ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q9SZ70 | MDPVQSHGSQSSLPPPFHARDFQLHLQQQQQHQQQHQQQQQQQFFLHHHQQPQRNLDQDHEQQGGSILNRSIKMDREETSDNMDNIANTNSGSEGKEMSLHGGEGGSGGGGSGEQMTRRPRGRPAGSKNKPKAPIIITRDSANALRTHVMEIGDGCDIVDCMATFARRRQRGVCVMSGTGSVTNVTIRQPGSPPGSVVSLHGRFEILSLSGSFLPPPAPPAATGLSVYLAGGQGQVVGGSVVGPLLCSGPVVVMAASFSNAAYERLPLEEDEMQTPVQGGGGGGGGGGGMGSPPMMGQQQAMAAMAAAQGLPPNLLGSVQLPPPQQNDQQYWSTGRPPY | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Sequence Mass (Da): 35785
Sequence Length: 339
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
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Q9S7C9 | MEGGYEQGGGASRYFHNLFRPEIHHQQLQPQGGINLIDQHHHQHQQHQQQQQPSDDSRESDHSNKDHHQQGRPDSDPNTSSSAPGKRPRGRPPGSKNKAKPPIIVTRDSPNALRSHVLEVSPGADIVESVSTYARRRGRGVSVLGGNGTVSNVTLRQPVTPGNGGGVSGGGGVVTLHGRFEILSLTGTVLPPPAPPGAGGLSIFLAGGQGQVVGGSVVAPLIASAPVILMAASFSNAVFERLPIEEEEEEGGGGGGGGGGGPPQMQQAPSASPPSGVTGQGQLGGNVGGYGFSGDPHLLGWGAGTPSRPPF | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) . Negatively regulates plant innate immunity (PTI) to pathogens through the down-regulation of the PAMP-triggered FRK1 expression . Acts redundantly with AHL18, AHL22 and AHL29 in the regulation of flowering and regulation of the hypocotyl elongation . Acts as a chromatin remodeling factor that negatively regulates the leaf senescence . Acts redundantly with AHL29/SOB3 to modulate hypocotyl growth inhibition in response to light .
Sequence Mass (Da): 31842
Sequence Length: 311
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
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Q9M9R4 | METVGRPRGRPRGSKNKPKAPIFVTIDPPMSPYILEVPSGNDVVEALNRFCRGKAIGFCVLSGSGSVADVTLRQPSPAAPGSTITFHGKFDLLSVSATFLPPLPPTSLSPPVSNFFTVSLAGPQGKVIGGFVAGPLVAAGTVYFVATSFKNPSYHRLPATEEEQRNSAEGEEEGQSPPVSGGGGESMYVGGSDVIWDPNAKAPSPY | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Sequence Mass (Da): 21459
Sequence Length: 206
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
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Q9C9K7 | MDGGYDQSGGASRYFHNLFRPELHHQLQPQPQLHPLPQPQPQPQPQQQNSDDESDSNKDPGSDPVTSGSTGKRPRGRPPGSKNKPKPPVIVTRDSPNVLRSHVLEVSSGADIVESVTTYARRRGRGVSILSGNGTVANVSLRQPATTAAHGANGGTGGVVALHGRFEILSLTGTVLPPPAPPGSGGLSIFLSGVQGQVIGGNVVAPLVASGPVILMAASFSNATFERLPLEDEGGEGGEGGEVGEGGGGEGGPPPATSSSPPSGAGQGQLRGNMSGYDQFAGDPHLLGWGAAAAAAPPRPAF | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) (By similarity). Acts redundantly with AHL18, AHL22 and AHL27 in the regulation of flowering and regulation of the hypocotyl elongation . Acts redundantly with AHL27/ESC to modulate hypocotyl growth inhibition in response to light .
Sequence Mass (Da): 30615
Sequence Length: 302
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
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Q96NN9 | MGGCFSKPKPVELKIEVVLPEKERGKEELSASGKGSPRAYQGNGTARHFHTEERLSTPHPYPSPQDCVEAAVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLDSLHKFQVKIEKEKVYVRASKQALQLQRRTKVMAKCISPSAGYSSSTNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRPKLSKSLDTQPEQLALRPKEFFRAYGIEVLTEAQVVTVDVRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLARGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKEVVLKSSKVVRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFPLAWRNNRKVNIPHWQMAHAQGRVAAQNMLAQEAEMSTVPYLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKGDEVIAVASMNYDPIVSKVAEVLASGRAIRKREVELFVLHSKTGDMSWLTGKGS | Function: Induces apoptosis through a caspase dependent pathway. Reduces mitochondrial membrane potential.
Sequence Mass (Da): 66791
Sequence Length: 605
Domain: The Rieske domain induces apoptosis.
Subcellular Location: Mitochondrion
EC: 1.-.-.-
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Q9NVV5 | MALVPCQVLRMAILLSYCSILCNYKAIEMPSHQTYGGSWKFLTFIDLVIQAVFFGICVLTDLSSLLTRGSGNQEQERQLKKLISLRDWMLAVLAFPVGVFVVAVFWIIYAYDREMIYPKLLDNFIPGWLNHGMHTTVLPFILIEMRTSHHQYPSRSSGLTAICTFSVGYILWVCWVHHVTGMWVYPFLEHIGPGARIIFFGSTTILMNFLYLLGEVLNNYIWDTQKSMEEEKEKPKLE | Function: Hydrolyzes bioactive fatty-acid esters of hydroxy-fatty acids (FAHFAs), but not other major classes of lipids . Show a preference for FAHFAs with branching distal from the carboxylate head group of the lipids .
Catalytic Activity: 9-hexadecanoyloxy-octadecanoate + H2O = 9-hydroxy-octadecanoate + H(+) + hexadecanoate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27458
Sequence Length: 238
Subcellular Location: Cell membrane
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P16454 | MKKTLLASSLIACLSIASVNVYAASESSISIGYAQSHVKENGYTLDNDPKGFNLKYRYELDDNWGVIGSFAYTHQGYDFFYGSNKFGHGDVDYYSVTMGPSFRINEYVSLYGLLGAAHGKVKASVFDESISASKTSMAYGAGVQFNPLPNFVIDASYEYSKLDSIKVGTWMLGAGYRF | Function: Promotes the invasion of pathogenic bacteria into eukaryotic cells by an unknown mechanism.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19548
Sequence Length: 178
Subcellular Location: Cell outer membrane
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O01427 | MENKPPVINLPEKETVNTPQKGGKFTINDFEIGRPLGKGKFGSVYLARTKTGHFHVAIKVLFKSQLISGGVEHQLEREIEIQSHLNHPNIIKLYTYFWDAKKIYLVLEYAPGGEMYKQLTVSKRFSEPTAAKYMYEIADALSYCHRKNVIHRDIKPENLLIGSQGELKIGDFGWSVHAPSNKRQTMCGTMDYLPPEMVNGADHSDAVDLWAIGVLCYEFLVGKPPFEHEDQSKTYAAIKAARFTYPDSVKKGARDLIGRLLVVDPKARCTLEQVKEHYWIQGMMEAKIRAEKQQKIEKEASLRNH | Function: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of chromosome segregation and cytokinesis . The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation . Required for histone H3 phosphorylation during segregation of homologous chromosomes in meiosis and mitosis . Required for histone H3 'Ser-10' phosphorylation . Phosphorylates tlk-1 at 'Ser-634', which enhances its activity . Phosphorylates zen-4 at 'Ser-680'. Required for the recruitment of bub-1 to the ring-shaped domain between chromosomes during meiotic anaphase I . Also required for the localization of the condensin I complex subunit smc-4 to mitotic chromosomes . Acts at the spindle midzone and the midbody to prevent cleavage furrow regression upon chromatin obstructions during cytokinesis .
PTM: Phosphorylated. Increased phosphorylation upon chromatin obstructions at anaphase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 34749
Sequence Length: 305
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9ZSP5 | MKLTHNFSFLLLLLLVHMSSKHILASKDSSSYVVYFGAHSHVGEITEDAMDRVKETHYDFLGSFTGSRERATDAIFYSYTKHINGFAAHLDHDLAYEISKHPEVVSVFPNKALKLHTTRSWDFLGLEHNSYVPSSSIWRKARFGEDTIIANLDTGVWPESKSFRDEGLGPIPSRWKGICQNQKDATFHCNRKLIGARYFNKGYAAAVGHLNSSFDSPRDLDGHGSHTLSTAAGDFVPGVSIFGQGNGTAKGGSPRARVAAYKVCWPPVKGNECYDADVLAAFDAAIHDGADVISVSLGGEPTSFFNDSVAIGSFHAAKKRIVVVCSAGNSGPADSTVSNVAPWQITVGASTMDREFASNLVLGNGKHYKGQSLSSTALPHAKFYPIMASVNAKAKNASALDAQLCKLGSLDPIKTKGKILVCLRGQNGRVEKGRAVALGGGIGMVLENTYVTGNDLLADPHVLPATQLTSKDSFAVSRYISQTKKPIAHITPSRTDLGLKPAPVMASFSSKGPSIVAPQILKPDITAPGVSVIAAYTGAVSPTNEQFDPRRLLFNAISGTSMSCPHISGIAGLLKTRYPSWSPAAIRSAIMTTATIMDDIPGPIQNATNMKATPFSFGAGHVQPNLAVNPGLVYDLGIKDYLNFLCSLGYNASQISVFSGNNFTCSSPKISLVNLNYPSITVPNLTSSKVTVSRTVKNVGRPSMYTVKVNNPQGVYVAVKPTSLNFTKVGEQKTFKVILVKSKGNVAKGYVFGELVWSDKKHRVRSPIVVKL | Function: Serine protease. Has a substrate preference for the hydrophobic residues Phe and Ala and the basic residue Asp in the P1 position, and for Asp, Leu or Ala in the P1' position. May play a role in the degradation of structural proteins in the extracellular matrix of cells located above sites of lateral root formation and thus facilitate lateral root emergence (By similarity).
Sequence Mass (Da): 82874
Sequence Length: 772
Subcellular Location: Secreted
EC: 3.4.21.-
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O43918 | MATDAALRRLLRLHRTEIAVAVDSAFPLLHALADHDVVPEDKFQETLHLKEKEGCPQAFHALLSWLLTQDSTAILDFWRVLFKDYNLERYGRLQPILDSFPKDVDLSQPRKGRKPPAVPKALVPPPRLPTKRKASEEARAAAPAALTPRGTASPGSQLKAKPPKKPESSAEQQRLPLGNGIQTMSASVQRAVAMSSGDVPGARGAVEGILIQQVFESGGSKKCIQVGGEFYTPSKFEDSGSGKNKARSSSGPKPLVRAKGAQGAAPGGGEARLGQQGSVPAPLALPSDPQLHQKNEDECAVCRDGGELICCDGCPRAFHLACLSPPLREIPSGTWRCSSCLQATVQEVQPRAEEPRPQEPPVETPLPPGLRSAGEEVRGPPGEPLAGMDTTLVYKHLPAPPSAAPLPGLDSSALHPLLCVGPEGQQNLAPGARCGVCGDGTDVLRCTHCAAAFHWRCHFPAGTSRPGTGLRCRSCSGDVTPAPVEGVLAPSPARLAPGPAKDDTASHEPALHRDDLESLLSEHTFDGILQWAIQSMARPAAPFPS | Function: Transcription factor playing an essential role to promote self-tolerance in the thymus by regulating the expression of a wide array of self-antigens that have the commonality of being tissue-restricted in their expression pattern in the periphery, called tissue restricted antigens (TRA) . Binds to G-doublets in an A/T-rich environment; the preferred motif is a tandem repeat of 5'-ATTGGTTA-3' combined with a 5'-TTATTA-3' box. Binds to nucleosomes (By similarity). Binds to chromatin and interacts selectively with histone H3 that is not methylated at 'Lys-4', not phosphorylated at 'Thr-3' and not methylated at 'Arg-2'. Functions as a sensor of histone H3 modifications that are important for the epigenetic regulation of gene expression. Mainly expressed by medullary thymic epithelial cells (mTECs), induces the expression of thousands of tissue-restricted proteins, which are presented on major histocompatibility complex class I (MHC-I) and MHC-II molecules to developing T-cells percolating through the thymic medulla . Also induces self-tolerance through other mechanisms such as the regulation of the mTEC differentiation program. Controls the medullary accumulation of thymic dendritic cells and the development of regulatory T-cell through the regulation of XCL1 expression. Regulates the production of CCR4 and CCR7 ligands in medullary thymic epithelial cells and alters the coordinated maturation and migration of thymocytes. In thimic B-cells, allows the presentation of licensing-dependent endogenous self-anitgen for negative selection. In secondary lymphoid organs, induces functional inactivation of CD4(+) T-cells. Expressed by a distinct bone marrow-derived population, induces self-tolerance through a mechanism that does not require regulatory T-cells and is resitant to innate inflammatory stimuli (By similarity).
PTM: Phosphorylated. Phosphorylation could trigger oligomerization.
Sequence Mass (Da): 57727
Sequence Length: 545
Domain: The L-X-X-L-L repeats may be implicated in binding to nuclear receptors.
Subcellular Location: Nucleus
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Q9Z0E3 | MAGGDGMLRRLLRLHRTEIAVAIDSAFPLLHALADHDVVPEDKFQETLRLKEKEGCPQAFHALLSWLLTRDSGAILDFWRILFKDYNLERYSRLHSILDGFPKDVDLNQSRKGRKPLAGPKAAVLPPRPPTKRKALEEPRATPPATLASKSVSSPGSHLKTKPPKKPDGNLESQHLPLGNGIQTMAASVQRAVTVASGDVPGTRGAVEGILIQQVFESGRSKKCIQVGGEFYTPNKFEDPSGNLKNKARSGSSLKPVVRAKGAQVTIPGRDEQKVGQQCGVPPLPSLPSEPQVNQKNEDECAVCHDGGELICCDGCPRAFHLACLSPPLQEIPSGLWRCSCCLQGRVQQNLSQPEVSRPPELPAETPILVGLRSASEKTRGPSRELKASSDAAVTYVNLLAPHPAAPLLEPSALCPLLSAGNEGRPGPAPSARCSVCGDGTEVLRCAHCAAAFHWRCHFPTAAARPGTNLRCKSCSADSTPTPGTPGEAVPTSGPRPAPGLAKVGDDSASHDPVLHRDDLESLLNEHSFDGILQWAIQSMSRPLAETPPFSS | Function: Transcription factor playing an essential role to promote self-tolerance in the thymus by regulating the expression of a wide array of self-antigens that have the commonality of being tissue-restricted in their expression pattern in the periphery, called tissue restricted antigens (TRA) (Probable). Binds to G-doublets in an A/T-rich environment; the preferred motif is a tandem repeat of 5'-. ATTGGTTA-3' combined with a 5'-TTATTA-3' box. Binds to nucleosomes (By similarity). Binds to chromatin and interacts selectively with histone H3 that is not methylated at 'Lys-4', not phosphorylated at 'Thr-3' and not methylated at 'Arg-2'. Functions as a sensor of histone H3 modifications that are important for the epigenetic regulation of gene expression. Mainly expressed by medullary thymic epithelial cells (mTECs), induces the expression of thousands of tissue-restricted proteins, which are presented on major histocompatibility complex class I (MHC-I) and MHC-II molecules to developing T-cells percolating through the thymic medulla (By similarity). Also induces self-tolerance through other mechanisms such as the regulation of the mTEC differentiation program . Controls the medullary accumulation of thymic dendritic cells and the development of regulatory T-cell through the regulation of XCL1 expression . Regulates the production of CCR4 and CCR7 ligands in medullary thymic epithelial cells and alters the coordinated maturation and migration of thymocytes . In thimic B-cells, allows the presentation of licensing-dependent endogenous self-anitgen for negative selection . In secondary lymphoid organs, induces functional inactivation of CD4(+) T-cells. Expressed by a distinct bone marrow-derived population, induces self-tolerance through a mechanism that does not require regulatory T-cells and is resitant to innate inflammatory stimuli .
PTM: Phosphorylated.
Sequence Mass (Da): 59042
Sequence Length: 552
Domain: Interacts via the first PHD domain with the N-terminus of histone H3 that is not methylated at 'Lys-4'. Disruption of the first PHD domain has been shown to lead to reduced transcriptional activity and to localization of the protein mainly in the cytoplasm in small granules. While the PHD zinc fingers are necessary for the transactivation capacity of the protein, other regions also modulate this function (By similarity).
Subcellular Location: Nucleus
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Q9NX04 | MTQDRPLLAVQEALKKCFPVVEEQQGLWQSALRDCQPLLSSLSNLAEQLQAAQNLRFEDVPALRAFPDLKERLRRKQLVAGDIVLDKLGERLAILLKVRDMVSSHVERVFQIYEQHADTVGIDAVLQPSAVSPSVADMLEWLQDIERHYRKSYLKRKYLLSSIQWGDLANIQALPKAWDRISKDEHQDLVQDILLNVSFFLEE | Function: Involved in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RSL24D1/RLP24 from the pre-ribosomal particles . Acts together with AFG2A, AFG2B and CINP .
PTM: Phosphorylated on serines by CK2 kinase.
Sequence Mass (Da): 23373
Sequence Length: 203
Subcellular Location: Nucleus
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Q499E6 | MAHDQPLLVVQEALRKCFPVVEEQQNLWQSTLQDCSPLLSSLSNLAEQLQAAQSLRFEDVPALRPFPDLQERLRRKQLEAGDVVLDKLAERLATLLKVRNTINSHVEQVFQAYEQHAAVLDIDTVLRPSVVSPSVADMLEWLQDIDRHYGSSYLKRKYLLSSIHWGDLASIQALPKAWDQISENECQTLVSDVLVSVSFFLEEPGGCAASGDLEHHS | Function: Involved in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RSL24D1/RLP24 from the pre-ribosomal particles. Acts together with AFG2A, AFG2B and CINP.
PTM: Phosphorylated on serines by CK2 kinase.
Sequence Mass (Da): 24442
Sequence Length: 217
Subcellular Location: Nucleus
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Q93ZF6 | MGCCCCLPSIPESSRTIDEHLPLSRATPSSLSNAYSSPLSPPIPLAITNINLQTSPPKLPRTQGNSSEASPGLTQVVPEKKTWHVDDLTDFELKKQYREAIDECPICLEEYEIDNPKLLTKCGHDFHLACILAWMERSEACPVCDKELVLTES | Function: Possesses E3 ubiquitin-protein ligase activity in vitro when associated with the E2 enzyme UBC8 in vitro . Plays combinatory roles with AIRP2 in the positive regulation of the abscisic acid-mediated drought stress response .
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 16940
Sequence Length: 153
Domain: The RING-type zinc finger domain is required for E3 ligase activity.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q9M022 | MRKSFKDSLKALEADIQFANTLASEYPEEYDGGYVQMRLSYSPAAHLFLFLLQWTDCHFAGALGLLRILIYKAYVDGKTTMSLHERKTSIREFYDVLFPSLLQLHGGITDVEERKQKEICDKRYRKKDRTDKGKMSEIDLEREEECGICLEIRNKVVLPTCNHSMCINCYRNWRARSQSCPFCRGSLKRVNSGDLWIYTCSAEIADLPAIYKENLKRLLIYIDKLPLVTSDPNLVPYAPLPR | Function: Possesses E3 ubiquitin-protein ligase activity in vitro when associated with the E2 enzyme UBC8 in vitro . Plays combinatory roles with AIRP1 in the positive regulation of the abscisic acid-mediated drought stress response . Plays a positive role in abscisic acid- and high salinity-regulated seed germination through the ubiquitin-proteasome-dependent down-regulation of ATP1/SDIRIP1 .
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 28049
Sequence Length: 242
Domain: The RING-type zinc finger domain is required for E3 ligase activity.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q8ZKR2 | MKAMNKVWVIGDASVDLVPEKQNSYLKCPGGASANVGVCVARLGGECGFIGCLGDDDAGRFLRQVFQDNGVDVTFLRLDADLTSAVLIVNLTADGERSFTYLVHPGADTYVSPQDLPPFRQYEWFYFSSIGLTDRPAREACLEGARRMREAGGYVLFDVNLRSKMWGNTDEIPELIARSAALASICKVSADELCQLSGASHWQDARYYLRDLGCDTTIISLGADGALLITAEGEFHFPAPRVDVVDTTGAGDAFVGGLLFTLSRANCWDHALLAEAISNANACGAMAVTAKGAMTALPFPDQLNTFLSSHSLAQAMTVK | Function: Phosphorylates 5-amino-1-(beta-D-ribosyl)imidazole (AIRs) to form 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole (AIR), an important intermediate in the purine and thiamine biosynthetic pathways . It allows the use of exogenous aminoimidazole riboside (AIRs) to satisfy the cellular requirement for purines and thiamine .
Catalytic Activity: 5-amino-1-(beta-D-ribosyl)imidazole + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+)
Sequence Mass (Da): 34238
Sequence Length: 319
Domain: Does not show significant conformational changes upon substrate binding.
EC: 2.7.1.223
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O93801 | MQQPIIGVGHSMGGCQIATLSVTSRRMFSTMILLDPAIGPPDMGLATLDLGQLTLRRRTQWPTREDAEKALRTSFSTWDSQVLNLLIKHSIHSDKQSIEMEDGPVSLVTGRYQELVNYIKPSFIRSGKVNGQELIHQTGPVDMYHMLGLVTCSALYLCGGESTLSVPRVRDLWLNRTAKLSYSKEPGETRKVDERIVPDTGHFLPMEEPKKCADIIADWIEKDKCIAWNCCVGKRGKTWCELSNASKEMSAEAWMKYLQSKL | Function: Abhydrolase domain-containing protein; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible for Japanese pear black spot disease by the Japanese pear pathotype . AK-toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA) . On cellular level, AK-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment . The acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety . Part of the EDA biosynthesis occurs in the peroxisome since these 3 enzymes are localized in peroxisomes . The exact roles of the 3 enzymes, as well as of additional AK-toxin clusters enzymes, including AKT4, AKT6 and AKTS1, have still to be elucidated . The Cytochrome P450 monooxygenase AKT7 on the other side functions to limit production of EDA and AK-toxin, probably via the catalysis of a side reaction of EDA or its precursor .
Sequence Mass (Da): 29432
Sequence Length: 262
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Peroxisome
EC: 3.1.1.-
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Q38898 | MDLKYSASHCNLSSDMKLRRFHQHRGKGREEEYDASSLSLNNLSKLILPPLGVASYNQNHIRSSGWIISPMDSRYRCWEFYMVLLVAYSAWVYPFEVAFLNSSPKRNLCIADNIVDLFFAVDIVLTFFVAYIDERTQLLVREPKQIAVRYLSTWFLMDVASTIPFDAIGYLITGTSTLNITCNLLGLLRFWRLRRVKHLFTRLEKDIRYSYFWIRCFRLLSVTLFLVHCAGCSYYLIADRYPHQGKTWTDAIPNFTETSLSIRYIAAIYWSITTMTTVGYGDLHASNTIEMVFITVYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIEAASNFVNRNRLPPRLKDQILAYMCLRFKAESLNQQHLIDQLPKSIYKSICQHLFLPSVEKVYLFKGVSREILLLLVSKMKAEYIPPREDVIMQNEAPDDVYIIVSGEVEIIDSEMERESVLGTLRCGDIFGEVGALCCRPQSYTFQTKSLSQLLRLKTSFLIETMQIKQQDNATMLKNFLQHHKKLSNLDIGDLKAQQNGENTDVVPPNIASNLIAVVTTGNAALLDELLKAKLSPDITDSKGKTPLHVAASRGYEDCVLVLLKHGCNIHIRDVNGNSALWEAIISKHYEIFRILYHFAAISDPHIAGDLLCEAAKQNNVEVMKALLKQGLNVDTEDHHGVTALQVAMAEDQMDMVNLLATNGADVVCVNTHNEFTPLEKLRVVEEEEEEERGRVSIYRGHPLERRERSCNEAGKLILLPPSLDDLKKIAGEKFGFDGSETMVTNEDGAEIDSIEVIRDNDKLYFVVNKII | Function: Highly selective and weak inward-rectifying potassium channel. Plays a role in both loading and unloading potassium into/from the phloem sap. Seems to control sugar loading into phloem via a voltage-dependent process. Blocked by physiological concentrations of external calcium and by external acidification. May interact with the cytoskeleton or with regulatory proteins. Dephosphorylation by PP2CA not only leads to the inhibition of potassium currents but also to an increase of the voltage-dependence of the channel. Regulated by the CBL4/CIPK6 calcium sensor/protein kinase complex via a kinase interaction-dependent but phosphorylation-independent translocation of the channel to the plasma membrane.
PTM: Dephosphorylated by PP2CA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91308
Sequence Length: 802
Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids. The pore-forming region H5 is enclosed by the transmembrane segments S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD signature motif which seems to be involved in potassium selectivity.
Subcellular Location: Endoplasmic reticulum membrane
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Q9XTG7 | MSTENAHLQKEDIVIESWLHKKGEHIRNWRPRYFILFRDGTLLGFRSKPKEDQPLPEPLNNFMIRDAATVCLDKPRPNMFIVRCLQWTTVIERTFYADSADFRQMWIEAIQAVSSHNRLKENAGNTSMQEEDTNGNPSGESDVNMDATSTRSDNDFESTVMNIDEPEEVPRKNTVTMDDFDFLKVLGQGTFGKVILCREKSSDKLYAIKIIRKEMVVDRSEVAHTLTENRVLYACVHPFLTLLKYSFQAQYHICFVMEFANGGELFTHLQRCKTFSEARTRFYGSEIILALGYLHHRNIVYRDMKLENLLLDRDGHIKITDFGLCKEEIKYGDKTSTFCGTPEYLAPEVIEDIDYDRSVDWWGVGVVMYEMMCGRLPFSAKENGKLFELITTCDLKFPNRLSPEAVTLLSGLLERVPAKRLGAGPDDAREVSRAEFFKDVDWEATLRKEVEPPFKPNVMSETDTSFFDREFTSMPVQLTPPRRGEELPTVDEEEELQANFIQFASYYVSGSLERSYDTNRSADKYEIR | Function: Acts downstream of PI3 kinase age-1 and kinase pdk-1 in the daf-2/insulin receptor-like transduction pathway . Essential role in regulating developmental arrest at the dauer stage . Phosphorylates Forkhead-related daf-16 and the longevity-promoting skn-1 transcription factors, which inhibits their entry into the nucleus and antagonizes their functions . Role in immune function and pathogen resistance . Downstream of age-1 and together with akt-1 and sgk-1, promotes cell survival during embryonic development . Plays a role in maintaining the gonadal basement membrane through antagonizing akt-1 activity .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 61058
Sequence Length: 528
Domain: The PH domain binds to phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) resulting in its targeting to the plasma membrane.
EC: 2.7.11.1
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P31751 | MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSASIRE | Function: AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.
PTM: Phosphorylation on Thr-309 and Ser-474 is required for full activity.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 55769
Sequence Length: 481
Domain: Binding of the PH domain to phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) following phosphatidylinositol 3-kinase alpha (PIK3CA) activity results in its targeting to the plasma membrane.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q60823 | MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRGPGEDAMDYKCGSPSDSSTSEMMEVAVNKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLGPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLDPLELDQRTHFPQFSYSASIRE | Function: AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinases, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.
PTM: Phosphorylation on Thr-309 and Ser-474 is required for full activity.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 55742
Sequence Length: 481
Domain: Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PIK3CA) results in its targeting to the plasma membrane.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q75HP9 | MKTSSFESASSSGGSGGGGGGGGGEGSGSFNLRNLSKLILPPLGVPAGGHAQSGHAGPNDRRVISPLDSRYRCWDTFMVVLVAYSAWVYPFEVAFMNASPKGGLEVADIVVDLFFAVDIVLTFFVAYIDSRTQLLVRDRRRIATRYLSTFFIMDVASTIPFQGLAYIVTGEVRESPAFSLLGILRLWRLRKVKQFFTRLEKDIRFNYFWIRCARLIAVTLFLVHCAGCLYYLIADRYPHREKTWIGAVIPDFQEASLWIRYTSSVYWSITTMTTVGYGDMHAQNTVEMIFNIFYMLFNLGLTAYLIGNMTNLVVEGTRRTMEFRNSIRAASNFVGRNHLPPRLKQQILAYMCLKFRAESLNQQQLMDQLPKSICKGICEYLFLPVVKDVYLFKGVSREVLLLMVTKMKPEYIPPKEDVIVQNEAPDDVYIVVSGEVEVIYSDGEAEERVVATLGTRGVFGEVSALSDRPQSFTLRTRTLCQLLRLRQAALKEAMQSKPEDSVVIIKNFLKHQIEMHDMKVEDLLGEDAAGEYDHGNIPCNLLTVAATGNSSFLEDLLKVGMDPDVGDSKGRTALHIAASKGYEDCVLVLLKQACNVNIKDAQGNTALWNAIAARHHKIFNILYHFARVSSPHHAAGDLLCLAARRGDLDTLRELLKHGLAVDSEDRDGATALRVALAEGHADVARLLVLNGASVDRAASHNEQQAAAAVSVDELRELMKTRELAHPVTIVVDSPSPAAAAVIREVGSSGDSRNGRRQSARSDGAHWPRVSIYRGHPFVRNRSSEAGKLINLPGTMEEFRIIIEEKLKVDARKTLIMNDEGAEIDSIDVIRDNDKLFIVTEEHMTAVASMDSVSGS | Function: Probable inward-rectifying potassium channel. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 94784
Sequence Length: 855
Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids. The pore-forming region H5 is enclosed by the transmembrane segments S5 and S6 in the Shaker-type (1P/6TM) and contains the GYGD signature motif which seems to be involved in potassium selectivity (By similarity).
Subcellular Location: Membrane
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P47197 | MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWIRAIQMVANSLKQRGPGEDAMDYKCGSPSDSSTSEMMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGDLFFHLSRERVFTEDRARFYGAEIVSALEYLHSTDVVYRDIKLENLMLDKDGHIKITDFGLSKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLGPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGSLELDQRTHFPQFSYSASIRE | Function: AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinases, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.
PTM: Phosphorylation on Thr-309 and Ser-474 is required for full activity.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 55543
Sequence Length: 481
Domain: Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PIK3CA) results in its targeting to the plasma membrane.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9P4U9 | MLNRFSYSSNAWHNLRVDGPDADGIAVIVLARSQSRNALTLPMLTDMVQLLSAMDADDSVKCIVFTGEGPFFCSGVDLTEGFGEIGKTRDTHRDAGGKLALAIHNCRKPTIAAINGTAVGVGITMTLPMSIRIAAKTAKISFPFVRRGIVADAASSFYLPRLVGYGRALHLFTTGALYPAESGLLHGLFSETVNPASSTLPRALEVARDIAVNASQVGVYLTRDLVYRSPRSPEQAHLLESAALYTRYQSRDFEEGVKSFLEKRKPRFQDTMREQSSEGVLERGDCVVGLASKPKL | Function: Enoyl-CoA hydratase; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible for Japanese pear black spot disease by the Japanese pear pathotype . AK-toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA) . On cellular level, AK-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment . The acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety . Part of the EDA biosynthesis occurs in the peroxisome since these 3 enzymes are localized in peroxisomes . The exact roles of the 3 enzymes, as well as of additional AK-toxin clusters enzymes, including AKT4, AKT6 and AKTS1, have still to be elucidated . The Cytochrome P450 monooxygenase AKT7 on the other side functions to limit production of EDA and AK-toxin, probably via the catalysis of a side reaction of EDA or its precursor .
Catalytic Activity: a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O
Sequence Mass (Da): 32127
Sequence Length: 296
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Peroxisome
EC: 4.2.1.17
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Q9Y243 | MSDVTIVKEGWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVADRLQRQEEERMNCSPTSQIDNIGEEEMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDCMDNERRPHFPQFSYSASGRE | Function: AKT3 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis.
PTM: Phosphorylation on Thr-305 and Ser-472 is required for full activity.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 55775
Sequence Length: 479
Domain: Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI(3)K) results in its targeting to the plasma membrane.
Subcellular Location: Nucleus
EC: 2.7.11.1
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Q63484 | MSDVTIVKEDWVQKRGEYIKNWRPRYFLLKTDGSFIGYKEKPQDVDLPYPLNNFSVAKCQLMKTERPKPNTFIIRCLQWTTVIERTFHVDTPEEREEWTEAIQAVADRLQRQEEERMNCSPTSQIDNIGEEEMDASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSSDAKSLLSGLLIKDPNKRLGGGPDDPKEIMRHSFFSGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKDDDDGMDCMDNERRPHFPQFSYSASGRE | Function: AKT3 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis (By similarity).
PTM: Phosphorylation on Thr-305 and Ser-472 is required for full activity.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 55796
Sequence Length: 479
Domain: Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI(3)K) results in its targeting to the plasma membrane.
Subcellular Location: Nucleus
EC: 2.7.11.1
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V5XYR2 | MSFCDDREGQRALRILQARLIRSPDACSFALTAVSSLLRKYSIDPRRIGRLEVGTESLVDKSKSIKSFVMQLFEESGNFDIEGVDTVNACYGGTNALFNAVNWVESSAWDGRDAIVVASDISLYGKGNARPTGGAGCVAMLVGPDAPIAFEPGRRGSYMAHTYDFYKPDFTTEYPYINGKHSIECYIQAVEACYRAYTKRERRATERLEEERPDHQAGYETPLDRFDYLCFHSPTNKLVSKSYARLLYVDYLENPANPIFAEVPDSIREVEYRASLTDKSIEKTFMGLAQERFARCVQPSTEIPNMCGNMYSASVYGSLCSLLCNVNSETLLGKRITIFSYGSGLASSMFSLKVRGSTKQMAEKLDVHRRLVDRVVVSPEDVRERAYLKKCFKPKGGAGPIPADVYSLAEVDELFRRVYTVKS | Function: Hydroxymethylglutaryl-CoA synthase-like protein; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible for Japanese pear black spot disease by the Japanese pear pathotype . AK-toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA) . On cellular level, AK-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment . The acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety . Part of the EDA biosynthesis occurs in the peroxisome since these 3 enzymes are localized in peroxisomes . The exact roles of the 3 enzymes, as well as of additional AK-toxin clusters enzymes, including AKT4, AKT6 and AKTS1, have still to be elucidated . The Cytochrome P450 monooxygenase AKT7 on the other side functions to limit production of EDA and AK-toxin, probably via the catalysis of a side reaction of EDA or its precursor .
Sequence Mass (Da): 47372
Sequence Length: 423
Pathway: Mycotoxin biosynthesis.
EC: 2.3.3.-
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V5XZS6 | MKTTIDMQVLYVTCTVLAALILGYIQAMIIYRLWFHPLSKYPGPWLARISNLYSAYYAWSGDLHIDMWRCHQKYGDFVRYAPNRLLVNTNTGLKAIYGFNKHVQKSTTYNVMVHRAPSSLTMTDPQESAQRRRIVGQGFSSTAINQYESIIMEHVQRLATQLVRRGSDRGSGWSAAQNMSDWGNHFSFDVISDIVFGARHETIGKPDNRYVLGCIDGANIRTSVLFQAAELTFGRVDRYLFPKSIESRNRFTPFVSSLVRTRLQSHDASRNDAFSLLVRAKDPETSEGLSMDAIGGECTTLVMAGSDITSTVIASTLFYLSTHTESYDRVKSELQQAFPTADDVRLGHRLNSCRYLRACIEESLRLSPPVGGAPWRRVVSDGLLVDGQSIPAGCDVGTSVYALHHNSAYFKAPFVFRPSRWLTDSGAQGRESRDIRLAQSAFAPFSIGPRSCLGKGMAYAELTLVLATLLSKYDMRAAEGPMRGIGGGRVGAPWGRHRENEFQLTGHVTSAKTGPYVEFKKS | Function: Cytochrome P450 monooxygenase; part of the gene clusters that mediate the biosynthesis of the host-selective toxins (HSTs) AK-toxins responsible for Japanese pear black spot disease by the Japanese pear pathotype . AK-toxins are esters of 9,10-epoxy 8-hydroxy 9-methyldecatrienoic acid (EDA) . On cellular level, AK-toxins affect plasma membrane of susceptible cells and cause a sudden increase in loss of K(+) after a few minutes of toxin treatment . The acyl-CoA ligase AKT1, the hydrolase AKT2 and enoyl-CoA hydratase AKT3 are all involved in the biosynthesis of the AK-, AF- and ACT-toxin common 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid (EDA) structural moiety . Part of the EDA biosynthesis occurs in the peroxisome since these 3 enzymes are localized in peroxisomes . The exact roles of the 3 enzymes, as well as of additional AK-toxin clusters enzymes, including AKT4, AKT6 and AKTS1, have still to be elucidated . The Cytochrome P450 monooxygenase AKT7 on the other side functions to limit production of EDA and AK-toxin, probably via the catalysis of a side reaction of EDA or its precursor .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58179
Sequence Length: 522
Pathway: Mycotoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q2NVW1 | MRWSCHPMSSVTSRLRSATADTFALVVYCFFTGMAIEILLSGMSLQQSLSSRVLAIPVNVIIAWPFGQYRDAVVSLASRHGPKQFWTRNLADLLAMSVFNHRSMRRFFLRWGWSGGSCSRRWSAMR | Function: Exports L-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14381
Sequence Length: 126
Subcellular Location: Cell inner membrane
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Q0WJC2 | MTMFSTGPRWRSAVADTFALVVYCFVIGMAIEVVISGMTFRQSLSSRLLSIPVNILIAWPYGMYRDAFIRFAQRHAGQRFWARNLADLLAYVSFQSPVYAMILWSVGADFEQMISAVASNAVVSMVMGVAYGYFLEYCRRLFRVAGYV | Function: Exports L-alanine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16746
Sequence Length: 148
Subcellular Location: Cell inner membrane
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Q54MJ7 | MFKRSLKVLLSNPPINRVKPSSTIIQPLSNTTTTTIINNNNITNFEKMTHKKSMTIDNICQNVRNAQYAVRGELVIRAEAISHQLQKQKTEGTKTLPFEEIVYCNIGNPQQLKQKPLTYFRQVVSLVECPDLLDNPYVEKIYPADVISRAKEILGSINNTTGAYSNSQGIGLVLRSVADFIERRDGHKSDPSEIFLTDGASVGVQRILKLLIKDRSDGILIPIPQYPLYSATIELYNGSQLGYLLNEEKGWSLEISQLEHSYNDAVSKGINPRALVIINPGNPTGQCLDRANMEEIVKFCLEKNVVLLADEVYQENVYVKESKPFISFKKVVKDMGGDYADLEMVSFHSVSKGFVGECGKRGGYMELNGVTQDVKAEIYKLASIGLCPNVIGQLVVDLMVRPPVAGEQSHDLYLKERDNIYESLKKRANLLTNALNNLEGVTCNPSEGAMYAFPQIRLPAKAVEYANSIGKAPDAYYCIQLLEATGICVVPGSGFGQKDGTWHFRTTFLPSEEAIEGVCKRIADFHQSFMNKYK | Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Mass (Da): 59495
Sequence Length: 534
Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
Subcellular Location: Mitochondrion matrix
EC: 2.6.1.2
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P52893 | MLSLSAKNHFTVSNSITHVIKSYHIRTLTSSAEKMPHITTPFSTSASSTKLKAFRKVRPVLQRHSSSWIVAQNHRRSLSGQSSLNDLRHLNRFPHHTLKTSNNEFYPAEQLTLEDVNENVLKAKYAVRGAIPMRAEELKAQLEKDPQSLPFDRIINANIGNPQQLQQKPLTYYRQVLSLLQYPELLNQNEQQLVDSKLFKLDAIKRAKSLMEDIGGSVGAYSSSQGVEGIRKSVAEFITKRDEGEISYPEDIFLTAGASAAVNYLLSIFCRGPETGVLIPIPQYPLYTATLALNNSQALPYYLDENSGWSTNPEEIETVVKEAIQNEIKPTVLVVINPGNPTGAVLSPESIAQIFEVAAKYGTVVIADEVYQENIFPGTKFHSMKKILRHLQREHPGKFDNVQLASLHSTSKGVSGECGQRGGYMELTGFSHEMRQVILKLASISLCPVVTGQALVDLMVRPPVEGEESFESDQAERNSIHEKLITRAMTLYETFNSLEGIECQKPQGAMYLFPKIDLPFKAVQEARHLELTPDEFYCKKLLESTGICTVPGSGFGQEPGTYHLRTTFLAPGLEWIKKWESFHKEFFDQYRD | Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Mass (Da): 66422
Sequence Length: 592
Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
Subcellular Location: Mitochondrion matrix
EC: 2.6.1.2
|
F4I7I0 | MRRFVIGQAKNLIDQSRRRQLHHHKNLSFVSLIPPFSAPSDSSSRHLSSSSSSDMSASDSSSSLPVTLDTINPKVIKCEYAVRGEIVNIAQKLQEDLKTNKDAYPFDEIIYCNIGNPQSLGQQPITFFREVLALCSYTALLDESATHGLFSSDSIERAWKILDQIPGRATGAYSHSQGIKGLRDAIADGIEARDGFPADPNDIFMTDGASPGVHMMMQLLITSEKDGILCPIPQYPLYSASIALHGGTLVPYYLDEASGWGLEISELKKQLEDARSKGITVRALAVINPGNPTGQVLSEENQRDVVKFCKQEGLVLLADEVYQENVYVPDKKFHSFKKVARSMGYGEKDLALVSFQSVSKGYYGECGKRGGYMEVTGFTSDVREQIYKMASVNLCSNISGQILASLIMSPPKPGDDSYESYIAEKDGILSSLARRAKTLEEALNKLEGVTCNRAEGAMYLFPCLHLPQKAIAAAEAEKTAPDNFYCKRLLKATGIVVVPGSGFRQVPGTWHFRCTILPQEDKIPAIVDRLTAFHQSFMDEFRD | Function: Is the major alanine aminotransferase in roots that catalyzes the conversion of alanine to pyruvate . Involved in the rapid conversion of alanine to pyruvate during recovery from low-oxygen stress .
PTM: The N-terminus is blocked.
Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Mass (Da): 59821
Sequence Length: 543
Pathway: Photosynthesis; C4 acid pathway.
Subcellular Location: Mitochondrion
EC: 2.6.1.2
|
A4IFH5 | MALRAGEHSQEAANGLKEKVLTLDSMNPYVRRVEYAVRGPIVQRALELEQELRQGVKKPFTEVIRANIGDAQAMGQIPITFPRQVLALCVHPDLLNSPDFPDDAKRRAERILQACGGHSLGAYSISAGVQMIREDVARYIERRDGGIPADPNNIFLSTGASDAIVTVLKLLVTGEGRTRTGVLIPIPQYPLYSAALAEFNAVQVDYYLDEERAWALDVAELRRALRQARDHCRPRALCVINPGNPTGQVQTRECIEDVIRFAYEEKLFLLADEVYQDNVYAESSQFHSFKKVLTEMGPPYAAQQELASFHSISKGYMGECGFRGGYVEVVNMDAAVKQQMQKLRSVRLCPPTPGQVLLDVAVSPPAPSDPSFPRFQAERRAVLAELAAKAKLTEQVFNEAPGIRCNPVQGAMYSFPRVQLPPRAVQRAQELGLAPDMFFCLRLLEETGICVVPGSGFGQREGTYHFRMTILPPMEKLRPLLEKLSQFHAKFTREYS | Function: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles (By similarity).
Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Mass (Da): 55275
Sequence Length: 496
Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.6.1.2
|
P24298 | MASSTGDRSQAVRHGLRAKVLTLDGMNPRVRRVEYAVRGPIVQRALELEQELRQGVKKPFTEVIRANIGDAQAMGQRPITFLRQVLALCVNPDLLSSPNFPDDAKKRAERILQACGGHSLGAYSVSSGIQLIREDVARYIERRDGGIPADPNNVFLSTGASDAIVTVLKLLVAGEGHTRTGVLIPIPQYPLYSATLAELGAVQVDYYLDEERAWALDVAELHRALGQARDHCRPRALCVINPGNPTGQVQTRECIEAVIRFAFEERLFLLADEVYQDNVYAAGSQFHSFKKVLMEMGPPYAGQQELASFHSTSKGYMGECGFRGGYVEVVNMDAAVQQQMLKLMSVRLCPPVPGQALLDLVVSPPAPTDPSFAQFQAEKQAVLAELAAKAKLTEQVFNEAPGISCNPVQGAMYSFPRVQLPPRAVERAQELGLAPDMFFCLRLLEETGICVVPGSGFGQREGTYHFRMTILPPLEKLRLLLEKLSRFHAKFTLEYS | Function: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles (By similarity).
Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Mass (Da): 54637
Sequence Length: 496
Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.6.1.2
|
P13191 | QELASFHSVSKGFMGECGFR | Function: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles (By similarity).
PTM: Glycation of Lys-11 inactivates the enzyme.
Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Mass (Da): 2218
Sequence Length: 20
Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.6.1.2
|
P25409 | MASRVNDQSQASRNGLKGKVLTLDTMNPCVRRVEYAVRGPIVQRALELEQELRQGVKKPFTEVIRANIGDAQAMGQRPITFFRQVLALCVYPNLLSSPDFPEDAKRRAERILQACGGHSLGAYSISSGIQPIREDVAQYIERRDGGIPADPNNIFLSTGASDAIVTMLKLLVSGEGRARTGVLIPIPQYPLYSAALAELDAVQVDYYLDEERAWALDIAELRRALCQARDRCCPRVLCVINPGNPTGQVQTRECIEAVIRFAFKEGLFLMADEVYQDNVYAEGSQFHSFKKVLMEMGPPYSTQQELASFHSVSKGYMGECGFRGGYVEVVNMDAEVQKQMGKLMSVRLCPPVPGQALMDMVVSPPTPSEPSFKQFQAERQEVLAELAAKAKLTEQVFNEAPGIRCNPVQGAMYSFPQVQLPLKAVQRAQELGLAPDMFFCLCLLEETGICVVPGSGFGQQEGTYHFRMTILPPMEKLRLLLEKLSHFHAKFTHEYS | Function: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles (By similarity).
Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Mass (Da): 55110
Sequence Length: 496
Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.6.1.2
|
Q6NYL5 | MLSKRSLRVLKWGRCEAAYAAAYPKVPDWVLNFSPLPSLSSPHRDFSAFPAAQSEHMQQKMSENGAIPRQGKVLTVDTMNANVKKVDYAVRGPIVQRAVQIEKELKEGVKKPFDEVIKANIGDAHAMGQRPITFFRQVMALCTYPQLLDDNKFPEDAKNRARRILQSCGGNSIGAYTTSQGIDCVRQDVAKYIERRDGGIPSDPDNIYLTTGASDGIVTILKLLTAGEGLTRTGVMISIPQYPLYSASIAELGAVQINYYLNEEKCWSLDISELQRSLQAARKHCNPRVLCIINPGNPTGQVQSRQCIEDVIQFAAKENLFLMADEVYQDNVYAKGCEFHSFKKVLFEMGPEYSKKVELASFHSTSKCYMGECGFRGGYMEVINMDADVKAQLTKLVSVRLCPPAPGQALMDLVVNPPQPGEPSHQTFMQERTAVLSALAEKAKLTEQILNTVPGISCNPVQGAMYSFPRITLPERAISEAKAKGQAPDMFYCMKLLEETGICLVPGSGFGQREGTYHFRMTILPPTDKLKLMLNKLKDFHQRFTQQYS | Function: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate.
Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Mass (Da): 61092
Sequence Length: 549
Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
EC: 2.6.1.2
|
Q8TD30 | MQRAAALVRRGCGPRTPSSWGRSQSSAAAEASAVLKVRPERSRRERILTLESMNPQVKAVEYAVRGPIVLKAGEIELELQRGIKKPFTEVIRANIGDAQAMGQQPITFLRQVMALCTYPNLLDSPSFPEDAKKRARRILQACGGNSLGSYSASQGVNCIREDVAAYITRRDGGVPADPDNIYLTTGASDGISTILKILVSGGGKSRTGVMIPIPQYPLYSAVISELDAIQVNYYLDEENCWALNVNELRRAVQEAKDHCDPKVLCIINPGNPTGQVQSRKCIEDVIHFAWEEKLFLLADEVYQDNVYSPDCRFHSFKKVLYEMGPEYSSNVELASFHSTSKGYMGECGYRGGYMEVINLHPEIKGQLVKLLSVRLCPPVSGQAAMDIVVNPPVAGEESFEQFSREKESVLGNLAKKAKLTEDLFNQVPGIHCNPLQGAMYAFPRIFIPAKAVEAAQAHQMAPDMFYCMKLLEETGICVVPGSGFGQREGTYHFRMTILPPVEKLKTVLQKVKDFHINFLEKYA | Function: Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate.
Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Mass (Da): 57904
Sequence Length: 523
Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
EC: 2.6.1.2
|
P11884 | MLRAALSTARRGPRLSRLLSAAATSAVPAPNQQPEVFCNQIFINNEWHDAVSKKTFPTVNPSTGEVICQVAEGNKEDVDKAVKAAQAAFQLGSPWRRMDASDRGRLLYRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDVYDEFVERSVARAKSRVVGNPFDSRTEQGPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS | Function: Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage.
Catalytic Activity: an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH
Sequence Mass (Da): 56488
Sequence Length: 519
Pathway: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.
Subcellular Location: Mitochondrion matrix
EC: 1.2.1.3
|
P47771 | MPTLYTDIEIPQLKISLKQPLGLFINNEFCPSSDGKTIETVNPATGEPITSFQAANEKDVDKAVKAARAAFDNVWSKTSSEQRGIYLSNLLKLIEEEQDTLAALETLDAGKPYHSNAKGDLAQILQLTRYFAGSADKFDKGATIPLTFNKFAYTLKVPFGVVAQIVPWNYPLAMACWKLQGALAAGNTVIIKPAENTSLSLLYFATLIKKAGFPPGVVNIVPGYGSLVGQALASHMDIDKISFTGSTKVGGFVLEASGQSNLKDVTLECGGKSPALVFEDADLDKAIDWIAAGIFYNSGQNCTANSRVYVQSSIYDKFVEKFKETAKKEWDVAGKFDPFDEKCIVGPVISSTQYDRIKSYIERGKREEKLDMFQTSEFPIGGAKGYFIPPTIFTDVPQTSKLLQDEIFGPVVVVSKFTNYDDALKLANDTCYGLASAVFTKDVKKAHMFARDIKAGTVWINSSNDEDVTVPFGGFKMSGIGRELGQSGVDTYLQTKAVHINLSLDN | Function: Cytoplasmic aldehyde dehydrogenase involved in ethanol oxidation. Required for pantothenic acid production through the conversion of 3-aminopropanal to beta-alanine, an intermediate in pantothenic acid (vitamin B5) and coenzyme A (CoA) biosynthesis.
Catalytic Activity: an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH
Sequence Mass (Da): 55188
Sequence Length: 506
Subcellular Location: Cytoplasm
EC: 1.2.1.3
|
Q54DG1 | MSTSAAATLPLSVISKNLRKVFLSQKTRKIDWRYSQLKAIKKMMSENKDNITAAVKKDLGKHEFEIHQTEIVMIQTELDETISHLESWNKTEKVYSPLHFKPASSYILKEPLGVVLIMSPWNYPVNLALIPLIGAIAGGNCALLKLSRHSYNISKLLHGLLTKYLDPECFEFDCEGGAPYITELLEYKWDHIFFTGSVKVGKIVYQAAAKFLTPVTLELGGKNPCIVDKDTDIKLTARRLIWGKCWNAGQTCIGLDYLIVHKSILEPLIEEFKVVLKEFFGEDIKKSTSFARIISSAAAERLQQLFSMGKVVIGGEADIAERYIAPTVIVDPDLDSPLMQDEIFGPVLPIVTYENIDECLEFIQNRPHALTLYLFSRDQAIQDKVLDGTQSGSLMINDTLLHFTNPNLPFGGIGDSGIGSYHGKGTFDIFVHKRGLVQSTTKKFLDLPLRYPPYTPFSDNVAGKILGSGW | Catalytic Activity: an aldehyde + H2O + NADP(+) = a carboxylate + 2 H(+) + NADPH
Sequence Mass (Da): 52563
Sequence Length: 470
Subcellular Location: Cytoplasm
EC: 1.2.1.5
|
P46367 | MFSRSTLCLKTSASSIGRLQLRYFSHLPMTVPIKLPNGLEYEQPTGLFINNKFVPSKQNKTFEVINPSTEEEICHIYEGREDDVEEAVQAADRAFSNGSWNGIDPIDRGKALYRLAELIEQDKDVIASIETLDNGKAISSSRGDVDLVINYLKSSAGFADKIDGRMIDTGRTHFSYTKRQPLGVCGQIIPWNFPLLMWAWKIAPALVTGNTVVLKTAESTPLSALYVSKYIPQAGIPPGVINIVSGFGKIVGEAITNHPKIKKVAFTGSTATGRHIYQSAAAGLKKVTLELGGKSPNIVFADAELKKAVQNIILGIYYNSGEVCCAGSRVYVEESIYDKFIEEFKAASESIKVGDPFDESTFQGAQTSQMQLNKILKYVDIGKNEGATLITGGERLGSKGYFIKPTVFGDVKEDMRIVKEEIFGPVVTVTKFKSADEVINMANDSEYGLAAGIHTSNINTALKVADRVNAGTVWINTYNDFHHAVPFGGFNASGLGREMSVDALQNYLQVKAVRAKLDE | Function: Potassium-activated aldehyde dehydrogenase involved in acetate formation during anaerobic growth on glucose.
Catalytic Activity: acetaldehyde + H2O + NADP(+) = acetate + 2 H(+) + NADPH
Sequence Mass (Da): 56724
Sequence Length: 519
Subcellular Location: Mitochondrion matrix
EC: 1.2.1.-
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O06478 | MFQYEELNKQFIGGKWQEGSSPNVLENKNPYTQKTFTTFRKATADDVDEAYRAAALAKKKWDAVNPFEKRTILEKAVTYIEENEEAIIYLIMEELGGTRLKAAFEIGLVKNIIKEAATFPIRMEGKILPSTIDGKENRLYRVPAGVVGVISPFNFPFFLSMKSVAPALGAGNGVVLKPHEETPICGGTLIAKIFENAGIPAGLLNVVVTDIAEIGDSFVEHPVPRIISFTGSTKVGSYIGQLAMKHFKKPLLELGGNSAFIVLEDADIEYAVNAAVFSRFTHQGQICMSANRVLVHSSIYDKFLELYQAKVESLKVGDPMDPDTIIGPLINSRQTDGLMKTVEQAIEEGAVPVKLGGFNGTIVEPTILKDVKPFMSIAKEELFGPVVSFMKFDSEDEAVDIANETPFGLSGAVHTSNLERGVAFAKRIETGMIHVNDTTINDEPNVAFGGEKQSGLGRLNGEWSLEEFTTLKWISVQHEKRSFPY | Function: A benzaldehyde dehydrogenase able to act on substrates with 3- and 4-hydroxy and methoxy substitutions; converts vanillin (4-hydroxy-3-methoxybenzaldehyde) to vanillic acid in vitro . The physiological substrate is unknown .
Catalytic Activity: benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH
Sequence Mass (Da): 53321
Sequence Length: 485
EC: 1.2.1.28
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P54115 | MTKLHFDTAEPVKITLPNGLTYEQPTGLFINNKFMKAQDGKTYPVEDPSTENTVCEVSSATTEDVEYAIECADRAFHDTEWATQDPRERGRLLSKLADELESQIDLVSSIEALDNGKTLALARGDVTIAINCLRDAAAYADKVNGRTINTGDGYMNFTTLEPIGVCGQIIPWNFPIMMLAWKIAPALAMGNVCILKPAAVTPLNALYFASLCKKVGIPAGVVNIVPGPGRTVGAALTNDPRIRKLAFTGSTEVGKSVAVDSSESNLKKITLELGGKSAHLVFDDANIKKTLPNLVNGIFKNAGQICSSGSRIYVQEGIYDELLAAFKAYLETEIKVGNPFDKANFQGAITNRQQFDTIMNYIDIGKKEGAKILTGGEKVGDKGYFIRPTVFYDVNEDMRIVKEEIFGPVVTVAKFKTLEEGVEMANSSEFGLGSGIETESLSTGLKVAKMLKAGTVWINTYNDFDSRVPFGGVKQSGYGREMGEEVYHAYTEVKAVRIKL | Function: Cytosolic aldehyde dehydrogenase which utilizes NADP(+) as the preferred coenzyme. Performs the conversion of acetaldehyde to acetate.
Catalytic Activity: acetaldehyde + H2O + NADP(+) = acetate + 2 H(+) + NADPH
Sequence Mass (Da): 54414
Sequence Length: 500
Pathway: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.-
|
Q94688 | FPLLMQAWKLGPALACGNTVVMKTAEQTPLTALYVAALAKEAGFPPGVINIISGYGPTAGAAISEHMDVDKVAFTGSTETAHIVMEAAAKSNLKRVSLELGGKSPMIVLADSDLDFAVDTCHHGLFFNMGQCCCAGSRIYVQEGVYDEFVKKSVERAKKRTVGDPFTEGIEQGPQIDTEQFNKINRMIEEGKQSGAKLLCGGKRWGDKGYYIEPTVFSDVPDDSTIGS | Catalytic Activity: an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH
Sequence Mass (Da): 24460
Sequence Length: 228
Pathway: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.
EC: 1.2.1.3
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P22281 | MLATRNLVPIIRASIKWRIKLSALHYCMSDAETSEALLEDNSAYINNEKHNLFLEKIFSDYQPFKHDNRTQVSCSQHMRDYRPLLTLSSATRSVLFSLLASDMSIILSISPNTGILLCIGHLLASDIEDVVIVLSRGSPLVDLASTRIFKLAQNGTLRFAIKRTTFQELRFLRKSKDENVMEAATRGIITIRQLYYENKVLPLRFTGNVATHIEENLEFEEQITWRTHVDSSIFPNTRCAYPSGYGPSAKIPCLSHKPNDILAYTGSTLVGRVVSKLAPEQVMKKVTLESGGKSTMAVFIQHDVTWAVENTQFGVFDRQGQCCIAQSGYTVHRSTLSQIVENNLEKDPSYVLHVDTESDIRGPFILKIHFESIPRRINSAKAENSKVLCGGPRENSVYLYPTLSATLTDECRIMKEEVFAPIITILCVKTVDEAIQRGNNSKFGLAAYVTKENVHGIILSTALKTVKLFIICVHLASYQIPFGGNKNSGMGAELGKRALENYTEGNHVLPVSLVKETLAPNTETASPARWPIH | Catalytic Activity: an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH
Sequence Mass (Da): 59507
Sequence Length: 533
Pathway: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.
Subcellular Location: Mitochondrion matrix
EC: 1.2.1.3
|
P32872 | MSKSKTKTDKRNQSSLSRIKLSALHYCMSDAEPSIAYLQDNSAFINNEWHNLVLEKIFPVYNPSTEEDITQVSEKSQHDSTEEDITQVSEKSQHDDDKAVVDISERGRLLNILADLIERDRDILAAIEHLDNGKPFDEAYLLDLASVLKELRYTAGWADKLHGTLRFAITIPTFQDLRFLRYTRHEPVGVCGEIIPWNIPLLMYIWKIGPALAAGNTVVLKPEELTPLTALTVATLIKEAGFPPGVVNVVSGYGPTAGAACLSHKDNDKLAFTGSTLVGKVVMKAAAKSNLKKVTLELGGKSPMIVFIDADLDWAVENAHFGVFFNQGQCCIAQSRITVHESIYDEIVERDLEKAKKQVLGNPFESDTRYGPQILKIEFDSIPRLINSAKAEGAKVLCGGGRDDSCVGYYIQPTVFADVTDEMRIAKEEIFGPVITISRFKSVDEAIKRVDNTKYGLAAYVFTKDKAIRISAALKAGTVWVNCVHVASYQIPFGGNKNSGMGRELGEYGLE | Catalytic Activity: an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH
Sequence Mass (Da): 56466
Sequence Length: 511
Pathway: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.
Subcellular Location: Mitochondrion matrix
EC: 1.2.1.3
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O74187 | MPSIFTHQWDTPVYKGSTSINTGLFINGEFVDGVKNTTIDVVNPANGKLITKISEATEADIDIAVEAAHKAFETTWGLNCSGSKRGDMLYKLAQLMEKNIDDLSAIEALDNGKTFLWAKSVDLSLSISTIKHYAGWADKNFGQVIETDEKKLTYSRHEPIGVVGQIIPWNFPLLMLAWKIGPALATGNCIVLKPSEFTPLSALRMCALIQEAGFPPGVVNVVTGYGSTTGQAISSHMKIDKVAFTGSTLVGRKVMEAAAKSNLKNVTLELGGKSPVVIFDDADLEQSVNWTAHGLFWNHGQACCAGTRIFVQEGIYDKFLQKFTDKIKEIKLGDPFGLGIDQGPQVSQIQYDRIMSYIESGRAEGATVHVGGERHGNEGYFIQPTIFTDTTPDMKIVKEEIFGPVGAVIKFKDGKEVIKQANDSNYGLAAAVFSQDINKAIETAHAFKAGTAWVNCANTIDAGVPFGGYKQSGIGRELGEYALHNYTNVKAVHVNLNWKM | Catalytic Activity: an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH
Sequence Mass (Da): 54395
Sequence Length: 500
Pathway: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.
EC: 1.2.1.3
|
P42041 | MTSVKLSTPQTGEFEQPTGLFINNEFVKAVDGKTFDVINPSTEEVICSVQEATEKDVDIAVAAARKAFNGPWRKETPENRGKLLNKLADLFEKNADLIAAVEALDNGKAFSMAKNVDVPAAAGCLRYYGGWADKIEGKVVDTAPDSFNYIRKEPIGVCGQIIPWNFPILMWSWKIGPAIATGNTVVLKTAEQTPLSAYIACKLIQEAGFPPGVINVITGFGKIAGAAMSAHMDIDKIAFTGSTVVGRQIMKSAAGSNLKKVTLELGGKSPNIVFADADLDEAIHWVNFGIYFNHGQACCAGSRIYVQEEIYDKFIQRFKERAAQNAVGDPFAADTFQGPQVSQLQFDRIMGYIEEGKKSGATIETGGNRKGDKGYFIEPTIFSNVTEDMKIQQEEIFGPVCTISKFKTKADVIKIGNNTTYGLAAAVHTSNLTTAIEVANALRAGTVWVNSYNTLHWQLPFGGYKESGIGRELGEAALDNYIQTKTVSIRLGDVLFG | Catalytic Activity: an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH
Sequence Mass (Da): 53916
Sequence Length: 497
Pathway: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.3
|
P50923 | LQDIINEFGGAMPQTFGVPVEEIVRGIKMGVRKVNIDTDCRMRMTGQFRRIAEQNKAEFDPRKFLKPAMDAMRDLCKARLEAFGTAGHASKIKVIPMDDMAKRYASGSLAPKTN | Cofactor: Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Function: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 12747
Sequence Length: 114
Pathway: Carbohydrate biosynthesis; Calvin cycle.
EC: 4.1.2.13
|
O65581 | MSAFVGKYADELIKTAKYIATPGKGILAADESTGTIGKRFASINVENIESNRQALRELLFTSPGTFPCLSGVILFEETLYQKTTDGKPFVELLMENGVIPGIKVDKGVVDLAGTNGETTTQGLDSLGARCQEYYKAGARFAKWRAVLKIGATEPSELSIQENAKGLARYAIICQENGLVPIVEPEVLTDGSHDIKKCAAVTETVLAAVYKALNDHHVLLEGTLLKPNMVTPGSDSPKVAPEVIAEYTVTALRRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLDVLKPWTLTFSFGRALQQSTLKAWAGKTENVAKAQATFLTRCKGNSDATLGKYTGGASGDSAASESLYEEGYKY | Function: Fructose-bisphosphate aldolase that plays a key role in glycolysis and gluconeogenesis.
PTM: S-glutathionylated at Cys-68 and Cys-173.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 38294
Sequence Length: 358
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
Subcellular Location: Cytoplasm
EC: 4.1.2.13
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P14540 | MGVEQILKRKTGVIVGEDVHNLFTYAKEHKFAIPAINVTSSSTAVAALEAARDSKSPIILQTSNGGAAYFAGKGISNEGQNASIKGAIAAAHYIRSIAPAYGIPVVLHSDHCAKKLLPWFDGMLEADEAYFKEHGEPLFSSHMLDLSEETDEENISTCVKYFKRMAAMDQWLEMEIGITGGEEDGVNNENADKEDLYTKPEQVYNVYKALHPISPNFSIAAAFGNCHGLYAGDIALRPEILAEHQKYTREQVGCKEEKPLFLVFHGGSGSTVQEFHTGIDNGVVKVNLDTDCQYAYLTGIRDYVLNKKDYIMSPVGNPEGPEKPNKKFFDPRVWVREGEKTMGAKITKSLETFRTTNTL | Cofactor: Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Function: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 39621
Sequence Length: 359
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
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Q8L638 | MGKLAVAAITSLWVIPMSIIVNHIVPEPYMDEIFHVPQAQQYCNGNFRSWDPMITTPPGLYYLSLAHVASLFPGMLLMENTSQSFSEACSTSVLRSTNAVSAVLCGVLVYEIIRFLGPNLSDRKATFMALVMSLYPLHWFFTFLYYTDVASLTAVLAMYLTCLKRRYVLSALFGTLAVFIRQTNVVWMLFVACSGILDFTLDSSKQKGKQEVNQELHQSSNKKGATLRSNLRKRKSDISSDTSDPFNHGQTVPSTEDTSDLVYDIYTVISTSWNLKWRILIKFSPFIFVVVAFGIFILWNGGIVLGAKEAHVVSLHFAQIMYFSLVSALFTAPLHFSVNQLRHQFHQLHRNWSLSLILTLVALVAGFVSVHFFSLAHPYLLADNRHYPFYLWRKIINAHWLMKYILVPVYVYSWFSILTLLAKTRRQTWILVYFLATCGVLVPTPLIEFRYYTIPFYLFMLHSCVRSSSFATWLLIGTIFVSINVFTMAMFLFRPFKWSHEDGVQRFIW | Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol. Can complement an ALG10-deficient yeast mutant.
Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58439
Sequence Length: 509
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.256
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Q4X162 | MSAVRPVSGISLAARYAVPFVLLLIPLWMAKVNTVVPDPYLDEVFHVPQAQAYWDHRWFHWDPKITTPPGLYIWSYILCAAALVLRGSPKELNAGALRATNVAAAAVFLPWRLQTLLDALRKVRNTRPSGAWLSHTVLNICLFPPLFFFSGLYYTDIVSLLAVIEAYNWDIKRSAGSWSLLKTAVFVATGLTALVLRQTNIFWVAIFLGGLQVVRRLRQSSKASQASSLLQIIQSGFNNELYDPLVSEASFFDYVKTSISLVSVGLRNFIPIIISTVPYLVILAAFGGFVLWNDGVVLGHKEFHTAGLHLSQMLYIWPYFMFFSWPILIFPVINLVLPNSVIPAFFDYGFTKKQKGLPRIWTALVIIPIMLAVVHFNTIIHPFTLADNRHYIFYVFRILRSHPAIRYAAVPTAYFVGGWAVISAFGFSTTKPQPQFVPITKSNELAAAQKGQLKEAARKKEKSERKSKSKKASQVTASPPAQDQFSPEVLARIQEHLAQRQKQQQEVPRASFVLVWLAATALSLVTAPLVEPRYFIIPWVMWRLHLPPQPVPLVYRQQRPRDEREALHADLATNFSLFMETYWFLAINAATGYIFLYKGFEWPQEPGKVQRFMW | Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69670
Sequence Length: 614
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.256
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Q59YV2 | MPLIIPSNDIYISIISKYVAIVIFLIFVIIMFNNITHHLTQPYIDEIFHLRQCQTYCQYNFHHWDNKITTPPGLYILGFIYSEGIKILTRSSSTGGGGGGGHLTCFNDNVLRSINLIGGVVILPRILQQFHNGWSKNSKNQFFWSINIISQPLLFTYYFLFYTDVSSTILIILSLGLINYKLLQYPMLSALVGFMSLWFRQTNIIWIAFIASIFIDRQIKIKTGVIDRIRQFIMKSLTNWNKLLGYIVNIILFVIFLKLNGGITLGDNDNHQIELHIVQVFYCFTFITFFTIPNWLNKSTIKKYYNFIINHIILNLVIGLIIWYIMENFTIVHPFLLADNRHYAFYIYKRLLSQSYLKPLILMAYHFSSFQIISSLIKGGQLSFIGIFSYLIAVGLTLIPSPLFEPRYYITPLIIFNLYINHPHNLLEFIWLNSINLITSYIFLHKGIIW | Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52530
Sequence Length: 450
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.256
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Q6BW42 | MWNVQVVLTSIFVIFCGIVFRLVALNVKDPFIDEIFHLRQCQTYCALRFDIWDHKITTPPGLYILGMVYAEVVKRITFTSESLVSVCENMNVLRSANLFGGLVVLPLIVQGLVEKEKPQFWTVNIVAMPLLFTYYFLFYTDIWASILIVASLALVVRQPLGLITSSYISGIIAFASLWFRQTNIIWIAFIASLLVDKRRREHHNDMGFVQNGINFIRQAVKDWVAVLPFISNIILFAIFVKYNEGITFGDKENHKLNLHIVQVFYCFTFMSMFTWPVWLSIRLIKRYIHFTILGNYGLNTIFTIGSGILIKFIIDNYTVVHPFLLADNRHYTFYIWKRILNREYSNIFMIPIYHFCTWNIIDSLSHNIGGLTPITIITFIGGIFITIIPSPLFEPRYYIVPLLIYRLYVRPTKEKVFGISISRHALEFFWFMMVDVAITVIFLCYEFTWFSEPGKIQRIVW | Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53911
Sequence Length: 461
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.256
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Q8T8L8 | MNGSWKLILPVGFVLYSLPLFLRVNGTSDYVIDEEFHIPQGLAFCRKEFDVWDPKITTFPGLYLIALLLNPLSLCTVTGLRMLSLAGAGINILLLYKIRRRILAGSGGNSYAAHEAITMSVLPPLYFFSHLYYTDTLSLTMVLLFYNYWQQEAHLPAAVFGAASVLMRQTNIVWVCMATGMTVLDTLVNQCARTGRVPKENVRLMGKELWLQLVSSPQLLCNCILSILAKCCFYASIILPFVGFLFINGSIVVGDKSAHEASLHVPQLFYFAIFAAGFGISNTIRQFRPAAELIRRNRVLSLLALLLILVVVHLNTEVHPYLLADNRHYTFYIWSRLYGRFWWFRYAMAPAYLLSICVLFCGLRHMPESFKLMFPLSLFLVLCFQRLLELRYFLVPYILFRLNTRHTRKGYAEWLELGAHLLLNVATFYVYFTKEFYWKNYRTPQRIIW | Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol (By similarity).
Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51783
Sequence Length: 449
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.256
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Q4HZE0 | MGSSSPAQTSNWYELFTGNWLSRPIRAVLVGALALPFVIWPRNQPQNSNPRLLAFFVYLLHLASIPWLYLVTKLVPEPYLDEIFHIPQAQKYCQGRFLEWDDKITTPPGLYLVSLITPGVVQRNGYLDYACSVQNLRAFNVFALAVLAYLALQCRREIEARLYEARFSTRLSNTSQYAVHTAFNIAFFPLLFFFSGLYYTDVASTAAVLVAFLNHLKRIGRDQNSVLSDLVTISLGVFTLFFRQTNVFWVVVFMGGLEAVHAVKTLRPERVDQPVILTLSEQLKHYAWRCSLGDVHDPPLHAMWPDDMIFCVLSLGIAALCNPIRVIRQIWPYITTLLLFGSFVAWNGGVVLVGDKSNHVATIHLPQMLYIWPFFAFFSLPLLIPYALPLANALRRLLYMKTSSWSISSSSNKSLSRKSSSKVSNSKGDVAVDAPGSEYPQPSKELQYFEVVFGSKIFLWPLYLLGTIIFSFGIVHYNTIIHPFTLADNRHYMFYVFRYTIRRAAWIRFALVIPYTVARWMTWGTMAGCSQWFMTMHGPACSAYSKGDGKSPFLNHPAFTNRGASPQQTDAAPPAEVKDLDANQQQELSQALKKDPLLASVEPATTSTGLIFLLATTLSLMTAPLVEPRYFIIPWVMWRLLVPAWKFHDHDSEGVAATLERHPKTKPLLLFLQRYDLRLILETFWFIVINAVTGYIFLTKPYVWKAEDGTVLDGGRLQRFMW | Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82116
Sequence Length: 722
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.256
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P0C147 | MGLFEMLPVSRLVHILVIYAASFAITDVMEDSFIQSRRLLLNRFIYRTGLFLVIIAACIWLAIVNTKVPEPYLDEVFHIPQAEKYLQGRWVEWDDKITTPPGLYLVSYVLVKARTWLSASAAAVNPRYSQDGVTAASLLRESNVYAVMAIAALVLRCRRFIETRHAPTNAKGPHFDSMYSIHTTVNITLFPVIFFFSGLYYTDLWSTATVLWAYENHLKRLTEQTTFWNDINTVILGVTALFMRQTNVFWVVVYFGGLESIHAIKKGAGSSSSKAVKAANIRDLAHALETYWALYAAGNIHDPPLSAASTYDVVWLVLSVAIAAVHNLPRVLRQVWPHISILGLFAGFVAWNGGVVLGDKSNHVATLHLAQMLYIWPLIAFFSAPLMLRCLVSTALYLRKLLQGHSAQPQKERSTKSSQKDWTLTCIGFIQQHTSSGLPFPLWYVSAAVATVIVHKSTIIHPFTLADNRHYMFYVFRYSILRRPEVRYLLVPFYVVCHRLCWHLLGGSSTQDGQRISFIQAPGVETVSSAPPKDTIKLKEEGRPEDGGESLSTGVLWLSATALSLITAPLVEPRYFIVPWVMWRIMVPAWRVQEPRSGEKGLLTRLRSWTQGLDLRLVLETLWFVAINLGTMYMFICRPYHWKDVDGKLMDEGRLQRFMW | Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74905
Sequence Length: 660
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.256
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Q7SA35 | MMDALRVLLETSTFNEVLRGLAISILLAKLTQSTTSSSKSQGSTFITASGFILIYFFARSWLALVNHYAPEPYLDEVFHIPQAQTYCEGRYHEWDNKITTPPGLYLLSVGWHKLVRLVECTPSSLRSNNLVATLLIALIALSCRRRIEAQTAVGIEKSAVSFYAYHTAINIALFPVIFFFSGLYYTDVASTLVMLVAYWNHLNRVASHSEKPGFLNGLWTVVLGVAALFMRQTNVFWVVVYMGGLEAAHVVKGLKPKPVSKNDTPDFVLENIRDSFGFWLRRYAVGDVHDPPVDMAWPDDWALCLLSIGIAALCNPLRVLRQVWPHITIMGLFAGFVAWNGGVVLGDKSNHIATIHLPQMLYIWPFFAFFSAPLLIPRVLSTLADLITHARTPTPSHTTTKDPGRSSWRFTKPSITSKKSSTTKPPQRSGPTPASSSSSSSSFSPDTNSSGRGFRFILDLVLSRKLYYPFYLLATILLSAAIIHYNTIIHPFTLADNRHYMFYIFRYTILRSSLVRLALVAAYTLSRWLIWKRLEGNNPPLRDLAGETGLKITKNKLGWRDEFSASPFVTQDFYGPKTIKTDEQKNIKDKQKEVEEEEEEEEKEDWLIGGAYTTLSLSSTQPSPATSSPPTSTVLLWLLTTTLSLVTAPLVEPRYFILPWVFYRLLVPAMPVSSSLVSSSSSSSFASSTTESGNGDGNDAATAARQQQNGNGKRGLLWNIIRRTDAALALETVWFLAINIGTMYMFLFKPFYWKTASGEMLDGGRLQRFMW | Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86360
Sequence Length: 771
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.256
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Q10254 | MFLGKAIILILWIFLAFTGLLAIQYYVPNPYLDEIFHIAQAQRFCRKDWDWDPAITTPPGLYLVSVALSPFIGCSNVSLRLINWLVGVIGLPWLINDIVSLLNNRKGDVVTYFAYTLSSLPPLWFFSFLYYTDIGSTFFVLLAYDFALRKSAFSSSVSCFFSLWFRQTNIVWMVFIAVTYFASNMSFFNPHLAEATFADVLLTIISFLGVFLKNLRRFSCPILSYGAVFCSFLAFLLWNGSIVLGDKSHHQASIHLSQINYFLWFFFFFSFPSYIIKYLMSHSRRSKLLSAVFSKKSFLIVSVLLLIAHFNTIFHPFILADNRHYLFYVFNRLFRIWWLKYLGPFSYLILYYFFLDISKLQMTSLTFFLLISTTILTLVPAPLVEFRYFLLPFLFWRFHLPLPSGRECLMEYALHMVINSVTLYIFLFRTFIWPSEPNALQRFMW | Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52279
Sequence Length: 445
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.256
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Q4P2W6 | MATSSSDRWPIPLKQHIPTLIFITVTVLTSNLVSRTQPTAYLDEIFHIPQAQQFCSALSSTSLFSAQQVWRQLTSVRYDAQLTTPPGMYAISVGMAKVLPGWECKDVVWLRSTNLVLLLTLPVLVARILGQIEEQARIASAAEDYSPSKTITQNLGKEITRHEIEMLQAKAKLQLPPTPSASHDDLAHIEPPTISIAQAALPAPTGSAAPLLRALKQREASAYTMALACTICFLPPLWFFGFLYYTDLASTWLVLAMLSLYNDLNTSNAHVAPTITGLLIALTSILAVAVRQTNIVWIGFAAAQATLSRVGKHVSHTQQGSDPVTQAIGMVKGAFGDNKKGWWTAVAINAAPMVPVLAVCVLFLRWNGSIVLGEKAAHQVALHLPQMGYFVAFALGFGLFPLLFSLQSMSHKAQDQGPSSSTLATFTHSVRSAVSALIDSTIASPGCILALAAALAGFYIAVDRFTIEHAYMLADNRHYTFYIWRKYRSSYAIPALDGMTIEPKLAVVPLFALALIAWSRALTHHAVNKRTGALFSLLFWMATAAVLVPTPLIEPRYFLMAYLLLRIYSHPYAPCEKQEKSAQLKWIYLALEAATYAAVNVITVGLFVNRPFQWPSHAVDVSRNEHTTMRFLW | Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69519
Sequence Length: 633
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.256
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Q6CEA5 | MLTVPPLIPRLLLALTPLATIAAAFFYFSQTNVLQPTPYIDEIFHIPQTQQYCKGHWNAWDSKITTPPGLYIIGYAWARMLTLTGLSESEACSTLSLRAVNLMAVVIYIPATLYIIQRRVWGSQAHFSAFSLVSFPLIWFYAALYYTDVWSTATVLMALAFALSPRVPFYMVQLSALMCAVSLFFRQTNILWAAVVAVIAIENSHYSNGAPPKNGALAQIFSTISYTFQIELPIFNILISYASVAVGFSFFLYINGGIALGDKDNHVAGNHIPQVFYCALFITTLGFPVWFTWAHLKAYISSSFSVLGLTVRPLFIFVLIPRLLKSYAIEHPFLLADNRHYVFYLWRRLLKPAIYSISVEDVMQSQDAIDPKTLDVISIGLKYALSAAIYFSLWNIWTTLTNSIPAAILVRGRGFNRRNGKSISPAIDLQCLTWPILLAMVFATLASLIPSPLIEPRYYILPYLFWRIYMTPTTAGKRVNTDARFLREWIWYMLINAATVYMFLYKPFEWAHEPGVLQRFMW | Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59346
Sequence Length: 522
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.256
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P50076 | MDAKKNTGEANNDVLEEEAAIQLIAPGIARNLTQEVITGIFCNVVIYPLLLIYFVLTFRYMTTNIVPYEFIDEKFHVGQTLTYLKGKWTQWDPKITTPPGIYILGLINYYCIKPIFKSWSTLTILRLVNLLGGIIVFPILVLRPIFLFNALGFWPVSLMSFPLMTTYYYLFYTDVWSTILILQSLSCVLTLPFGPVKSIWLSAFFAGVSCLFRQTNIIWTGFIMILAVERPAILQKQFNTHTFNNYLKLFIHAIDDFSNLVLPYMINFVLFFIYLIWNRSITLGDKSSHSAGLHIVQIFYCFTFITVFSLPIWISRNFMKLYKLRIKRKPVQTFFEFIGIMLIIRYFTKVHPFLLADNRHYTFYLFRRLIGNKSRLIKYFFMTPIYHFSTFAYLEVMRPNQLTFHPITPLPIKEPVHLPIQLTHVSWTALITCTMVTIVPSPLFEPRYYILPYFFWRIFITCSCEPLIKDLKPAKEGENPITISSTKRLFMEFLWFMLFNVVTLVIFSKVSFPWTTEPYLQRIIW | Function: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61793
Sequence Length: 525
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.256
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Q9XEE9 | MAIYFILYTLLTIIFAVSLSLFLSVINARKSRKRAVGFFHPYTNDGGGGERVLWCAVKAIQEENPDLDCVIFTGDHDSSSDSLARRAVDRFGVHLQSPPKVIHLNKRKWIEESTYPHFTMIGQSLGSVYLAWEALRMFTPLYFLDTSGYAFTYPLARIFGCKVVCYTHYPTISLDMISRVRQRNSMYNNDASIAKSNWLSTCKLVYYRAFSWMYGMVGSCTHLAMVNSSWTKSHIEVLWRIPERITRVYPPCDTSGLQAFPLERSSDPPKIISVAQFRPEKAHMLQLEAFSLALEKLDADVPRPKLQFVGSCRNNSDEERLQKLKDRAVELKVDGDVQFYKNAMYRELVELLGNAVAGLHGMIDEHFGISVVEYMAAGAIPIAHNSAGPKMDIVLEEDGQKTGFLAETVEEYAEAILEIVKMNETERLKMAESARKRAARFSEQRFCEDFKTAIRPIFTGPLK | Function: Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
Catalytic Activity: alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP + 2 H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52573
Sequence Length: 463
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.131
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Q75B12 | MESCWLTMESYQAALVVCIVSGLILAVAGYGNVRRLACEFLLKPPKRFRDDICEALLRGPENDQKPVLVDFGWRHGAVRRQMLLASAKASAYSNERHGSKIHISPDDIARGRSFADALDVHRRSGRILFGFFHPFCNAGGGGEKVLWKAVETTLKQSLNNIVVVYTGDCDTTGARILSNVEHRFGSQLDSERIVFIFLRHRKWVESRTWPRMTLLGQALGSIVLSIEAALCCPPDVWCDTMGYPFGYPFVSWLCRIPIITYTHYPVVSIDMLDKLRMMPEFRNSPTLWAKFLYWRIFMRCYTFAGSFVDLAVTNSTWTYNHINAIWSRTGNVSIIYPPCSTENLVIENAHDMWDRKHQAVVIAQFRPEKRHALILRSFSNFVKKTGSNMKLLMLGSTRGQEDRDYVKKLEQLAYSELAIPKESLEFITDCKYEKMKKYLQESSFGINAMWNEHFGIAVVEYAASGLITLAHASAGPLLDIIVPWDIEGDKQLERGSDKNRTGFFFKDRSDPDFCKITAEFPTLEELFVRADQLTDEERLAISQRAKRCVLHKFSDLKFSEDWAQVVDRTIQLLHTLRNDKVE | Function: Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum (By similarity).
Catalytic Activity: alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP + 2 H(+)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 66635
Sequence Length: 582
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.131
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P53993 | MSDTVISLISHSITTVFYLVPLIIALIIPFSLYSGFRRKSKTVAFFHPYCNAGGGGERVLWAAIRTMQKKFPDHKYFVYSGDTDATKEQILLKARQRFGIELDPSNIQFIYLHWRTLVEARHYKHCTMLFQALAGLILALEAWFRMVPAVFIDSMGYPLSLPAFRLSGSKVVAYVHYPTISCDMLDVVESRQETFNNSSTIAQSNVLSWGKLTYYRLFACLYWLAGKAAHVGMVNGSWTQRHITSIWSRRDVSIVYPPCDVEAFLNIESVAESLLEDTKTVRLLSVGQIRPEKNHKLQLEVLHDVKEPLEKMGYNVELCIAGGCRNEEDQERVKMLKNEAEKLDISEQLIWQLNVPYEDLVVELSKALISIHTMHNEHFGISVVEAMAASTIILSNDSGGPRMDIVKDYEGHCVGYLSITKEEYVETILKIVEEGLKKRNDTRKYARKSLTRFGEAAFETHWNKEIEKVL | Function: Mannosyltransferase involved in the last steps of the synthesis of Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum. Catalyzes the addition of the 4th and 5th mannose residues to the dolichol-linked oligosaccharide chain.
Catalytic Activity: alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP + 2 H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53647
Sequence Length: 470
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.131
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Q06062 | MNPMTRRHTWTRLACALSLGVAAFAAQADEGALYGPQAPKGSAFVRAYNAGNSELDVSVGSTSLNDVAPLGSSDFKFLPPGSYTAQVGQQSLPVKLDPDSYYTLVSQPGGKPQLVAEPPFKNKQKALVRVQNLSGSKLTLKTADGKTDVVKDVGPQSHGDREINPVKVNLALFDGSKKVSDLKPVTLARGEVVCLYVTGSGGKLAPVWVKRPVKAD | Function: Together with AlgI and AlgJ, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases resistance to opsonic killing in the host.
Sequence Mass (Da): 22834
Sequence Length: 216
Pathway: Glycan biosynthesis; alginate biosynthesis.
Subcellular Location: Periplasm
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Q51371 | MPDISLSIPRRRLPRLRPLAAAVLGAVLLHGQAWAAQPVEKPQPVPAQAGNEPGLTQGLKETGNYTVTTAPAEPLHLDPPKLPDLSGYTAAAVEAKIVRKPGGRASVQRMVQQQPLKEFTGGSNRLAEWVKRQRQMPQAIFIEGGYVNLAQLAGKLPASALEQVEPGVFVARLPIVVSQGATLDIDKQVKELRLSQERGAFLVNDGMLFVRDSKVTGWSESKKEPAWFKTPNEFRPFLISWGGAEVYLSNSTFTSFGYNASKAYGISISQYSPGMDKQMKRPRPKGWVIDSTIVDSWYGFYCYEADDLVVKGNTYRDNIVYGIDPHDRSHRLIIADNTVHGTRKKHGIIVSREVNDSFIFNNRSYENKLSGIVLDRNSEGNLVAYNEVYRNHSDGITLYESGDNLLWGNQVLANRRHGIRVRNSVNIRLYENLAAGNQLIGVYGHIKDLTNTDRNIALDPFDTKVSLIVVGGKLAGNGSGPLSVDSPLSLELYRVAMLAPTKSSGISLPGVLGEKQDQILDLLVRQDKAVLIDPVESQAELQD | Function: Catalyzes the epimerization of beta-D-mannuronate to alpha-L-guluronate during the synthesis of the linear polysaccharide alginate . In addition, is part of a periplasmic protein complex that protects alginate from degradation by AlgL by channeling the newly formed alginate polymer through a scaffold that transfers the alginate polymer through the periplasmic space to the outer membrane secretin AlgE .
Catalytic Activity: [(1->4)-beta-D-mannuronosyl](n) = [alginate](n)
Sequence Mass (Da): 59802
Sequence Length: 543
Domain: The C-terminal region contains a right-handed beta-helix (RHbetaH) fold, which is common among proteins that bind and cleave long-chain linear polysaccharides.
Pathway: Glycan biosynthesis; alginate biosynthesis.
Subcellular Location: Periplasm
EC: 5.1.3.37
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Q887Q3 | MNSHASNGRSRNWPHALLESALLTSALLMASSVALANAPAVPEAPKALVKELHQAKTYTITSPPTGPLEMAKPVLPDLSGYTTEAALKKIARNKPGKITVARMMEETGLKEFIGGDNKMAEWVVRQKGIPQAIMISDGYVNLQDLVKKVPKQFLSEVSPGVYVARLPILVKETGIFEIDSKTKELRLSQEKGSFIVSEGKMLITNTSVNAWSETRNGLAAYRTPDEFRPFVLTWGGSQTWIAKTKMASMGYNQSKSYGVSISQYTPNTAKVLKRGEPTGWIIDSEFADMWYGFYCYETRDFVVKGNTYRDNIVYGIDPHDRSHGLIIAENDVYGTKKKHGIIISREVDNSFIFRNKSHNNKLSGVVLDRNSVGNIVAYNEIYQNHTDGITLYESGNNLLWGNRVIANRRHGIRVRNSVNIKLYENVAMANGLMGVYGHIKDLNDTDRDIELDPFDAQVSLIMVGGELSSNGSGPLSIDSPLSVELYRVSMLMPTKEVGISLNGILGERQDEILDLLVRQKKAVLIDPVESQTELRE | Function: Catalyzes the epimerization of beta-D-mannuronate to alpha-L-guluronate during the synthesis of the linear polysaccharide alginate . In addition, is part of a periplasmic protein complex that protects alginate from degradation by AlgL by channeling the newly formed alginate polymer through a scaffold that transfers the alginate polymer through the periplasmic space to the outer membrane secretin AlgE (By similarity).
Catalytic Activity: [(1->4)-beta-D-mannuronosyl](n) = [alginate](n)
Sequence Mass (Da): 59486
Sequence Length: 536
Domain: The C-terminal region contains a right-handed beta-helix (RHbetaH) fold, which is common among proteins that bind and cleave long-chain linear polysaccharides.
Pathway: Glycan biosynthesis; alginate biosynthesis.
Subcellular Location: Periplasm
EC: 5.1.3.37
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Q51392 | MVFSSNVFLFLFLPVFLGLYYLSGERYRNLLLLIASYVFYAWWRVDFLLLFAGVTVFNYWIGLRIGAAGVRTRAAQRWLILGVVVDLCVLGYFKYANFGVDSLNEIITSFGMQPFVLTHILLPIGISFYTFESISYIIDVYRGDTPATHNLIDFAAFVAIFPHLIAGPVLRFKDLVDQFNHRTHTVDKFAEGCTRFMQGFVKKVFIADTLAALADHCFALQNPTTGDAWLGALAYTAQLYFDFSGYSDMAIGLGLMMGFRFMENFNQPYISQSITEFWRRWHISLSTWLRDYLYISLGGNRGSTFQTYRNLFLTMLLGGLWHGANFTYIIWGAWHGMWLAIERALGVNAAPRVLNPLKWVITFLLVVIGWVIFRAENLQVAWRMYEAMFSFGTWQLSELNRANLTGLQVGTLVLAYLVLAFFGLRQFYNQPLQTKAPKAAANSDEVAADGPASAQPRAPREAAGDPAAIAYSPSGALVYQPSWLSQLPVLATRLALLLLFAASVLKLSAQSYSPFLYFQF | Function: Together with AlgJ and AlgF, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases resistance to opsonic killing in the host.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58746
Sequence Length: 520
Pathway: Glycan biosynthesis; alginate biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.3.1.-
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Q887Q6 | MVFSSNVFLFMFLPIFLGLYYLSGQRYRNLLLLIASYIFYAWWRVDFLALFIGVTVWNYWIGLKVGAAGVRTKPAQRWLLLGVIVDLCILGYFKYANFGVDSINAAMTSMGLEPFILTHVLLPIGISFYVFESISYIIDVYRGDTPATRNLIDFAAFVAIFPHLIAGPVLRFRDLADQFNNRTHTLDKFSEGATRFMQGFIKKVFIADTLAIVADHCFALQNPTTGDAWLGALAYTAQLYFDFSGYSDMAIGLGLMMGFRFMENFKQPYISQSITEFWRRWHISLSTWLRDYLYITLGGNRGGKVATYRNLFLTMLLGGLWHGANVTYIIWGAWHGMWLAIEKAVGINTKPYSFNVIRWALTFLLVVIGWVIFRSENLHVAGRMYGAMFSFGDWQLSELNRASLTGLQVATLVVAYATLAFFGLRDFYQNREKDSGKSARADGPATEQPGTIKAVPGDAPGSLHLPGYTVGSEAQVQPAYWVADWPRYAMRALILLLFVASILKLSAQSFSPFLYFQF | Function: Together with AlgJ and AlgF, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases the ability of alginate to act as a defense barrier (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58606
Sequence Length: 518
Pathway: Glycan biosynthesis; alginate biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.3.1.-
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Q51393 | MTQSISRPLQYAYIAAFGGLLLGLAGWSLKSVPGFSAAADTPLLNGKLAHAFEAHYDKEFPIKRLGTNLWAALDYTLFHEGRPGVVIGKDGWLFTDEEFKPAPSGQQLEDNWALVRGVQRELNRRGVKLVLAVIPAKARLYPEHIGREQPAALHDSLYQDFLARARAAGIDSPDLLGSLRQAKDNGAVFLRTDTHWSPLGAETVAQRLGAEIRETHLLDVPAQNFVTRVGEERTHKGDLLSFLPLDPLFDELLPRPEQLQQRTTEAAPALPGGQQSGAGDDLFGDSQQPRLALVGTSYSANPRWNFEGALKQALSADLINYAKEGKGPLEPMLELLQDEGFRKDPPQLLVWEFPERYLPMASDLSQFDADWVAQLKASGGRDERLAASRND | Function: Together with AlgI and AlgF, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases resistance to opsonic killing in the host.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 43107
Sequence Length: 391
Pathway: Glycan biosynthesis; alginate biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.3.1.-
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Q94G86 | MAANVQTSSLLFLVFLLLQNFYSANSQSFLGVNYGQLSDNLPSLQATVNLLKSTTIQKVRLFGAEPAVIKAFANTGVEIVIGFDNGDIPTLASNPNVASQFVKSNVMSFYPASNIIAITVGNEVLTSGDQKLISQLLPAMQNVQNALNAASLGGKVKVSTVHAMAVLSQSYPPSSGVFNPGLGDTMKALLQFQSANDAPFMISPYPYFAYKNQPTPDTLAFCLFQPNAGQVDSGNGHKYTNMFDAQVDAVHSALNAMGFKDIEIVVAETGWPHGGDSNEVGPSLDNAKAYVGNLINHLKSKVGTPLMPGKSIDTYLFSLYDEDKKTGASSEKYFGLFKPDGSTTYDVGLLKNTQNPTTPATPTPTPKAAGSWCVPKPGVSDDQLTGNINYACGQGIDCGPIQPGGACFEPNTVKAHAAYVMNLYYQSAGRNSWNCDFSQTATLTNTNPSYGACNFPSGSN | PTM: Glycosylated.
Catalytic Activity: Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.
Sequence Mass (Da): 48838
Sequence Length: 460
Domain: The N-terminal region (1-350) contains the enzymatic activity while the C-terminal region (360-460) can bind laminarin. Both regions are allergenic by themselves.
Subcellular Location: Secreted
EC: 3.2.1.39
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Q92TW1 | MIPLPIRPLSHSEFAPFGDVIEPDDAKSFPINAGKCIRYHDLARVETSGPEARTLVSLLKGEPYDIPLTLKMVERHPLGSQAFIPLTGNPFLVVVAPDEGGEPGEPIAFETGPGQGVNIAQNVWHGILTPLRSTSEFVVIDRGGSGCNLEEHFFEKPYQVEYA | Function: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source.
Catalytic Activity: (S)-ureidoglycolate = glyoxylate + urea
Sequence Mass (Da): 17777
Sequence Length: 163
Pathway: Nitrogen metabolism; (S)-allantoin degradation.
EC: 4.3.2.3
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Q8UD04 | MTDFLEIRPLTKEAFTPFGDVIETTPSSMRHINGGQTERHHALSAPEAAGEGARIILNIFRGQPRVFPHKIDMMERHPLGSQSFSPLSGRPFLVVVAQDDGGRPARPQVFLARGDQGVNYRRNVWHYPLMPLQAVSDFLVADREGPGNNLEEYFFDEPFMIAEPSL | Function: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source.
Catalytic Activity: (S)-ureidoglycolate = glyoxylate + urea
Sequence Mass (Da): 18643
Sequence Length: 166
Pathway: Nitrogen metabolism; (S)-allantoin degradation.
EC: 4.3.2.3
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A6WWR5 | MHVETLVIEPLTKEAFAPFGDVIETEGAELRLINNGTTERYHDLARVEAAGTEARVLVNIFRGQSFEAPIDIVMMERHPFGSQAFIPLNGRPFLVVVAEDDGGKPARLRVFLAHGNQGVNYLRNVWHHPLLALEQKSDFLIVDRAGKEDNLEEFFFSDTTYRIETTKPA | Function: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source.
Catalytic Activity: (S)-ureidoglycolate = glyoxylate + urea
Sequence Mass (Da): 19049
Sequence Length: 169
Pathway: Nitrogen metabolism; (S)-allantoin degradation.
EC: 4.3.2.3
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A9M929 | MQIETLTVEPLTKEAFAPFGDVIEVEGAQLRLINNGTTERYHDLARVEAAGTQTRVLINIFRGQSFAAPIDIMMMERHPFGSQAFIPLNGRPFLVVVAEDAGAGPARPRAFLARGDQGVNYLRNIWHHPLLALEQKSDFLVVDRAGREDNLEEYFFSDYAYRIETTQTA | Function: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source.
Catalytic Activity: (S)-ureidoglycolate = glyoxylate + urea
Sequence Mass (Da): 19011
Sequence Length: 169
Pathway: Nitrogen metabolism; (S)-allantoin degradation.
EC: 4.3.2.3
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P77555 | MKISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRLEETGPCSAILHADNAAGQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGFIGISMCQSDPMVVPFGGAEIYYGTNPLAFAAPGEGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGVPTTDPFAVHALLPAAGPKGYGLMMMIDVLSGVLLGLPFGRQVSSMYDDLHAGRNLGQLHIVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQDQDIKQRKAAVEGIEIVDDIYQYLISDALYNTSYETKNPFAQ | Function: AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin . It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions . Catalyzes the oxidation of ureidoglycolate to oxalurate .
Catalytic Activity: (S)-ureidoglycolate + NAD(+) = H(+) + N-carbamoyl-2-oxoglycine + NADH
Sequence Mass (Da): 37967
Sequence Length: 349
Pathway: Nitrogen metabolism; (S)-allantoin degradation; oxalurate from (S)-ureidoglycolate: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.350
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P75713 | MGYLNNVTGYREDLLANRAIVKHGNFALLTPDGLVKNIIPGFENCDATILSTPKLGASFVDYLVTLHQNGGNQQGFGGEGIETFLYVISGNITAKAEGKTFALSEGGYLYCPPGSLMTFVNAQAEDSQIFLYKRRYVPVEGYAPWLVSGNASELERIHYEGMDDVILLDFLPKELGFDMNMHILSFAPGASHGYIETHVQEHGAYILSGQGVYNLDNNWIPVKKGDYIFMGAYSLQAGYGVGRGEAFSYIYSKDCNRDVEI | Cofactor: Also able to use Co(2+).
Function: Involved in the anaerobic nitrogen utilization via the assimilation of allantoin. Catalyzes the second stereospecific hydrolysis reaction (deamination) of the allantoin degradation pathway, producing S-ureidoglycolate and ammonia from S-ureidoglycine.
Catalytic Activity: (S)-2-ureidoglycine + H2O = (S)-ureidoglycolate + NH4(+)
Sequence Mass (Da): 28730
Sequence Length: 261
Subcellular Location: Cytoplasm
EC: 3.5.3.26
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Q8UFI8 | MKTVTARPLTAEAFAPYGSVADISELENLVSLADAYEGTGEAKTPVLQLVQAKAMSGSPVISQMEIHPFSSQTFLPLDQSSSLIVVCEAGEDGMPDESTIKAFLASPSQIVTYRHGVMHHRLTPLAPSGRFAMTMWQTGRGGDTVLYPLHTPVSVDISDITP | Function: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source (By similarity).
Catalytic Activity: (S)-ureidoglycolate = glyoxylate + urea
Sequence Mass (Da): 17318
Sequence Length: 162
Pathway: Nitrogen metabolism; (S)-allantoin degradation.
EC: 4.3.2.3
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Q01594 | MVESYKKIGSCNKMPCLVILTCIIMSNSLVNNNNMVQAKMTWTMKAAEEAEAVANINCSEHGRAFLDGIISEGSPKCECNTCYTGPDCSEKIQGCSADVASGDGLFLEEYWKQHKEASAVLVSPWHRMSYFFNPVSNFISFELEKTIKELHEVVGNAAAKDRYIVFGVGVTQLIHGLVISLSPNMTATPDAPESKVVAHAPFYPVFREQTKYFNKKGYVWAGNAANYVNVSNPEQYIEMVTSPNNPEGLLRHAVIKGCKSIYDMVYYWPHYTPIKYKADEDILLFTMSKFTGHSGSRFGWALIKDESVYNNLLNYMTKNTEGTPRETQLRSLKVLKEVVAMVKTQKGTMRDLNTFGFKKLRERWVNITALLDQSDRFSYQELPQSEYCNYFRRMRPPSPSYAWVKCEWEEDKDCYQTFQNGRINTQNGVGFEASSRYVRLSLIKTQDDFDQLMYYLKDMVKAKRKTPLIKQLFIDQTETASRRPFI | Function: Able to cleave the C-S bond of sulfoxide derivatives of Cys to produce allicin, thus giving rise to all sulfur compounds which are responsible for most of the properties of garlic, such as the specific smell and flavor as well as the health benefits like blood lipid or blood pressure lowering.
Catalytic Activity: an S-alkyl-L-cysteine S-oxide = 2-aminoprop-2-enoate + an S-alkyl sulfenate
Sequence Mass (Da): 55639
Sequence Length: 486
Domain: The 6 Cys residues of the EGF-like domain are arranged in a disulfide pattern different from the one found in the canonical EGFs. The function of this domain is unclear. It may be a binding site for other proteins or the docking site for a putative alliinase receptor.
Subcellular Location: Vacuole
EC: 4.4.1.4
|
Q9U389 | MNDPLDSLSNDEFEIIETFDPETEDREDQWSIQQSIRIEPISIQMPNTLQSQRAPSPVGSKAPESLKDEDPDRTPEASIVETPLLTETLKEDRTPMSTPLASLVNSSQSPEFTLQNMSIVSESECSNNSSLVNVADVESTEIALRTSLLLVSELKSQLQAAKMSESTLLKSNSNHEIEENKKLSEKMEVMKNEFELKMQESAASVEKVIQEKDSAIEQLKVQLAQSQQVAELWKQGAEKNSNAQYSDSKTTIDRLLEENSKLRNLVDEEVARRLEESERRKLAEDQLKHARGGSVFDPPASFVASQLAERTTYSLNLEHELITLRKELEETKEALKKSVEESSNKDEIVSALHELAGPTGEHPHARFERAGDQQSEAEMSSTWSAGRLLELSRQIVHFISHQ | Function: Autophagy receptor, which is required for allophagy, an autophagic process in which paternal organelles, including mitochondria and membranous organelles, are degraded in early embryos. After fertilization, recruited to ubiquitin-modified paternal organelles and is required for the formation of autophagosomes around the paternal organelles. Also plays a role in the regulation of autophagy in germ cells.
PTM: Phosphorylation on Thr-74 by ikke-1 is required for allophagic function.
Sequence Mass (Da): 45158
Sequence Length: 402
Domain: The C-terminal region is required for localization to paternal organelles.
Subcellular Location: Cytoplasm
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P94575 | MKLKESQQQSNRLSNEDLVPLGQEKRTWKAMNFASIWMGCIHNIPTYATVGGLIAIGLSPWQVLAIIITASLILFGALALNGHAGTKYGLPFPVIIRASYGIYGANIPALLRAFTAIMWLGIQTFAGSTALNILLLNMWPGWGEIGGEWNILGIHLSGLLSFVFFWAIHLLVLHHGMESIKRFEVWAGPLVYLVFGGMVWWAVDIAGGLGPIYSQPGKFHTFSETFWPFAAGVTGIIGIWATLILNIPDFTRFAETQKEQIKGQFYGLPGTFALFAFASITVTSGSQVAFGEPIWDVVDILARFDNPYVIVLSVITLCIATISVNVAANIVSPAYDIANALPKYINFKRGSFITALLALFTVPWKLMESATSVYAFLGLIGGMLGPVAGVMMADYFIIRKRELSVDDLYSETGRYVYWKGYNYRAFAATMLGALISLIGMYVPVLKSLYDISWFVGVLISFLFYIVLMRVHPPASLAIETVEHAQVRQAE | Function: Uptake of allantoin into the cell . Allantoin uptake is not dependent on sodium, and PucI is likely to be a proton-coupled symporter . Shows highest recognition for binding of allantoin, good recognition for binding of hydantoin, L-5-benzylhydantoin and 5-hydroxyhydantoin, and to a lesser extent for a range of nucleobases and nucleosides .
Catalytic Activity: (S)-allantoin(in) + H(+)(in) = (S)-allantoin(out) + H(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53982
Sequence Length: 490
Subcellular Location: Cell membrane
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P75712 | MEHQRKLFQQRGYSEDLLPKTQSQRTWKTFNYFTLWMGSVHNVPNYVMVGGFFILGLSTFSIMLAIILSAFFIAAVMVLNGAAGSKYGVPFAMILRASYGVRGALFPGLLRGGIAAIMWFGLQCYAGSLACLILIGKIWPGFLTLGGDFTLLGLSLPGLITFLIFWLVNVGIGFGGGKVLNKFTAILNPCIYIVFGGMAIWAISLVGIGPIFDYIPSGIQKAENGGFLFLVVINAVVAVWAAPAVSASDFTQNAHSFREQALGQTLGLVVAYILFAVAGVCIIAGASIHYGADTWNVLDIVQRWDSLFASFFAVLVILMTTISTNATGNIIPAGYQIAAIAPTKLTYKNGVLIASIISLLICPWKLMENQDSIYLFLDIIGGMLGPVIGVMMAHYFVVMRGQINLDELYTAPGDYKYYDNGFNLTAFSVTLVAVILSLGGKFIHFMEPLSRVSWFVGVIVAFAAYALLKKRTTAEKTGEQKTIG | Function: Uptake of allantoin into the cell.
Catalytic Activity: (S)-allantoin(in) + H(+)(in) = (S)-allantoin(out) + H(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52456
Sequence Length: 484
Subcellular Location: Cell inner membrane
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Q9PP26 | MSLIKIDQKAYEYNLRHIAKKIGSFQRLICVFKDNAYGHGAKLLAPLAKNLGVSFVAVKSEEEAREIEEFFENILILSHRPHGNENSRFIYALNDISQVKNYKQDIKIHLKIDTGMHRNGICVENLEHAINLIQGSDLKLTGMFTHFASADEMDGSFFVQKENFQKAKKIVKKYFSNLLFHSYNSAALFRGKIPEDEYCRVGLVQFGYGDSNLKRVLSLYAHRLSQRILQKGQSIGYGGIFTAAKDMEVATYDLGYADGLFRYNGRGELVLGNGKAMLGKMSMDSFSCENSGEEICVFKDADIWADFFHTINYEILVKLNPNIQRVLV | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 37256
Sequence Length: 328
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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Q9F8I0 | MRPVWAEVNLENIRHNFREVKRLARQAEAMPVIKANAYGHGAVEVAKALIAEGAKRFAVAILDEGIKLREAGIDAPVLILGYTPPEEVEKLLFYNLTPTLHHRELALAYQERLERLKKTLFYHLKIDTGMGRIGFWYEELEKIEEVLKLKNLEAEGVYTHFARADEQDLSFSKLQIERFNIVLKHLKAKGIEVKYRHAANSAAIMRLPEAHYDLVRPGIMLYGEYPSRDVPRELAHLKPALTLKARVSQVKKVPAGFTVSYGSTYVTSKATLIVSLPLGYADGYFRRLSNRGVVLINGKRWSIAGRVCMDQLMVAVDETERVNPGDEAVLLGKQGEETITAMEMADLVGTINYEILTNISYRVPRIYV | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 41632
Sequence Length: 368
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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Q9A7Q9 | MTDAQDTRITIDLDALAHNYAALRARAGDAEVAPAVKADAYGLGAAPVADRLWAEGARSFYVARLAEGVALRRSLGDREATIYVLDGATPGSGEALEGAQLVPVLNSLPQVEAWNVQARSGRLRAALHIDTGMNRLGLRPEELKVLVGSFDRLKRLDVELVVSHLACADTPEHPLNATQLARFQEAAALLPGVRRSLANSGGLFLGEAYRFDQTRPGVSLYGGGPEGRPHPEIRAVATVEAPILQVRVVPRGESIGYGAGWTASDNTRVAIVAAGYADGVPRAAFPRGEVWFDGARRPMLGRVSMDLIAVDVTDCDAARPGAMVELFGANLPVDDAADAAGTSAYERLTRLTLRGVRRYVGGAR | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 38637
Sequence Length: 364
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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Q3J3L4 | MATATLTIDLDAIAANWRALDQMTASDCQTGAVVKADSYGLGAAKVAHALARAGARRFFVATCEEGADVRRALGSGPQICVFSGHMEGDTALIRDFDLTPMLNSIDQLTRHFEALGGQPFGLQLDSGMNRLGLEPGEWEAVAGFALEAGPELLMSHLACSDDPDHPMNAEQLGAFRAMTDGTGVPRSLSATGGILLGPAWHFELTRPGIGLYGGRPFENARPVVRLSLPVIQVREVEIGEPVGYSNTWTAEHTSTIATVAAGYADGLPRTLSSRATLYAGRVPCPLVGRVSMDLITVDVSHLPEVPETLDILGPHQTPDDLADTAGTIGYEILTSLGRRYQRRYGALAA | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 37037
Sequence Length: 349
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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Q8KB67 | MSASHEQNSAAAPNGPNLSEALISLGNLRHNLACIRAITGPQCRVMGIVKANAYGHGATQVTATLEAEGVRDFGVANIYEAIELLQEHRMLPDSRILAFASPLAGHIDLYLQHGVEMTVCDHETARAAESIAAACGRRLQVQLKVDTGMGRLGVTPEEAAELLELIEACPNLELTGIYTHFAESDKPEGFTARQLERFLHVTGAYERRTGKTVTKHAANSGAIISMPDARLDMVRPGILLYGCHPVDAAPSTVPVRPVMQFQSRVIFVKEVPAGTAISYNRTWSAPKATRIATISAGYADGFHRALSNQARVSIGGKSFPQVGTITMDQTMVNLGSDDSVKVGDTAVLFGWDGPSAGEQALAAGTISYELLCSVSRRVRRIVV | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 40987
Sequence Length: 383
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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Q1QU82 | MSRPLIADIDLDALRRNYCLARDQAPHSRAIAVVKADAYGHGAVACADALRDLAPAFAVACLEEALTLREAGITQPIVLLEGFFDAAELSLIDAHRLWTAVHSDWQIDALLAYRPRQPIPTWLKLDSGMHRLGFAPEAFEARWQRLAAATEHVTDLHLMTHFATADALDAAYFRRQMACIASLRQRLEAPVCLANSPATLAWPEAHGDWNRPGVMLYGSDPLEGANDASRALEPVMTLRSEIIAVRELAEGEAVGYGGRWRASRPSRIGVVAGGYGDGYDRHARDGTPVLVEGQRVPLAGKVSMDMLTVDLTELPEAGIGSPVVLWGEGLPIDEVARHCDTISYTLMTGVLPRVPRRYRNAETG | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 39714
Sequence Length: 364
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
|
A8EXF8 | MSLCTLAINLSAIKNNYFLLQDICKTSLVGAVVKADGYGLGAVQISKALIEENCRHFFVASSEEGVNVRKALGIDVNILVLNGVFEHDALELIEYNLIPILNNLKQIEIWQQFGNLKNLLLPCYLHFNTGINRLGLSSNEIEQLINNRDLLKGLNLQYIISHLAISEEIDNPYNLEQLNKFKAYLRYFPSIKASLANSGGIFLGQDYHFDLVRPGAALYGLNPLMQNPVTLKAPIIHLQNLTLDSHIGYNMTFTTKRDSVIATLPLGYADGYSRNFSNQGKVFINGRSVPIVGRVSMDLINIDVTDLPPSDIFLGQEVEIIGNHCTPDKIASIIGTIGYEVLTSLGNRYRRKYTR | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 39561
Sequence Length: 355
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
|
Q4UNC8 | MSLCTLEINLSAIKNNYLLLQDICKTSLVGAAVKANGYGLGAVQISKALIEENCRHFFVASSEEGVNLRKALASWHESVFRHCEKNYTVIRRSNPVKNSVSQNFFNYFSGLQQCFAPRNDGSSIHATTPKALDNDVNILVLNGVFEHDALELIEYNLTPVLNNLKQIEIWQKFSNLKNRLLPCYLHFNTGINRLGLTHNEIEQLINNRDLLKGLDLQYIISHLAVSEEIDNPYNLEQLNRFKTYLQYFPNVKASLANSGGIFLGQDYHFDLARPGAALYGLNPVIDLSNNLSYKEEFEGDTERRTAAYINVREDSSTGSTYKLPLEGGYSRGLQNPVTLKAPIIHLQNLTLDSHIGYNMTFTTERDSVIATLPLGYADGFSRNFSNQGEVFINGRSVPIVGRISMDLINIDVTDLPPLDIFLGQEAEIIGNYCTPDKIASIIGTIGYEVLTSLGSRYKRIYK | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 51764
Sequence Length: 462
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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P36117 | MLQFNTENDTVAPVFPMEQDINAAPDAVPLVQTTTLQVFVKLAEPIVFLKGFETNGLSEIAPSILRGSLIVRVLKPNKLKSISITFKGISRTEWPEGIPPKREEFSDVETVVNHTWPFYQADDGMNSFTLEHHSSNNSSNRPSMSDEDYLLEKSGASVYIPPTAEPPKDNSNLSLDAYERNSLSSDNLSNKPVSSDVSHDDSKLLAIQKTPLPSSSRRGSVPANFHGNSLSPHTFISDLFTKTFSNSGATPSPEQEDNYLTPSKDSKEVFIFRPGDYIYTFEQPISQSYPESIKANFGSVEYKLSIDIERFGAFKSTIHTQLPIKVVRLPSDGSVEETEAIAISKDWKDLLHYDVVIFSKEIVLNAFLPIDFHFAPLDKVTLHRIRIYLTESMEYTCNSNGNHEKARRLEPTKKFLLAEHNGPKLPHIPAGSNPLKAKNRGNILLDEKSGDLVNKDFQFEVFVPSKFTNSIRLHPDTNYDKIKAHHWIKICLRLSKKYGDNRKHFEISIDSPIHILNQLCSHANTLLPSYESHFQYCDEDGNFAPAADQQNYASHHDSNIFFPKEVLSSPVLSPNVQKMNIRIPSDLPVVRNRAESVKKSKSDNTSKKNDQSSNVFASKQLVANIYKPNQIPRELTSPQALPLSPITSPILNYQPLSNSPPPDFDFDLAKRGAADSHAIPVDPPSYFDVLKADGIELPYYDTSSSKIPELKLNKSRETLASIEEDSFNGWSQIDDLSDEDDNDGDIASGFNFKLSTSAPSENVNSHTPILQSLNMSLDGRKKNRASLHATSVLPSTIRQNNQHFNDINQMLGSSDEDAFPKSQSLNFNKKLPILKINDNVIQSNSNSNNRVDNPEDTVDSSVDITAFYDPRMSSDSKFDWEVSKNHVDPAAYSVNVASENRVLDDFKKAFREKRK | Function: May regulate endocytosis by recruiting RSP5 ubiquitin ligase activity to specific plasma membrane proteins in response to extracellular stimuli.
PTM: Ubiquitinated by RSP5.
Sequence Mass (Da): 102540
Sequence Length: 915
Subcellular Location: Cytoplasm
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Q59478 | MLKSGVMVASLCLFSVPSRAAVPAPGDKFELSGWSLSVPVDSDNDGKADQIKEKTLAAGYRNSDFFTLSDAGGMVFKAPISGAKTSKNTTYTRSELREMLRKGDTSIATQGVSRNNWVLSSAPLSEQKKAGGVDGTLEATLSVDHVTTTGVNWQVGRVIIGQIHANNDEPIRLYYRKLPHHQKGSVYFAHEPRKGFGDEQWYEMIGTLQPSHGNQTAAPTEPEAGIALGETFSYRIDATGNKLTVTLMREGRPDVVKTVDMSKSGYSEAGQYLYFKAGVYNQNKTGKPDDYVQATFYRLKATHGAQR | Function: Degrades alginates that contain guluronic acid.
Catalytic Activity: Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
Sequence Mass (Da): 33512
Sequence Length: 307
Subcellular Location: Secreted
EC: 4.2.2.3
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Q59639 | MKIISCKSIIVSSLLALSATATAGSFNDISWTLENEDNLPETDASGCALKPSTSTSTSKTFEFGLTDDSNCLDGKQRDEFKYQRRTGYNRLTGYFTIDGNYSDFNKMGVAQTHDHSTSDTGVFSIYQVRKENGSYIFGVQGDSNYSNNGWSDHPQVKISLDTRYELIIKTNGLPNGNSYEDANLYLDDVKIWSSSIEVGGEEKQYKKIGAYQLTGGEGEFHVKWDSVKLYTGK | Catalytic Activity: Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and beta-D-mannuronate at their reducing end.
Sequence Mass (Da): 25873
Sequence Length: 233
Subcellular Location: Secreted
EC: 4.2.2.3
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O03979 | MGVDIEKGVAWMQARKGRVSYSMDFRDGPDSYDCSSSMYYALRSAGASSAGWAVNTEYMHAWLIENGYELISENAPWDAKRGDIFIWGRKGASAGAGGHTGMFIDSDNIIHCNYAYDGISVNDHDERWYYAGQPYYYVYRLTNANAQPAEKKLGWQKDATGFWYARANGTYPKDEFEYIEENKSWFYFDDQGYMLAEKWLKHTDGNWYWFDRDGYMATSWKRIGESWYYFNRDGSMVTGWIKYYDNWYYCDATNGDMKSNAFIRYNDGWYLLLPDGRLADKPQFTVEPDGLITAKV | Function: Lysis of bacterial host cell wall.
Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 34453
Sequence Length: 296
Subcellular Location: Host cell wall
EC: 3.5.1.28
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Q38135 | MTIYDKTFLLGTGQGSSQKASNRYIVIHDTANDNNQGDNSATNEASYMHNNWQNAYTHAIAGWDKVYLVGEPGYVAYGAGSPANERSPFQIELSHYSDPAKQRSSYINYINAVREQAKVFGIPLTLDGAGNGIKTHKWVSDNLWGDHQDPYSYLTRIGISKDQLAKDLANGIGGASKSNQSNNDDSTHAINYTPNMEEKEMTYLIFAKDTKRWYITNGIEIRYIKTGRVLGNYQNQWLKFKLPVDTMFQAEVDKEFGTGATNPNRDISKG | Catalytic Activity: Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Sequence Mass (Da): 30214
Sequence Length: 270
Subcellular Location: Secreted
EC: 3.5.1.28
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P37710 | MKKESMSRIERRKAQQRKKTPVQWKKSTTLFSSALIVSSVGTPVALLPVTAEATEEQPTNAEVAQAPTTETGLVETPTTETTPGTTEQPTTDSSTTTESTTESSKETPTTPSTEQPTADSTTPVESGTTDSSVAEITPVAPSATESEAAPAVTPDDEVKVPEARVASAQTFSALSPTQSPSEFIAELARCAQPIAQANDLYASVMMAQAIVESGWGASTLSKAPNYNLFGIKGSYNGQSVYMDTWEYLNGKWLVKKEPFRKYPSYMESFQDNAHVLKTTSFQAGVYYYAGAWKSNTSSYRDATAWLTGRYATDPSYNAKLNNVITAYNLTQYDTPSSGGNTGGGTVNPGTGGSNNQSGTNTYYTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSGSGGSNNNQSGTNTYYTVKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFVGQKLIVKKGASGNTGGSNNGGSNNNQSGTNTYYTIKSGDTLNKIAAQYGVSVANLRSWNGISGDLIFAGQKIIVKKGTSGNTGGSSNGGSNNNQSGTNTYYTIKSGDTLNKISAQFGVSVANLQAWNNISGSLIFAGQKIIVKKGANSGSTNTNKPTNNGGGATTSYTIKSGDTLNKISAQFGVSVANLRSWNGIKGDLIFAGQTIIVKKGASAGGNASSTNSASGKRHTVKSGDSLWGLSMQYGISIQKIKQLNGLSGDTIYIGQTLKVG | Function: Hydrolyzes the cell wall of E.faecalis and M.lysodeikticus. May play an important role in cell wall growth and cell separation.
Sequence Mass (Da): 77025
Sequence Length: 737
Domain: LysM domains are thought to be involved in peptidoglycan binding.
Subcellular Location: Secreted
EC: 3.2.1.-
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