da): 34977
Sequence Length: 317
Pathway: Aromatic compound metabolism; 3-phenylpropanoate degradation.
EC: 1.13.11.16
|
P9WKH2 | MPVVKINAIEVPAGAGPELEKRFAHRAHAVENSPGFLGFQLLRPVKGEERYFVVTHWESDEAFQAWANGPAIAAHAGHRANPVATGASLLEFEVVLDVGGTGKTA | Function: Catalyzes the oxidative degradation of the heme macrocyclic porphyrin ring in the presence of a suitable electron donor such as ascorbate or NADPH--cytochrome P450 reductase, with subsequent release of free iron.
Catalytic Activity: 3 AH2 + 2 H(+) + heme b + 3 O2 = 3 A + Fe(2+) + 3 H2O + mycobilin a
Sequence Mass (Da): 11185
Sequence Length: 105
EC: 1.14.99.57
|
O22252 | MASILNQTQELQESSKVLGHLRCENFFLFPGENTLSDGLRGVLYFLGLAYCFIGLSAITARFFKSMENVVKHSRKVVTIDPITKAEVITYKKVWNFTIADISLLAFGTSFPQISLATIDAIRNMGERYAGGLGPGTLVGSAAFDLFPIHAVCVVVPKAGELKKISDLGVWLVELVWSFWAYIWLYIILEVWSPNVITLVEALLTVLQYGLLLVHAYAQDKRWPYLSLPMSRGDRPEEWVPEEIDTSKDDNDNDVHDVYSDAAQDAVESGSRNIVDIFSIHSANNDTGITYHTVADTPPDSATKKGKAKNSTVFDIWKHQFVDAITLETSESKKVDSIYLRIAKSFWHLLLAPWKLLFAFVPPCNIAHGWIAFICSLLFISGVAFVVTRFTDLISCVTGINPYVIAFTALASGTSWPDLVASKIAAERQLTADSAIANITCSNSVNIYVGIGVPWLINTVYNYFAYREPLYIENAKGLSFSLLIFFATSVGCIVVLVLRRLIIGAELGGPRLWAWLTSAYFMMLWVVFVVLSSLKVSGVI | Function: Vacuolar transporter that exchanges protons with Mg(2+), Zn(2+) and Fe(2+) ions. May control the partitioning of Mg(2+) and Zn(2+) between plant organs. Could also transport Cd(2+) in vitro.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59792
Sequence Length: 539
Subcellular Location: Vacuole membrane
|
Q5ZEG0 | MAALLLLSSAARVGVAAPLALRQQRPVVLPGGQLRTGSGAGAASAWAARPLRPELAAVSRPAVPARGRAPLFRPRAWMASSQIASSAFTWGTIAVLPFYTLMVVAPNADVTKRAVDSSAPYVALGILYAYLLYLSWTPDTLRAMFASKYWLPELTGIVRMFASEMTVASAWIHLLAVDLFAARQVYHDGIKNNIETRHSVSLCLLFCPIGIATHVLTKVLAGSIGRSH | Function: Required for neoxanthin biosynthesis, an intermediary step in abscisic acid (ABA) biosynthesis. Involved in an ABA pathway that acts at or downstream of ethylene receptors and positively regulates root ethylene response. In coleoptiles the MHZ4-dependent ABA pathway acts at or upstream of EIN2 to negatively regulate coleoptile ethylene response.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24422
Sequence Length: 228
Subcellular Location: Plastid
|
Q6MMQ9 | MAKRHVIFVVGSTATGKSEWALKLAQEFNGVIVNCDSVQLYKKLDIGSAKPSKAEQALVPHYLLDYVNPPEEMTAGNYCRDFYAILEEIPADKPVFVVGGTGFYFMAIEKGMYPVIPVPVEIQAQVALELETEEGAIRLHAEMMKADPEYGAKIHLADRYRIGRAIELIRSQGKSVTQIQAEFESQRKPFPFPLLKIGPSWDREVLRERIGQRVEKMLAAGLIEEVQGLLDEGLASWAPISSVGYKETLEYLRGGISLSQLQEEITTNTHQLAKRQRTWFQRDKDIQWFDGASGFAEVRTVVEKFLKP | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 34706
Sequence Length: 308
EC: 2.5.1.75
|
B8DT91 | MPSAGVERHDGARVISIVGPTASGKTGLGIAIARRLADRGERAEIVNADAYQMYRGMDIGTAKASDEERAAVRHHLLDVIEPSETMSVARFQQMARETIADLKSRGIRPILVGGSGLYARAAIDDISFPGTDPQIREHLEERERTEGATALFRELAVKDPQAAEHMDPRNPRRIIRALEVIEVTGKPYSATLPRYRYVIPSVQLGLDLDRADLDKRIDVRTRQMFDGGFVDEVARLRSHLGPTAARALGYQQVIDHLDGLVDLDDTMADIAQKTKRLARKQMGWFGRDPRIHWLSALNPALVDNAMAVIDHADAGDYDAIDMHAQEYVQHHLGDIRRPSGAGPV | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 38028
Sequence Length: 344
EC: 2.5.1.75
|
Q7U347 | MRKYFKERDVPFIIFLMGPTASGKTSVVIELKKQKLGIKIISVDSALVYKNMNIGTAKPSVDELEIAPHQLIDIRDPADCYSVSDFYHDAILEINKIIRSGYVPVLVGGTMLYFKTLLTGLYQLPGKSQNIRNDLIYEAQKIGWVNMYNKLKCIDPIVSKTIHCNDHKRIIRALEVFLSSGKTLTELKQKFLNQQSQRYKVLQFALMPSKREFLYNRIEQRFYKMLKSGFEDEVRLLFSRPDLHDGYQSSISCVGYRQMWEYLSGNVEYDQMIYKGIYATRRLVKNQLTWLKKWPNVHWLNGDNVLIAVNDMLSVLSKYSCVI | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 37538
Sequence Length: 323
EC: 2.5.1.75
|
Q7U383 | MTPRAIICLAGPTAAGKSASTLALAQRWPLEIINVDSATIYRGMDIGTAKPSAAERAQVPQHLLDIRDPAQSYSAAEFRADALRLIAEIHARGRIPLLAGGTMLYYKALREGLDDLPQADPALRAELEARAARLGWPALHAELALLDPATAARLSPNDSQRIQRALEICRLAGQPMSALLQGERRGDAPSPYRYVTLSLEPSERAALHARIAQRFDAMLAAGLVEEVRGLHARPDLHPGLPSVRCVGYRQMWSYLDGDIDLDTAREQGVAATRQLAKRQLTWLRAQPERVIIDCLAGDAVARTVDAMARALPD | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 34049
Sequence Length: 313
EC: 2.5.1.75
|
O51761 | MKEDRVVFIFGPTAVGKSNILFHFPKNKAEIINVDSIQVYKEFNIASSKPSKNLMKHIKHHLVDFLDPEKDYTIGIFYEQALKIVKEIRQKKKIPIFVGGTAFYFKHLKDGFPSTPLVTSKIRIYVNNLLELKGKSYLLKELKNVDPIRFNMLNKNDIYRIKRSLEVYYQTGIPISQFQKKQSSEFKNIVIIGLKRSFEDLKTRISIRINEMLNSGLLSEIKGLFSKGYNENTPAFKGIGYNEFLLWKSRPCYGLNDIIGLINKNSFLYAKRQMTFFAKISDVLWLHPEDDLDNILNLIFKVDKEI | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Mass (Da): 35631
Sequence Length: 306
EC: 2.5.1.75
|
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