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Q8H5T6 | MADSTATCIDIILAIILPPLGVFFKFGCGIEFWICLLLTFFGYLPGIIYAVWVITK | Function: Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6230
Sequence Length: 56
Subcellular Location: Membrane
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Q7T0T2 | MAEELKRFLYKKLPSIEGLHAIVVSDRDGVPVIKVANENAPELALRPSFLSTFALATDQGSKLGLSKNKSIICYYDTCQVVQFNRLPLVVSFIASSDANTGLLLSLNEELGDLFEELQHAVEI | Function: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator plays a dual role for the small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD): it (1) acts as a guanine nucleotide exchange factor (GEF), activating the small GTPases Rag and (2) mediates recruitment of Rag GTPases to the lysosome membrane. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13538
Sequence Length: 123
Subcellular Location: Late endosome membrane
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Q9KLK7 | MNIRPSQIKHKQRIASFITHAVVVVMGVLIVSVLFQSYQISSRLMAQEGQRTSVQTSSLIQSLFDFRLAALRIHQDSTAKNASLINALVSRDSSRLDEFFSSVDELELSNAPDLRFISSHDNILWDDGNASFYGIAQQELNKLIRRVAISGNWHLVQTPSEGKSVHILMRRSSLIEAGTGQVVGYLYVGIVLNDNFALLENIRSGSNSENLVLAVDTTPLVSTLKGNEPYSLDYVVHSAKDAMRDSFIVGQTFLEVESVPTYLCVYSIQTNQNVLTLRDNFYFWMAFALISMIGVSIASRWWLQKRIQREIETLMNYTHKLMDLDTKSEFIGSKIYEFDYFGRTLEQSFRRLANKEKQFEDLFNFALSPTMLWNTSGRLIRMNPSAQIQFLREDAQNHFLFEILERQLLPTITNAAQGNNPSDVTTEVDGRVYRWNLSPIMVEGQIISIITQGQDITTIAEAEKQSQAARREAEESARVRAEFLAKMSHELRTPLNGVLGVSQLLKRTPLNDEQREHVAVLCSSGEHLLAVLNDILDFSRLEQGKFRIQKNEFRLKELVCAIDRIYRPLCNEKGLELVVNSNITTAAIVRSDQIRINQILFNLLNNAIKFTHQGSIRVELQLIEGDPLAQLVIQVVDTGIGIREQDLTVIFEPFMQAESTTTREYGGSGLGLTIVHSLVEMLSGQLHVSSEYGIGTRFEIQLPIELVEKPDAPQQLLPAPDPQPLFDKTLRVLLVEDNHTNAFIAQAFCRKYGLDVSWVTDGLQAIEELKIHDYDLVLMDNQLPYLDGVETTRTIKKVLHLPVVVYACTADGLEETRQAFFHAGAEYVLVKPLKEQTLHKALEHFKHHHGQKNAGLN | Function: At low cell density, in absence of AI-2 (autoinducer 2), LuxQ has a kinase activity and autophosphorylates on a histidine residue. The phosphoryl group is then transferred to an aspartate residue in the response regulator domain. The phosphoryl group is transferred to LuxU, and ultimately to LuxO. At high cell density, in the presence of AI-2, the kinase activity is inactivated, and the response regulator domain has a phosphatase activity (By similarity).
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96930
Sequence Length: 857
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
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P54302 | MTTTRSNIKKRRSLATLITKIIILVLAPIILGIFIQSYYFSKQIIWQEVDRTKQQTSALIHNIFDSHFAAIQIHHDSNSKSEVIRDFYTDRDTDVLNFFFLSIDQSDPSHTPEFRFLTDHKGIIWDDGNAHFYGVNDLILDSLANRVSFSNNWYYINVMTSIGSRHMLVRRVPILDPSTGEVLGFSFNAVVLDNNFALMEKLKSESNVDNVVLVANSVPLANSLIGDEPYNVADVLQRKSSDKRLDKLLVIETPIVVNAVTTELCLLTVQDNQSVVTLQIQHILAMLASIIGMIMIALMSREWIESKVSAQLESLMSYTRSAREEKGFERFGGSDIEEFDHIGSTLESTFEELEAQKKSFRDLFNFALSPIMVWSEESVLIQMNPAARKELVIEDDHEIMHPVFQGFKEKLTPHLKMAAQGATLTGVNVPIGNKIYRWNLSPIRVDGDISGIIVQGQDITTLIEAEKQSNIARREAEKSAQARADFLAKMSHEIRTPINGILGVAQLLKDSVDTQEQKNQIDVLCHSGEHLLAVLNDILDFSKIEQGKFNIQKHPFSFTDTMRTLENIYRPICTNKGVELVIENELDPNVEIFTDQVRLNQILFNLVSNAVKFTPIGSIRLHAELEQFYGAENSVLVVELTDTGIGIESDKLDQMFEPFVQEESTTTREYGGSGLGLTIVKNLVDMLEGDVQVRSSKGGGTTFVITLPVKDRERVLRPLEVSQRIKPEALFDESLKVLLVEDNHTNAFILQAFCKKYKMQVDWAKDGLDAMELLSDTTYDLILMDNQLPHLGGIETTHEIRQNLRLGTPIYACTADTAKETSDAFMAAGANYVMLKPIKENALHEAFVDFKQRFLVERT | Function: At low cell density, in absence of AI-2 (autoinducer 2), LuxQ has a kinase activity and autophosphorylates on a histidine residue. The phosphoryl group is then transferred to an aspartate residue in the response regulator domain. The phosphoryl group is transferred to LuxU, and ultimately to LuxO. At high cell density, in the presence of AI-2, the kinase activity is inactivated, and the response regulator domain has a phosphatase activity.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96915
Sequence Length: 859
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
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Q4R5M8 | MLPAAMKGLGLALLAVLLCSAPAHGLWCQDCTLTTNSSHCTPKQCQPSDTVCASVRITDPSSSRKDHSVNKMCASSCDFVKRHFFSDYLMGFINSGILKVDVDCYEKDLCNGVAGAGHSPWALAGGLLLSLGPALLWAGP | Function: Believed to act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits alpha-3:beta-4-containing nAChRs maximum response. May play a role in the intracellular trafficking of alpha-7-containing nAChRs and may inhibit their expression at the cell surface. Seems to inhibit alpha-7/CHRNA7 signaling in hippocampal neurons (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 14757
Sequence Length: 140
Subcellular Location: Cell membrane
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Q9WUC3 | MLPAAMKSLGLALLALLLCPSPAHGLWCQDCTLANSSHCAPKQCQPTDTVCASVRITDPSSSRKDHSVNKMCASSCDFVKRHFFSDYLMGFINSGILKVDVDCCEKDLCNGASVAGRSPWALAGGLLLSLGPALLWAGP | Function: Believed to act as modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits alpha-3:beta-4-containing nAChRs maximum response. In vitro inhibits alpha-3:beta-4-containing nAChRs maximum response . May play a role in the intracellular trafficking of alpha-7-containing nAChRs and may inhibit their expression at the cell surface . Seems to inhibit alpha-7/CHRNA7 signaling in hippocampal neurons (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 14669
Sequence Length: 139
Subcellular Location: Cell membrane
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Q17RY6 | MALLALLLVVALPRVWTDANLTARQRDPEDSQRTDEGDNRVWCHVCERENTFECQNPRRCKWTEPYCVIAAVKIFPRFFMVAKQCSAGCAAMERPKPEEKRFLLEEPMPFFYLKCCKIRYCNLEGPPINSSVFKEYAGSMGESCGGLWLAILLLLASIAAGLSLS | Function: Required for sperm migration into the oviduct and male fertility by controlling binding of sperm to zona pellucida (By similarity). May play a role in cell growth .
Location Topology: Lipid-anchor
Sequence Mass (Da): 18673
Sequence Length: 165
Subcellular Location: Secreted
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Q9CWP4 | MAFLVALLVVLGLQLVQSNALTCHVCEAQNSYACSNPSQCPGEKKFCLLAVTRIFERFFYVSKQCTRRCPTPVVSPPSTNPPSEPKEFLIEKPMPFLFYKCCQWDSCNGEGPPTDQLLKEQPGKASGRRHRYIELLLTGFMVLTANGLSALCLL | Function: Required for sperm migration into the oviduct and male fertility by controlling binding of sperm to zona pellucida . May play a role in cell growth (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 17134
Sequence Length: 154
Subcellular Location: Secreted
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Q86Y78 | MEPGPALAWLLLLSLLADCLKAAQSRDFTVKDIIYLHPSTTPYPGGFKCFTCEKAADNYECNRWAPDIYCPRETRYCYTQHTMEVTGNSISVTKRCVPLEECLSTGCRDSEHEGHKVCTSCCEGNICNLPLPRNETDATFATTSPINQTNGHPRCMSVIVSCLWLWLGLML | Function: Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain . Inhibits nicotine-induced Ca(2+) influx through nAChRs . In vitro, specifically inhibits alpha-3:beta-4 and alpha-7 nAChR currents in an allosteric manner . Acts as a positive regulator of Wnt/beta-catenin signaling (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 19118
Sequence Length: 171
Domain: The UPAR/Ly6 domain is sufficient for inhibiting alpha-3:beta-4 and alpha-7-dependent nAChR currents.
Subcellular Location: Secreted
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D3ZTT2 | MEPSPALAWLLLLSLVADCLKAAQSRDFTVKDIIYLHPSTTPYPGGFKCFTCEKAADNYECNRWAPDIYCPRDTRYCYTQHTMEVTGNSISVTKRCVPLEECLSTGCRDSEHEGYKICTSCCEGNICNLPLPRNDTDATFATTSPINQTNGHPHCVSVIVSCLWVWLGLTL | Function: Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain . Inhibits nicotine-induced Ca(2+) influx through nAChRs (By similarity). In vitro, specifically inhibits alpha-3:beta-4 and alpha-7 nAChR currents in an allosteric manner (By similarity). Acts as a positive regulator of Wnt/beta-catenin signaling (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 19051
Sequence Length: 171
Domain: The UPAR/Ly6 domain is sufficient for inhibiting alpha-3:beta-4 and alpha-7-dependent nAChR currents.
Subcellular Location: Secreted
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A2VE33 | MKSFLFAGIVVVLTVAAVDTLRCIQCNSLKDSCVAKNATECPSNATTSCTSFSTNFYHGEHPTWYEDHACSEENCSNTTVESFTVSVSENETFHFESQCCLGEPCNQTSNTTASPHQVGSGNMECPACYGNNETSCNETRKCYGERCVSIIAEFTNETKTLVLKGCSNVSISTCESLGAGNQTFRGVTFRKFECGDNFSTTTPLATTDTGSQASFTPLALASILLLSLLL | Function: Secreted protein specifically required to prevent invasion of Gram-negative bacteria in the inner mucus layer of the colon epithelium, a portion of the large intestine which is free of commensal microbiota. Prevents invasion of flagellated microbiota by binding to the flagellum of bacteria, such as P.mirabilis, thereby inhibiting bacterial motility in the intestinal lumen. Segregation of intestinal bacteria and epithelial cells in the colon is required to preserve intestinal homeostasis.
PTM: Highly N-glycosylated. Not O-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24724
Sequence Length: 230
Subcellular Location: Cell membrane
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Q6UX82 | MKGILVAGITAVLVAAVESLSCVQCNSWEKSCVNSIASECPSHANTSCISSSASSSLETPVRLYQNMFCSAENCSEETHITAFTVHVSAEEHFHFVSQCCQGKECSNTSDALDPPLKNVSSNAECPACYESNGTSCHGKPWKCYEEEQCVFLVAELKNDIESKSLVLKGCSNVSNATCQFLSGENKTLGGVIFRKFECANVNSLTPTSAPTTSHNVGSKASLYLLALASLLLRGLLP | Function: Secreted protein specifically required to prevent invasion of Gram-negative bacteria in the inner mucus layer of the colon epithelium, a portion of the large intestine which is free of commensal microbiota. Prevents invasion of flagellated microbiota by binding to the flagellum of bacteria, such as P.mirabilis, thereby inhibiting bacterial motility in the intestinal lumen. Segregation of intestinal bacteria and epithelial cells in the colon is required to preserve intestinal homeostasis.
PTM: Highly N-glycosylated. Not O-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25265
Sequence Length: 237
Subcellular Location: Cell membrane
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Q9D7S0 | MRGVFIAGVIAAFAITVVDSLNCTQCYTYNSTCDGQATECNEQSFSCVESSINSTLGGFLHVYQNKFCSASNCTENSTEVAFTVHLFDDQRYHFASQCCQGESCNATHSESGTQNVTDMQCMSCYGHNKTLCEEKPQKCYEGEQCVFIIAEMVNGSGRVELKGCSDISNSTCQFLSPGNTTVGEFVFKSVECTQPTEYTNSTTTIPPITNTSLTSVTRPGIKTSPASVTPQASMGTKASFTSSIFGSLLLLKLLF | Function: Secreted protein specifically required to prevent invasion of Gram-negative bacteria in the inner mucus layer of the colon epithelium, a portion of the large intestine which is free of commensal microbiota. Prevents invasion of flagellated microbiota by binding to the flagellum of bacteria, such as P.mirabilis, thereby inhibiting bacterial motility in the intestinal lumen. Segregation of intestinal bacteria and epithelial cells in the colon is required to preserve intestinal homeostasis.
PTM: Highly N-glycosylated. Not O-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 27524
Sequence Length: 255
Subcellular Location: Cell membrane
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Q5ZU17 | MTYSFSKPVSWVFLFTAVIYLVSLSFIQYPATTVLKPIPIVCLIVGVFRTSLSSSAKILLILALVFSLAGDVVLTLPFSLQLELGIACFLLAHCFYITLFLKSFEFNRLHLFYYLPIFLFMGFAAFTMIPYLGNLLIPVMIYFCVLMLMVFSAFQVKKETLTISSGALFFLISDLTLALNLFIYTQADVRIFVMFTYYVAQFLLTFGLVRLYEKGG | Function: Specifically hydrolyzes the vinyl ether bond of lysoplasmenylcholine (pLPC) and lysoplasmenylethanolamine (pLPE) to release a fatty aldehyde and glycerophospho-choline or glycerophospho-ethanolamine . Has no activity on diradyl plasmalogen, 1-alkenyl-glycerol, and monoacylglycerophospho-ethanolamine or monoacylglycerophospho-choline . May serve to protect the bacterium from lysis by lysoplasmalogen derived from plasmalogens of the host .
Catalytic Activity: 1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + H2O = a 2,3-saturated aldehyde + sn-glycerol 3-phosphocholine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24536
Sequence Length: 216
Subcellular Location: Cell inner membrane
EC: 3.3.2.2
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P64838 | MGSIAGFSSAVLSKLGIPVPYAPRLLAGGWVVAGWAGLAYGVYLTVIALRLPPGSELTGHAMLQPAFKASMAVLLAAAAVAHPIGRERRWLVPALLLSATGDWLLAIPWWTWAFVFGLGAFLLAHLCFIGALLPLARQAAPSRGRVAAVVAMCVASAGLLVWFWPHLGKDNLTIPVTVYIVALSAMVCTALLARLPTIWTAVGAVCFAASDSMIGIGRFILGNEALAVPIWWSYAAAEILITAGFFFGREVPDNAAAPTDS | Function: Specifically hydrolyzes the vinyl ether bond of lysoplasmenylcholine (pLPC) and lysoplasmenylethanolamine (pLPE) to release a fatty aldehyde and glycerophospho-choline or glycerophospho-ethanolamine.
Catalytic Activity: 1-O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + H2O = a 2,3-saturated aldehyde + sn-glycerol 3-phosphocholine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27391
Sequence Length: 261
Subcellular Location: Cell membrane
EC: 3.3.2.2
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Q5VWZ2 | MAAASGSVLQRCIVSPAGRHSASLIFLHGSGDSGQGLRMWIKQVLNQDLTFQHIKIIYPTAPPRSYTPMKGGISNVWFDRFKITNDCPEHLESIDVMCQVLTDLIDEEVKSGIKKNRILIGGFSMGGCMAIHLAYRNHQDVAGVFALSSFLNKASAVYQALQKSNGVLPELFQCHGTADELVLHSWAEETNSMLKSLGVTTKFHSFPNVYHELSKTELDILKLWILTKLPGEMEKQK | Function: Has depalmitoylating activity toward KCNMA1. Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site.
Catalytic Activity: H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]
Sequence Mass (Da): 26316
Sequence Length: 237
Subcellular Location: Cytoplasm
EC: 3.1.2.22
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Q9DD65 | MRTLVVLLLVAVANARVYERCEWARLLRNQGMDGYRGISLANWVCLTEWESHYNTRATNHNTDGSTDYGIFQINSRWWCNDSQTPTSNACNIRCSELLTDDVIVAIKCAKRVVRDPNGIGAWVAWRQHCQGQDLSSYLAGCGL | Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 16169
Sequence Length: 143
Subcellular Location: Secreted
EC: 3.2.1.17
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C1IIX1 | MRVLPLALLVGLLAVSDAKVLGKCEFARLLETRYNLSRNDIKNWVCIAEFESSFNTAATNRNRNRSTDYGIFQINNKYWCGSDYGKNVCGIPCSDLMSDDITAALRCAETVRRATERYRGRGKGYTAWVAYNSKCKKRDLDQYMAECWSRGSNSIFPF | Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents (By similarity). Has bacteriolytic activity against Gram-positive bacterium M.luteus, and Gram-negative shrimp pathogenic bacteria V.alginolyticus, V.parahaemolyticus and V.vulnificus. May play a role in host defense .
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 17999
Sequence Length: 158
Subcellular Location: Secreted
EC: 3.2.1.17
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Q9HWK6 | MHKRTYLNACLVLALAAGASQALAAPGASEMAGDVAVLQASPASTGHARFANPNAAISAAGIHFAAPPARRVARAAPLAPKPGTPLQVGVGLKTATPEIDLTTLEWIDTPDGRHTARFPISAAGAASLRAAIRLETHSGSLPDDVLLHFAGAGKEIFEASGKDLSVNRPYWSPVIEGDTLTVELVLPANLQPGDLRLSVPQVSYFADSLYKAGYRDGFGASGSCEVDAVCATQSGTRAYDNATAAVAKMVFTSSADGGSYICTGTLLNNGNSPKRQLFWSAAHCIEDQATAATLQTIWFYNTTQCYGDASTINQSVTVLTGGANILHRDAKRDTLLLELKRTPPAGVFYQGWSATPIANGSLGHDIHHPRGDAKKYSQGNVSAVGVTYDGHTALTRVDWPSAVVEGGSSGSGLLTVAGDGSYQLRGGLYGGPSYCGAPTSQRNDYFSDFSGVYSQISRYFAP | Function: Lysine-specific endoprotease . Involved in corneal virulence.
PTM: Experiments performed in E.coli. Processing of pro-endopeptidase to mature endopeptidase is probably autocatalytic, as mutations in the probable active site residues prevent processing, and purified inactive pro-endopeptidase disappears in the presence of active endopeptidase.
Catalytic Activity: Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro.
Sequence Mass (Da): 48213
Sequence Length: 462
Subcellular Location: Secreted
EC: 3.4.21.50
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P21776 | SKMKKCEFAKIAKEQHMDGYHGVSLADWVCLVNNESDFNTKAINRNKGI | Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 5570
Sequence Length: 49
Subcellular Location: Secreted
EC: 3.2.1.17
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Q976J8 | MVVLKCPVCNGDVNVPDDALPGEIVEHECGAQLEVYNDHGRLALRLAEQVGEDWGE | Function: Carrier protein that bears the covalently bound substrates for arginine and lysine biosynthesis; bound L-glutamate is sequentially converted to L-ornithine, while bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine.
PTM: Formation of an isopeptide bond between the gamma-carboxyl group of the C-terminal glutamate and the amino group of alpha-aminoadipate (AAA) is catalyzed by LysX. The bound AAA is then converted to L-lysine in a series of reactions catalyzed by LysZ, LysY and LysJ. Release of the product L-lysine is catalyzed by LysK. Formation of an isopeptide bond between the gamma-carboxyl group of the C-terminal glutamate and the amino group of L-glutamate is catalyzed by ArgX. The bound substrate is then sequentially converted to ornithine which is eventually converted to L-arginine .
Sequence Mass (Da): 6104
Sequence Length: 56
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway.
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Q5SH22 | MVGTCPECGAELRLENPELGELVVCEDCGAELEVVGLDPLRLEPAPEEAEDWGE | Function: Carrier protein that bears the covalently bound substrates for lysine biosynthesis; the bound alpha-aminoadipate (AAA) is sequentially converted to L-lysine.
PTM: Formation of an isopeptide bond between the gamma-carboxyl group of the C-terminal glutamate and the amino group of alpha-aminoadipate (AAA) is catalyzed by LysX. The bound AAA is then converted to L-lysine in a series of reactions catalyzed by LysZ, LysY and LysJ. Release of the product L-lysine is catalyzed by LysK .
Sequence Mass (Da): 5812
Sequence Length: 54
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway.
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O06136 | MVAAAGEPLNCQRANPEVTVKLPSADVVPRLRGRQRVVVHVDSRTARCVGALALVCAACWLIALLAGDYRHAQWAVAGRLGWSLTVLAAVAFIARGIFLGRPVTAMHATAAGLFLLAGLAAHVLVADLLGEILIAGSGWALMWPTSAHPRPEDLPRVWALINATRADSLAPFAMQAGKSHHFSAAGTAALAYRTRIGYAVVSGDPIGDEAQFPQLVADFAAMCHMHGWRIVVVGCSERRLGLWSDPMVVGQSLRPIPIGRDVVIDVSNFEMTGRRFRNLRQAVKRTHNFGVTTEIVAEQQLDDQRQAELAEVLAASPSGARTDRGFCMNLDGVLEGRYPGIQLIIARDASGRVQGFHRYATAGGGSDMSLDVPWRRRGAPNGIDERLSADMIAAAKDAGVQRLSLAFAAFPDLFGANQLGRLQRVCRALIHILDPLIALESLYRYLRKFHALDERRYVLISMTQVFALALVLLSLEFVPRRRHL | Function: Plays a role in mycobacterial fitness . Likely enhances survival of pathogenic strains . Considerably reduces the overall net negative charge on bacterial surface when bacteria are exposed to an acidic environment .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52642
Sequence Length: 484
Domain: Unlike homologous domains of MprF and LysX that are positioned in the cytoplasm, the MprF-like domain of LysX2 is in the extracytoplasmic region.
Subcellular Location: Cell inner membrane
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P37161 | MRALLGICVLALVTPAVLGRTMDRCSLAREMANMGVSRDQLSKWACIAEHESSYRTGVVGPPNTDGSNDYGIFQINDMYWCQPSSGKFSHNGCDVSCNALLTDDIKSSVRCALKVLGQQGWSAWSTWHYCSGYLPPIDDCFV | Function: Unlikely to play an active role in the humoral immune defense. May have a function in the digestion of bacteria in the food. May be involved in the clearance of bacteria from the larval gut before metamorphosis.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 15591
Sequence Length: 142
EC: 3.2.1.17
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Q02978 | MAATASAGAGGIDGKPRTSPKSVKFLFGGLAGMGATVFVQPLDLVKNRMQLSGEGAKTREYKTSFHALTSILKAEGLRGIYTGLSAGLLRQATYTTTRLGIYTVLFERLTGADGTPPGFLLKAVIGMTAGATGAFVGTPAEVALIRMTADGRLPADQRRGYKNVFNALIRITREEGVLTLWRGCIPTMARAVVVNAAQLASYSQSKQFLLDSGYFSDNILCHFCASMISGLVTTAASMPVDIAKTRIQNMRMIDGKPEYKNGLDVLFKVVRYEGFFSLWKGFTPYYARLGPHTVLTFIFLEQMNKAYKRLFLSG | Function: Catalyzes the transport of 2-oxoglutarate (alpha-oxoglutarate) across the inner mitochondrial membrane in an electroneutral exchange for malate. Can also exchange 2-oxoglutarate for other dicarboxylic acids such as malonate, succinate, maleate and oxaloacetate, although with lower affinity. Contributes to several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism (By similarity). Maintains mitochondrial fusion and fission events, and the organization and morphology of cristae . Involved in the regulation of apoptosis (By similarity). Helps protect from cytotoxic-induced apoptosis by modulating glutathione levels in mitochondria (By similarity).
Catalytic Activity: (S)-malate(in) + 2-oxoglutarate(out) = (S)-malate(out) + 2-oxoglutarate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34062
Sequence Length: 314
Subcellular Location: Mitochondrion inner membrane
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Q9CR62 | MAATASPGAGRMDGKPRTSPKSVKFLFGGLAGMGATVFVQPLDLVKNRMQLSGEGAKTREYKTSFHALTSILKTEGLKGIYTGLSAGLLRQATYTTTRLGIYTVLFERLTGADGTPPGFLLKALIGMTAGATGAFVGTPAEVALIRMTADGRLPADQRRGYKNVFNALVRIAREEGVPTLWRGCIPTMARAVVVNAAQLASYSQSKQFLLDSGYFSDNILCHFCASMISGLVTTAASMPVDIVKTRIQNMRMIDGKPEYKNGLDVLLKVVRYEGFFSLWKGFTPYYARLGPHTVLTFIFLEQMNKAYKRLFLSG | Function: Catalyzes the transport of 2-oxoglutarate (alpha-oxoglutarate) across the inner mitochondrial membrane in an electroneutral exchange for malate. Can also exchange 2-oxoglutarate for other dicarboxylic acids such as malonate, succinate, maleate and oxaloacetate, although with lower affinity. Contributes to several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism (By similarity). Maintains mitochondrial fusion and fission events, and the organization and morphology of cristae (By similarity). Involved in the regulation of apoptosis . Helps protect from cytotoxic-induced apoptosis by modulating glutathione levels in mitochondria (By similarity).
Catalytic Activity: (S)-malate(in) + 2-oxoglutarate(out) = (S)-malate(out) + 2-oxoglutarate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34155
Sequence Length: 314
Subcellular Location: Mitochondrion inner membrane
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P0C582 | MSSVKQSAQAATSDVVDTAKNATAETVTAATDFLHTPAVRAALPFINGGLSGMVATTVIQPIDMIKVRIQLAGEGKAGGPKPTPLGVTRDIIASGKAMDLYTGLSAGLLRQAVYTTARIGCFDTFMSRLSARAKEKGQSVGFKERASAGLAAGGLAAMIGNPADLALIRMQSDGLKPVAERKNYKSVIDALGGIARNEGVAALWAGAAPTVVRAMALNFGQLAFFSEAKAQLKARTQWSSKVQTLSASAIAGFFASFFSLPFDFVKTRLQKQTRGPDGKLPYNGMVDCFAKVAKQEGVFRFYRGFGTYYVRIAPHAMVTLLVADYLGWLTK | Function: Catalyzes the transport of 2-oxoglutarate across the inner mitochondrial membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35047
Sequence Length: 331
Subcellular Location: Mitochondrion inner membrane
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F1RFX9 | MQSWDPCLTPLELHGALFLHGPYWTPGLFRLIALGTCGDSCTHVRQPPKTWMGATVFVQPLDLVKNRMQLSGEGAKTREYKTSFHALTSILRAEGLRGIYTGLSAGLLRQATYTTTRLGIYTVLFERLTGADGTPPGFLLKALIGMTAGATGAFVGTPAEVALIRMTADGRLPPDQRRGYKNVFDALIRIVREEGVPTLWRGCIPTMARAVVVNAAQLASYSQSKQFLLDSGYFSDNILCHFCASMISGLVTTAASMPVDIAKTRIQNMRTIDGKPEYKNGLDVLVKVIRYEGFFSLWKGFTPYYARLGPHTVLTFIFLEQMNKAYKRLFLSG | Function: Catalyzes the transport of 2-oxoglutarate (alpha-oxoglutarate) across the inner mitochondrial membrane in an electroneutral exchange for malate . Can also exchange 2-oxoglutarate for other dicarboxylic acids such as malonate, succinate, maleate and oxaloacetate, although with lower affinity . Contributes to several metabolic processes, including the malate-aspartate shuttle, the oxoglutarate/isocitrate shuttle, in gluconeogenesis from lactate, and in nitrogen metabolism (By similarity). Maintains mitochondrial fusion and fission events, and the organization and morphology of cristae (By similarity). Involved in the regulation of apoptosis (By similarity). Helps protect from cytotoxic-induced apoptosis by modulating glutathione levels in mitochondria (By similarity).
Catalytic Activity: (S)-malate(in) + 2-oxoglutarate(out) = (S)-malate(out) + 2-oxoglutarate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36777
Sequence Length: 333
Subcellular Location: Membrane
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P16947 | MARKDTNKQYSLRKLKTGTASVAVAVAVLGAGFANQTEVKAAEKKVEAKVEVAENNVSSVARREKELYDQIADLTDKNGEYLERIGELEERQKNLEKLEHQSQVAADKHYQEQAKKHQEYKQEQEERQKNQEQLERKYQREVEKRYQEQLQKQQQLETEKQISEASRKSLSRDLEASREAKKKVEADLAALTAEHQKLKEEKQISDASRQGLSRDLEASREAKKKVEADLAALTAEHQKLKEEKQISDASRQGLSRDLEASREAKKKVEADLAEANSKLQALEKLNKELEEGKKLSEKEKAELQARLEAEAKALKEQLAKQAEELAKLKGNQTPNAKVAPQANRSRSAMTQQKRTLPSTGETANPFFTAAAATVMVSAGMLALKRKEEN | Function: This protein is one of the different antigenic serotypes of protein M. Protein M is closely associated with virulence of the bacterium and can render the organism resistant to phagocytosis.
Location Topology: Peptidoglycan-anchor
Sequence Mass (Da): 43915
Sequence Length: 389
Subcellular Location: Secreted
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Q96PG2 | MKAEATVIPSRCARGLPSWQVLSPVQPWQTSAPQNTTQPKLLAPHQHEKSQKKSSLLKELGAFHITIALLHLVFGGYLASIVKNLHLVVLKSWYPFWGAASFLISGILAITMKTFSKTYLKMLCLMTNLISLFCVLSGLFVISKDLFLESPFESPIWRMYPNSTVHIQRLELALLCFTVLELFLPVPTAVTAWRGDCPSAKNDDACLVPNTPLHLKGLPVEPPPSYQSVIQGDAQHKQHQRLREVKQVAPDTWIVTDGAAIWTQTAN | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29747
Sequence Length: 267
Subcellular Location: Membrane
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Q99N03 | MAGQAPTAVPGSVTGEVSRWQNLGPAQPAQKVAQPQNLVPDGHLEKALEGSDLLQKLGGFHIAIAFAHLAFGGYLISTVKNLHLVVLKCWYPLWGTVSFLVAGMAAMTTVTFPKTSLKVLCVIANVISLFCALAGFFVIAKDLFLEGPFPWPIWRPYPEPTTYIQRLELTLFCFTFLEIFLSGSTAITAYRMKRLQAEDKDDTPFVPDTPMELKGLSLGPPPSYKDVAQGHSSSDTGRALATSSGLLLASDSFHQALLHTGPRTLRK | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28972
Sequence Length: 267
Subcellular Location: Membrane
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Q9NXJ0 | MMSSKPTSHAEVNETIPNPYPPSSFMAPGFQQPLGSINLENQAQGAQRAQPYGITSPGIFASSQPGQGNIQMINPSVGTAVMNFKEEAKALGVIQIMVGLMHIGFGIVLCLISFSFREVLGFASTAVIGGYPFWGGLSFIISGSLSVSASKELSRCLVKGSLGMNIVSSILAFIGVILLLVDMCINGVAGQDYWAVLSGKGISATLMIFSLLEFFVACATAHFANQANTTTNMSVLVIPNMYESNPVTPASSSAPPRCNNYSANAPK | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28069
Sequence Length: 267
Subcellular Location: Membrane
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Q2YDM3 | MTGIFCIFMWYLLLILYMGQIKGVFGTYEPITYKTGCSLWGIFFIISGISIIRATWYPSQRQLTCAMLENILCMILAIISMILTIVELSTFKSVSYRNYGQAKLGRQISRVLLSFYPLEVSMALTYSIFGCVGLCRKKEDARTADTEEVEDAF | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17429
Sequence Length: 153
Subcellular Location: Membrane
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Q5J8X5 | MIGIFHIFMWYFLLVLYMGQIKGAFGTYEPVTYKTGCTLWGIFFIIAGVFLIRVTKYPTRSGIISTLIINIICIITTITAVTLTIIELSHFNSVSYRNYGQAKLGREVSRILLFFYGLEFSIALTHSIYSCSNLFRRQNDLTSVTEEAESTP | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17307
Sequence Length: 152
Subcellular Location: Membrane
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Q5FWC3 | MECRNPKVSSANITVLGVIQIMIGIYHVLMWYFLLLLYMGQIKGVFGTYEPVTYKMGTSLWGFAFVISGAFTVKAAKYQSRHMILCTMSLNILCIIITIVAASLTIVELSHFRSVSYRNYGQAKLGREVSRVLLCSYPLEFAIALLYSISSCAYLPLSSIVKSLVRKTWRLSSLAAWRQMIWLEAGNQEETLESVTEVVEGNS | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22802
Sequence Length: 203
Subcellular Location: Membrane
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Q96JA4 | MESTSQDRRATHVITIKPNETVLTAFPYRPHSSLLDFLKGEPRVLGATQILLALIIVGFGTIFALNYIGFSQRLPLVVLTGYPFWGALIFILTGYLTVTDKKSKLLGQGVTGMNVISSLVAITGITFTILSYRHQDKYCQMPSFEEICVFSRTLFIVLFFLPSDVTQNSEQPAPEENDQLQFVLQEEFSSDDSTTNAQSVIFGGYAFFKLTLSRSPLVSQPGNKGREFVPDEQKQSILPSPKFSEEEIEPLPPTLEKKPSENMSIQLDSTFKQMKDEDLQSAIVQPSQMQTKLLQDQAASLQVFPSHSALKLEDISPEDLPSQALPVEGLSEQTMPSKSTSSHVKQSSNLTANDLPPQGILSQDTSSQDMLFHDMTSQDMQSLDMLSQDTPSHAMPPQDIPSQDMLSQALSAHAILPEASTSHIVQFPEIQHLLQQPPDLQPENTEPQNQQILQMSYQDIRSEVMEETKEWKSEEELHRRKSSRRHSLNQQTKALQYLRRHSLDVQAKGQKSSKRHSLDQQSKGWQSPKQKSLDQQIKDWLSPKRHSVDKQAQLNQTKEQLPDQQAEDQQAKGEQYPEGQSKDGQVKDQQTDKEQNSKKQTQDQQTEDQPAQEKKSPKGQFQNVQAEGQQAQVEKVPKLLCQDSESQIQQYQFWQFHKGNLQAGQPRTVNLLAKNPLTG | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76580
Sequence Length: 679
Subcellular Location: Membrane
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Q8N5U1 | MSAAPASNGVFVVIPPNNASGLCPPPAILPTSMCQPPGIMQFEEPPLGAQTPRATQPPDLRPVETFLTGEPKVLGTVQILIGLIHLGFGSVLLMVRRGHVGIFFIEGGVPFWGGACFIISGSLSVAAEKNHTSCLVRSSLGTNILSVMAAFAGTAILLMDFGVTNRDVDRGYLAVLTIFTVLEFFTAVIAMHFGCQAIHAQASAPVIFLPNAFSADFNIPSPAASAPPAYDNVAYAQGVV | Function: May be involved in signal transduction as a component of a multimeric receptor complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25050
Sequence Length: 240
Subcellular Location: Membrane
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P57109 | MKLYTYYRSTSSYRVRIALALKGLDYQSLPVNLIRDGGEHRQPAYLALNPQGRVPALQVDEGELLIQSPAIIEYLEERYPQPALLSSDPLRRARERGVAALVGCDIHPLHNASVLNLLRQWGHDEEQVRQWIGHWVGQGLAAVEQLIGDQGWCFGDRPGLADVYLVPQLYAAERFGVALDAWPRIRRVADLAAAHPAFRQAHPANQPDTPAA | Catalytic Activity: 4-maleylacetoacetate = 4-fumarylacetoacetate
Sequence Mass (Da): 23685
Sequence Length: 212
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6.
EC: 5.2.1.2
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P57113 | MQAGKPVLYSYFRSSCSWRVRIALALKGIDYEIVPINLIKDGGQQFSEEFQTLNPMKQVPALKIDGITIGQSLAILEYLEETRPIPRLLPQDPQKRAIVRMISDLIASGIQPLQNLSVLKQVGQENQMPWAQKAITSGFNALEKILQSTAGKYCVGDEVSMADVCLAPQVANAERFKVDLSPYPTISHINKALLALEAFQVSHPCRQPDTPAELRT | Cofactor: Glutathione is required for the MAAI activity.
Function: Probable bifunctional enzyme showing minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1, 3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with t-butyl and cumene hydroperoxides (By similarity). Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.
PTM: The N-terminus is blocked.
Catalytic Activity: 4-maleylacetoacetate = 4-fumarylacetoacetate
Sequence Mass (Da): 23961
Sequence Length: 216
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6.
Subcellular Location: Cytoplasm
EC: 5.2.1.2
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Q9X4F7 | MANETVLYDYWRSSASYRVRIALNLCGEAYRSVPVDLLAKAHRAPEHLARNPQGLVPVLDIDGERLTQSLAIIEYLAETRDGTGLLPAHPIDRQRVRALSYAVAMDIHPVCNLGVVARVMAGAGDGEAARREWMQKFIGEGLAAFERMLDHPATGAFCHGDRPTMADLCLVPQVYNARRWDVDLAACPLLVAIDRRCAGIDAFQRAHPDRAKP | Catalytic Activity: 4-maleylacetoacetate = 4-fumarylacetoacetate
Sequence Mass (Da): 23525
Sequence Length: 213
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6.
EC: 5.2.1.2
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Q9KSB2 | MMSLILYGYWRSSAAYRVRIALNIKQLVYESRAVHLSREGGEQHHAEFHRLNPSELIPVLIDGELCLNQSLAIIEYLDETYPAPRLIPERGAERYQVKALALDIAADIHPINNLRILQYLTAKLGVADEEKNRWYRHWIDKGFQGLEEKLRHTAGEYCVGNRLSLVDVCLVPQVYNAERFDLDMSRYPTLQQIAARLRALPAFAQAAPENQPDAC | Catalytic Activity: 4-maleylacetoacetate = 4-fumarylacetoacetate
Sequence Mass (Da): 24628
Sequence Length: 215
Pathway: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 5/6.
EC: 5.2.1.2
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Q3AEU2 | MRIKDVLFVKGSSGFYFDDQKAIKSGAVTDGFTYKGKPLTPGFSRVRQGGEAVSIMLFLENGEIAVGDCVAVQYSGVDGRDPVFLADNFIEVLEEEIKPRLVGYNLVRFREAARYFTNLTDKRGKRYHTALRYGLTQALLDAVAKINRTTMAEVIAEEYGLDLTLNPVPLFAQSGDDRYINADKMILKRVDVLPHGLFNHPAKTGEEGKNLTEYALWLKQRIKTLGDHDYLPVFHFDVYGTLGTVFNDNLDRIADYLARLEEKVAPHPLQIEGPVDLGSKERQIEGLKYLQEKLITLGSKVIIVADEWCNNLSDIKEFVDAGAGGMVQIKSPDLGGVNDIIEAVLYAKEKGTGAYLGGSCNETDVSAKITVHVGLATGPAQLLVKPGMGVDEGLTIMRNEMMRTLAILQRNKVTFQKKVG | Function: Involved in the methylaspartate cycle. Catalyzes the formation of the alpha,beta-unsaturated bond by the reversible anti elimination of ammonia from L-threo-beta-methylaspartate (L-threo-(2S,3S)-3-methylaspartate) to give mesaconate. It can also catalyze the amination of fumarate and ethylfumarate, and the deamination of hydroxylamine, hydrazine, methylamine and ethylamine.
Catalytic Activity: (2S,3S)-3-methyl-L-aspartate = mesaconate + NH4(+)
Sequence Mass (Da): 46398
Sequence Length: 420
Pathway: Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 2/4.
EC: 4.3.1.2
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Q05514 | MKIVDVLCTPGLTGFYFDDQRAIKKGAGHDGFTYTGSTVTEGFTQVRQKGESISVLLVLEDGQVAHGDCAAVQYSGAGGRDPLFLAKDFIPVIEKEIAPKLIGREITNFKPMAEEFDKMTVNGNRLHTAIRYGITQAILDAVAKTRKVTMAEVIRDEYNPGAEINAVPVFAQSGDDRYDNVDKMIIKEADVLPHALINNVEEKLGLKGEKLLEYVKWLRDRIIKLRVREDYAPIFHIDVYGTIGAAFDVDIKAMADYIQTLAEAAKPFHLRIEGPMDVEDRQKQMEAMRDLRAELDGRGVDAELVADEWCNTVEDVKFFTDNKAGHMVQIKTPDLGGVNNIADAIMYCKANGMGAYCGGTCNETNRSAEVTTNIGMACGARQVLAKPGMGVDEGMMIVKNEMNRVLALVGRRK | Function: Involved in the methylaspartate cycle. Catalyzes the formation of the alpha,beta-unsaturated bond by the reversible anti elimination of ammonia from L-threo-beta-methylaspartate (L-threo-(2S,3S)-3-methylaspartate) to give mesaconate. It can also use L-erythro-beta-methylaspartate (L-erythro-(2S,3R)-3-methylaspartate), L-aspartate, fumarate and ethylfumarate as substrates.
Catalytic Activity: (2S,3S)-3-methyl-L-aspartate = mesaconate + NH4(+)
Sequence Mass (Da): 45534
Sequence Length: 413
Pathway: Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 2/4.
EC: 4.3.1.2
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Q5V465 | MRIEDVRTVPGLSGFFFDDQQAIKDGATQTGFAYDGQPVTDGFDRIREAGEALIVEIELADGSIATGDCAAVQYSGAGGRDPLFRAEKYRPVVEGAVADALRGQDATQFGANATMLEEMSPQRSGGDQLHTAVRYGVSQALLNAAAQARGVTPTDVLADTYDTEPATSPVPVFGQSGDERRINAEKMLIKGVPVLPHGLFNSVEKVGENGEGLRDYLAWLSDRATALGPEPYSPRFHVDVYGILGKVFGPPYDRTEVTDYFETLREAAAPYPLQVEGPMDAGGRQAQITEMAELREGLADAGVDVDIVADEWCNTFEDVQAFVDAEAADLVQIKTPDLGGIQRSAEAVLYCDGTDTRAYVGGTCNETVTSARACAHVALATDAAQVLAKPGMGFDEGFMVVTNEMRRALARRDATQEVPADD | Function: Involved in the methylaspartate cycle. Catalyzes the formation of the alpha,beta-unsaturated bond by the reversible anti elimination of ammonia from L-threo-beta-methylaspartate (L-threo-(2S,3S)-3-methylaspartate) to give mesaconate (Probable).
Catalytic Activity: (2S,3S)-3-methyl-L-aspartate = mesaconate + NH4(+)
Sequence Mass (Da): 45117
Sequence Length: 422
Pathway: Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 2/4.
EC: 4.3.1.2
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P37515 | MLRTEKEKMAAGELYNSEDQQLLLERKHARQLIRQYNETPEDDAVRTKLLKELLGSVGDQVTILPTFRCDYGYHIHIGDHTFVNFDCVILDVCEVRIGCHCLIAPGVHIYTAGHPLDPIERKSGKEFGKPVTIGDQVWIGGRAVINPGVTIGDNAVIASGSVVTKDVPANTVVGGNPARILKQL | Function: Catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars. Acetylates glucose exclusively at the C6 position and maltose at the C6 position of the non-reducing end glucosyl moiety. Is able to acetylate maltooligosaccharides.
Catalytic Activity: acetyl-CoA + D-maltose = 1-O-acetylmaltose + CoA
Sequence Mass (Da): 20210
Sequence Length: 184
EC: 2.3.1.79
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P77791 | MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLAEEHTLRQQILADLFGQVTEAYIEPTFRCDYGYNIFLGNNFFANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPIDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL | Function: Catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars . Acetylates glucose exclusively at the C6 position and maltose at the C6 position of the non-reducing end glucosyl moiety. Is able to acetylate maltooligosaccharides .
Catalytic Activity: acetyl-CoA + D-maltose = 1-O-acetylmaltose + CoA
Sequence Mass (Da): 20096
Sequence Length: 183
EC: 2.3.1.79
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P40333 | MFAVFWTNLRCLGYNTFTCGVETPTTWGKVGSLDASSSTFTTYRGYPLAMAISAGTPACDSPDDNIRRAINTLRADLSALLRGESVAYSAFLSACTKFDGFAQSCHGMLSDDTLDLLYSFSESLLALSENMALLETKKEAESNKFTAEVMAILSDKTSGLDLSDDKNEPTSPTPAYVEPCARWLKDNWYNPYPSGEVRTQIARQTRTSRKDIDAWFIDARRRIGWNEVRRKHFENKRVDIVRAASIFTGPQSIPAEVDALPDHIELEFAGILSRARSLYEEKFSPSKLAVKLDTAVKDMTPSLKEQLKNDEARRKREASTVGIINQRARHAYPTPERSPASAAELLASPPSFAIDSDKLPSVGRKRRRSLESDETVSSPLCKRPRSQSVFCELSPVKGLPSPSPSTQDELLETSAAPSPQPSLLPKLTPTDSARSTGKRKRRLSDGFQYPAAKRPEIRPQVVSDPFPATSSEHWEQWFREHVLSSPELTLTGDIPPAVTTDAPDSNTPLDIQLFNFPLIPDLPPSVPVVPAPTAELNIIEPLEVPAVTQVNVDPEATALDHTFSWMASDFPPPLQSTNTFPSSSPFSALDGMSLPFPDTRSSAFLPDPSLWSNISDPDLDFSTVFSQPSTNSAMTSSIQVPLQPTWLTSRSLSEQEREAKRKELEELEARAQAIRAEISAP | Function: Has a major regulatory role in sexual and asexual development. It may bind DNA itself or it may have a role in preventing DNA-binding of another protein.
Sequence Mass (Da): 75057
Sequence Length: 681
Domain: The C-terminal domain has a high percentage of Ser, Pro and Thr residues.
Subcellular Location: Nucleus
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Q0PAR0 | MIFLKNICKNIGENAILKNVSLSIEKGEFVAIIGQSGSGKTSLLNIIGTLDTPSSGTYVFDEYEVTKLNNDEKARLRREKIGFIFQRYNLLSLLSAKENVSLPAVYAGKNLQERSQNAKKLLNDLELAHKLDSKPNELSGGQQQRVSIARALINGGELILADEPTGALDSKSGIMVLEILQKLNEQGHTIVLVTHDPKIAAQAKRVIEIKDGEILSDTKKEKAQEKLILKTMPKEKKTLTLLKNQAFECFKIAYSSILAHKLRSILTMLGIIIGIASVVCVVALGLGSQAKVLESIARLGTNTIEIRPGKGFGDLRSGKTRLNFSDLETLRSLEYLEAVDAHSNTSGVATYTNISLSARAEGVGVNNFAIEGLRIDAGRILNNDDVKNSTNVAVLDFNAKKNLFPDEKSENILGRVVLFNSQPFKIIGVLQKDTDKPIEDNVVRFYIPYTTLMNKLTGDRNLREIIVKVKDDVSSTLAENAIIRILEIKRGQKDFFTFNSDTFKQAITANKRTTTILTACVAVIALIVGGIGVMNIMLVSVSERTREIGIRMAIGARREDIMMQFLIEAVMICTIGAILGVILSIFVIFAFNTLSTDFPMILNAYSVLLGLLSSMFIGVVFGFFPARNAANLNPISALSKE | Function: Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70273
Sequence Length: 641
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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Q3B5J7 | MAPTTPLLELVDVHRTYPVGESTVNALRGVSLEIREGEFVAIMGSSGSGKSSLLHILGLLDNPDRGEYRILGRNVNALPEDGQAGLRNHVAGFVFQQFHLLKRMSIVDNVRLPHIYSGLKGDFRHEALESLKKVGLMHRLDHTPGQLSGGEQQRVAIARALIGNPMILFADEPTGNLDSRNSLEIMKILEELHREGRTIVMVTHEDEIAAYADRVITMRDGLVVSDQRRDRVCLPAGPSVPLTLDPHAMMDASRNLSVWQDGRFIGFVQQAFQSIFANKVRSLLSVLGILVGVASVIAMMALGEGAKVSIEEELKSMGSNLISVRGGSARVRGAAQGDGAVARFTFKDVKDISRMHSLVKGAAGTVNGSGQIVFGNRNWSTTLDGVGYEYGSMRAFVPSIGRWFTRDEIRKREKVAVIGVTVARELFGNNNPIGHTVKINRINFKVIGIAPAKGFSTHRDQDDVVLVPVTTAMYRVLGRDYLNSIYVEVRSAEGIDGAKEAVSDLIVKNHRLREGDDSFNIRDMTEIQEMLSSTTRTMSMLLGAIAAISLLVGGIGIMNIMLVSVTERTREIGLRKAIGARREDIMLQFLVESVGLTLSGGIIGIIAGIGISALLAVFAGWAVKTSIVSIVLATFFSAITGIFFGLWPARKAAELRPVEALRYE | Function: Non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72260
Sequence Length: 664
Subcellular Location: Cell inner membrane
EC: 7.6.2.-
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O06924 | MQKEKVWDKLSTDTEERMNAANELFSDRKVVPSQNGVALLEAVIRAGDRINLEGNNQKQADFLAECLGSCDSEKINNLHMVQSAVPLPIHLDIFDKGIAKKLDFAYGGPMAAKVAEFLREGKLELGAIHTYLELFARYFMDLTPRVSLICAYEGDKDGNLYTGFNTEDTPVIAEATKFRQGIVIAQVNKLVDKVQRVDIPGEWVDAVIESPKPFYLEPLFTRDPANITDTQVLMGMMALKGIYGEYGVQRLNHGIGFFTAAIELLLPTYGNELGLKGKICKHFALNPHPTMIPAIEDGWVESIHSFGGELGMQKYCEARPDIFFIGPDGSMRSNRAYSQTAGHYATDMFIGGTLQIDKYGNSSTATASRVAGFGGAPNMGCDAKGRRHVTDSWLKCGAEFEDQAALLGDMPRGKRLVVQMQETFKEKMDPSFVEKLDAWNLAKNANLDLAPVMIYSDDLTHIVTEEGIAYLAKCRGLEERMAAIRGVAGYTEVGLSADPKETKTLRERGIVKTPEDLGIDRSRANRSMLAAKSVKDLVDCSGGLYEPPARFVNW | Function: Alpha subunit of the biotin-independent and biotin-dependent malonate decarboxylase multienzyme complex (EC 4.1.1.88 and EC 7.2.4.4, respectively). Acts as an acyl-carrier protein (ACP) transferase component. This first step in malonate decarboxylation involves the exchange of an acetyl thioester residue bound to the activated ACP subunit for a malonyl thioester residue. Has a weak activity with acetyl-CoA as substrate.
Catalytic Activity: acetyl-[ACP] + malonate = acetate + malonyl-[ACP]
Sequence Mass (Da): 61148
Sequence Length: 554
Subcellular Location: Cytoplasm
EC: 2.3.1.187
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O06923 | MEQLMSLFPAISTLFTQDPVISITRIALIIFGFFLSYFGFKRTLEPLIMVPMGLGMIAINAGVLFLEAGVVGTIHLDPLVSEPSVLVNLMQVNWLQPVYNFTFSNGLIACIVFFGIGAMSDISFILIRPWASIIVALFAEMGTFATLIIGIKMGLLPNEAAAVATIGGADGPMVLFASLILAKDLFVPIAIIAYLYLSLTYAGYPYLIKLLVPKKYRGLEVEMDFPEVSQRSKFVFSVLACMLLCLLLPVASPLILSFFLGIAIKEAQIEPFQNLLETTLTYGSTLFLGLLLGALCEAKTILDPKISLIVVLGITALLISGIGGVLGGWIVYWFSKGKFNPVIGIAGVSCLPTTAKIAQKTVTEENPYAVILPLAMGAGVCGLIVSAIATGVFISTLFLLN | Function: Beta subunit of the biotin-dependent malonate decarboxylase multienzyme complex (EC 7.2.4.4). Acts as an integral membrane-bound carboxybiotin protein decarboxylase by releasing the carboxyl group of the carboxylated biotin carrier MADF. The free energy of the decarboxylation reaction is used to pump Na(+) out of the cell.
Catalytic Activity: H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + n Na(+)(in) = CO2 + N(6)-biotinyl-L-lysyl-[protein] + n Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43024
Sequence Length: 401
Subcellular Location: Cell membrane
EC: 7.2.4.1
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Q13477 | MDFGLALLLAGLLGLLLGQSLQVKPLQVEPPEPVVAVALGASRQLTCRLACADRGASVQWRGLDTSLGAVQSDTGRSVLTVRNASLSAAGTRVCVGSCGGRTFQHTVQLLVYAFPDQLTVSPAALVPGDPEVACTAHKVTPVDPNALSFSLLVGGQELEGAQALGPEVQEEEEEPQGDEDVLFRVTERWRLPPLGTPVPPALYCQATMRLPGLELSHRQAIPVLHSPTSPEPPDTTSPESPDTTSPESPDTTSQEPPDTTSPEPPDKTSPEPAPQQGSTHTPRSPGSTRTRRPEISQAGPTQGEVIPTGSSKPAGDQLPAALWTSSAVLGLLLLALPTYHLWKRCRHLAEDDTHPPASLRLLPQVSAWAGLRGTGQVGISPS | Function: Cell adhesion leukocyte receptor expressed by mucosal venules, helps to direct lymphocyte traffic into mucosal tissues including the Peyer patches and the intestinal lamina propria. It can bind both integrin alpha-4/beta-7 and L-selectin, regulating both the passage and retention of leukocytes. Isoform 2, lacking the mucin-like domain, may be specialized in supporting integrin alpha-4/beta-7-dependent adhesion strengthening, independent of L-selectin binding.
PTM: The Ser/Thr-rich mucin-like domain may provide possible sites for O-glycosylation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40155
Sequence Length: 382
Subcellular Location: Membrane
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Q61826 | MESILALLLALALVPYQLSRGQSFQVNPPESEVAVAMGTSLQITCSMSCDEGVARVHWRGLDTSLGSVQTLPGSSILSVRGMLSDTGTPVCVGSCGSRSFQHSVKILVYAFPDQLVVSPEFLVPGQDQVVSCTAHNIWPADPNSLSFALLLGEQRLEGAQALEPEQEEEIQEAEGTPLFRMTQRWRLPSLGTPAPPALHCQVTMQLPKLVLTHRKEIPVLQSQTSPKPPNTTSAEPYILTSSSTAEAVSTGLNITTLPSAPPYPKLSPRTLSSEGPCRPKIHQDLEAGWELLCEASCGPGVTVRWTLAPGDLATYHKREAGAQAWLSVLPPGPMVEGWFQCRQDPGGEVTNLYVPGQVTPNSSSTVVLWIGSLVLGLLALVFLAYRLWKCYRPGPRPDTSSCTHL | Function: Cell adhesion leukocyte receptor expressed by mucosal venules, helps to direct lymphocyte traffic into mucosal tissues including the Peyer patches and the intestinal lamina propria. It can bind both the integrin alpha-4/beta-7 and L-selectin, regulating both the passage and retention of leukocytes. Both isoform 1 and isoform 2 can adhere to integrin alpha-4/beta-7. Isoform 2, lacking the mucin-like domain, may be specialized in supporting integrin alpha-4/beta-7-dependent adhesion strengthening, independent of L-selectin binding.
PTM: O-glycosylated; contains syalic acid. The Ser/Thr-rich mucin-like domain may provide possible sites for O-glycosylation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 43652
Sequence Length: 405
Subcellular Location: Membrane
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O06926 | MAKWTELQDKSFLEATARERAVGIVDEGTFTEFCGPFDKIYSPHLPLMGEAIEYDDGLVAGVGKIGKKPIFVISQEGRFIGGSIGEVSGAKMVKTIQLASDLYEEMVSEKPDLPEEMRPAVVISFETGGVRLHEANAGLLAHAEVMDQIQNCRGRVPIISLIGSRVGCFGGMGFVAAATDVIIMSQFGRLGLTGPEVIEQEMGKDEFDASDRALVYRTTGGKHKYIIGDCNYLAADSIRSFRETTTAVLQKPMEEIETFRRIGSMEKIKEQIELVKLSVSLKPKDSMDVWAHAGNENPESLINMTLDEFLAQAKRLKA | Function: Gamma subunit of the biotin-dependent malonate decarboxylase multienzyme complex (EC 7.2.4.4). The two subunits MADC and MADD are required for the transfer of the malonate carboxy group from the acyl-carrier protein (ACP) to the prosthetic group of the biotin carrier MADF. Required for the regeneration of ACP.
Catalytic Activity: malonyl-[ACP] + N(6)-biotinyl-L-lysyl-[protein] = acetyl-[ACP] + N(6)-carboxybiotinyl-L-lysyl-[protein]
Sequence Mass (Da): 34900
Sequence Length: 318
Subcellular Location: Cytoplasm
EC: 2.1.3.10
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G5EDB2 | MPILHQKIASTGGQPSTNSLALRRLPLVVIPRKRKYKNYVSRRRNTQLLASLRRCVSDPNVYKSYNHWKALLRPMTPIKSGAPTPKTVTPMPVPQIPPHQKMTPNPTPTQNPVQLPLPHAVSEKPGDKKSTGPTPSPVPSKAPISAAKLPGTVTKVAPLLSAAQPPPKTLAPAPGASETNSGSGPVSKQVSGKLTELKSKNGTVTEKTEKAVLRIPSSASTRAKAASAVAPEANPAPVPTATKPSPFAPAIAPLRDGAPAQPPAPIQASAPLRPPVAKQNSLQKPPEPKRSVGAPPKALPSELVNKIDGIEFLPQSSNQNTDDGQQPTTSTGGAKALRRAYGSKSGTTICAIGSPNVPSTSQPQQGDNEKRLIEKKLSLRKKKLSGEGVPPAGSMLTGSKSGVEIGLSSNLTTTNNNNNKEQTDEQRAKKTVNAVAAAFSTQAGSGNATTVDDPASTTTSKENPAAQPPKPKSAAVQNLISQLQLPASVSAKVDKIIACGDKARKPSRSGLQASQARPKVPEIVSSQRTQHQDDKDGHLIYSKGDFILNRFTIYDTLGEGTFGKVVRVNDSLSDTFMALKIIKNVSKYREAAKLEVKVLQKLAEKDPEKKNWVIHMGSYFDYNGHICLLFDLMGSSIFDFLKANHYKPYPMEQTLHITWQLCNAVKFLHDNKLTHTDLKPENILFVDSRYTTKLVDKKPLRVLHSTHVRLIDFGSATFDHEHHSIIVSTRHYRAPEVILELGWSQPCDVWSIGCILYELYTGVTLFQTHENREHLAMMERVLGDIPLRMAKRTKTKFFINGRLDWVNTSADAAYVRDNCKPLRRSMSCTDPEHVELFELIENMLMFEPLARMKLPEALQHRYFNRLPENLKIPCKMDASTNPRINGD | Function: Probable dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Negatively regulates p38 MAPK signaling to allow for the plasma membrane of body wall muscle cells to form projections, also called muscle arms, that extend and connect the body wall muscles to target motor neurons. Negative regulation of p38 MAPK signaling may in turn modulate the trafficking of the muscle specific receptor eva-1 to the lysosome, to ensure proper display of the eva-1 receptor on the plasma membrane of muscle cells and allow for muscle arm extension towards guidance cues.
Sequence Mass (Da): 96910
Sequence Length: 887
Subcellular Location: Cytoplasm
EC: 2.7.11.-
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Q757I6 | MSPTNNGRNKKLGPRRKVPGRVSKSKSRAKVQAGDAKRVLDANALKWEKVDVPDTLGDFGGFYGLEEIDGVDVEVVDGKVQFVARDESRLKSPADAVDGTDMVEVDEDAGMEDVTEFRNLDDVAEGELSALSDEGSASEDDGSDSSGSSDMDEDDDQELQSEIFNKDIGLDEAEAPELPSWTNTMKLSATVLQGLSRLGFSNPTEIQLQSIPKALDGHDIMGKASTGSGKTLAYGIPILEGIIRDDTDSRPIGLIFTPTRELAHQVTDHLREVGALLVKRNPYSIMCLTGGLSIQKQERLLKYKGSARVVVATPGRFLELLEKDQTLIDRFAKVDTLVLDEADRLLQDGHFEEFERILKHLSRARKFTNGKKHGWKTMIYSATFSLDYFNKLSNTSWKKMKKAPSENEMEEVLKHLMTKIPFRGKPLIIDTNPEQKVASQIKESLIECLPTERDLYVYYFVTLYPGTTLVFCNAIDSVKKLNAYLHNLKISAFQIHSSMLQKNRLKSLEKFQEQAKKNQALNKPTVLIASDVAARGLDIPGIQHVIHYHLPRSADVYIHRSGRTARAENEGVAVTICSPQEAMGPLRKLRRVLAGKAGSKGKRWQNEIALLPVEPDIVSQLRERSRLASALADSEIATSSLSKDDNWLKKAADDLGIDVDSDDETKDTFLAKNKTKKLNKQLDKSTSKSYKMELNALLNTPIRKDARKSYLTGGLSNLADDLTKKKGHSSIIGHDKVDALTLLKSKSKRAKR | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 83477
Sequence Length: 752
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q4WMS3 | MGQKRQRDSKNLTLHSKKRKKAENATATDSDDGWDGIVGADELNWKEVALPDRLEDAGGFYGLEEIEGVDIVRGSGNGEVKFKAVAGKPKKSILKKKALEDENPEYEEEWSGFSDDDADRPENASSTVVEKPEKSDRKADKKSEKNADKKEAKDAKKKEAKAAKKEQKEKGSAIQRDMSINAGLSFAALQDTEEDDGADVSAWDSLGLSPEILTGLSKMKFGSPTSVQEACIPQILEGHDVIGKASTGSGKTLAFGIPILEHYLEKKRDDISAQKEQMSEKDSTPIALILSPTRELAHQLSKHIGELIAQAPGVNARIALLTGGLSVQKQQRLLSGADIVIGTPGRVWEILSTGQGLIRKMQQIKFLVVDEADRLLSEGHFKEVEEILNSLDRVEDGEVPDGEDQASEEESDPSSERQTLVFSATFHRDLQQKLAGKRKWTRGDIMDKKESMDYLLQKLNFREEKPKFIDMNPISQMADNLKEGIVECGAMEKDLFLYTLLLYHPKHRTLVFTNSISAVRRLTKLLQTLQLPALALHSSMAQKARLRSVERFSSPSSDPSTILIATDVAARGLDIKGIDLVIHYHAPRTADTYVHRSGRTARAGASGKSVIICGPDEMVGVVRLAAKVHANMANGKKLPLESLELDRRVVSRVKPRVSLASRITDANIAKEKISAEDNWLRNAAEDLGVEYDSEEFDESNGKGRGRGRGRHQKQKEVGSVSKAELAGLRAELKQLLSQRVNVGVSERYLTAGRVDIDALLRGEGNTSFLGPVDPLNF | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 85509
Sequence Length: 777
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q59ZH9 | MAKQGKNKVSKPRKPPTLKQKLKKESKVVKAKDLQWKLVDIPDNLGDYEGFYGLEEIDGVDVQIVNGKAEFIVRDNGKVENKSKKEETNENGENNMDVEDNETPEVEDEKPTEQEEEEEEEEEEEEEEEEEEEEEEFAGFEDDENNQEDANTSERVSNNDKDDKLAESNDELNAVSFANLDLPLPDDNEINLPNWQEGDLGSSISAYTLYGLSQLDFKKPTPIQKETIPIALSGKDVIGKATTGSGKTLAYGIPILEKYIQSLNLIKQNNKDKKINHPTGIIFAPTRELAHQVVDHLNKLAKYSPLSTRGIVSITGGLSIQKQQRLLRHGPGIIVATPGRMLELVQGDSELAKRLASIDIIVLDEADRLLQDGHFDEFEKILELFGKNRPKSKSIEWKWQTLVFSATFSRDLFRKLDRHQKGKSSSLMGNDEIVQLLNEKLKFKDKKPTLVDANPKEIVSGQITEALVECGPTERDLYLYYFLLMYKGSTLVFANSIDSVKRLVPLLNNLNIPAFSIHSSMIQKQRLRALEKFKEASQKNEVAVLVASDVAARGLDIPNIDHVVHYHLPRSADVYIHRSGRTARAGKEGVSVMFCSPQEASGPLRKLRRLVAGNSNKESRLNMHNDVKLLPIEMDLVSQIKPRVEISSKLADASISSTATRKEDSWVKQAAEDLGLDDLSGLEDFEDDIIKKQRKRKEGKMLSKDETKALKYELKTLLANPIKKNTRKSYITSGLQNLAHQMVTGAHHDDVLGHEKVNALSDLKGSKNKNKKIEKKRISKKK | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 88059
Sequence Length: 782
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q1E7Y4 | MAQKRSHNHKDHTAKAIKRRKFNAATAKSSDDAAHDIVSVDQLDWKTVTLPDRLDDAEGFYGLEEIEGVDILRPSGGGEIKFKASKSKIKGILKNSTDKSGQPAEDWEEWSGFGDDSEDGDGTTLEAEKKAENHGKVNDRRTKTNNSNKEKESNKLPKDRGPRIKTDNGIKTGVSFAALQDEVEEDVDVSAWDSLDLSAELQTSLGRLKFSSPTPIQSACIPAVLQGHDVIGKASTGSGKTLAFGIPIVEYFLGKYRGGRAPTASEERESTKEPMALILSPTRELAHQLNKHLTDLVNHAPNTQVRIATVTGGLSIYKQQRLLADADIIIATPGRLWEVVGSMTGFLSKLKKIRFLVIDEADRLLSEGHFKEVEEILNAIDKVEITEEAYGERSEREPEPEPDEEKKAEPRQTLVFSATFHKGLQQKLSGKIRYRNDDLLDKKESMEYLLRKLNFREERPKFIDVNPISQMAQNLKEGLVQCAPMDKDLLLYTLLLYHPKHRTLVFTNSISAVRRLTQLLQNLNLPTFALHSSMAQKARLRSVERFSSLSSDPSSILVATDVAARGLDIKGIDLIVHYHIPRTADTYVHRSGRTARASASGKSILICAPEETTGVARLVAKIHSNKKDSSATESKMEKKVPLQSVDLDRRIIDRLRPRVTLAKKITESILAKEKLSSEDDWLRSAAEDLGVDYDSDEFAEQQSKGKGKGRGRGGGRQAREQKAASLSKAELAGLKAQLRELVSKKVNVGISEKYLTAGRVDVDALLRGEGNDAFLGHVEKLSF | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 86750
Sequence Length: 783
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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P0CQ90 | MAKIDKKTKLKLNKKSVRAPSKPTTEKKPKKYVTADTLTWKPVKTSSFSGIDGGGGMMMLEELEDVGIEWEETDGGRKIAKFVEVESKTSKGKKNAAQEEPNQEGRGDDEKASSASETEEGKKADDKEAVEEDDEEEFPDFAGFAEEDLNAADEEEHPNLDDEPAFNDDLLPEWSSISLHPSLKRSFLASSFTAPTAIQSRAIPAGITGRDVVGVAETGSGKTLAYSLPILHYLLGQRKSKAGIKRPLSALVLCPTRELALQVMDHLNALLKHALATPDGEKPQGPPRVSVGSVVGGLSAQKQKRILERGCDVIVATPGRLWDLIKADDELATSVRTLRFLVIDEADRMIENGHFAELESIVKLTQRSTAQQGPDDDDPVFQAMATLFEESTAREDMQTFVFSATLSKDLQKNLKRRSRSWKGKGKRSSTLEDLVEKLDFRDENPEVIDLSPEGGVVSSLRESMIESTKDDKDLYLYYFLLRYPGRSIVFVNSIDSIRRLLPLFTLLQLPVFPLHSHLQQKQRLKNLDRFKSNPKGILIATDVAARGLDIPQVDHVVHFNLPRTADAYIHRSGRTARAQNEGFALQLVSPDEKSVQRALMKSLERTHELPDLPIEAGFLPSLRERLRVATEIEKAQHRATKATHDKNWLLEAAEAMDIDIDPSMLDGEDDDPDAPYYKPKKQDRGKGKASVENLKMELKALLQEKLVARGVSIRYPTSGSKVIVDDLIKSTGHGMLLGASTSKAYDQVEKTGKRKLGSGRPGAVKKKKVEGR | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 85544
Sequence Length: 772
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q4IBS2 | MVPPSKKRKLPAATGPATKRSKNIPKPSSSKKKSGKESRSTVEAGALSWASVGEDFGGLEVIEGVDVVKDGNRVQFLVSGDKNKSNIIDPQQEVVDGDRPFEGFGDDAVEVGDIDSGEVGSDQAGAESKKPQGKNKGKNEPKEGQEKADQETNKKQKQKQNKNKLDGKNGAGNKQDEQLVKAAQGVQKSSTRGGNTFGALADGNDYKDQEDVDMAAWVSLNLSPQIISAIAKLKFMKPTKIQKRTIPEIVAGHDVIGKAQTGSGKTLAFGIPMVERWLEMQEQGVKRTGPMSLVLSPTRELAKQLGDHLKALCDGLPSAPYVCVVTGGLSILKQQRQLEKADIVIGTPGRLWEVLSGDRALQSKFAKIRFLVVDEADRLFKVGQFKEAEDIIGALDGKSPGDDAESEEESDEEDEDDEDAARQTLVFSATFDKDLQTKLAGKGKSSGNDDEKMAYLMKCLKFRGEPKFIDVNPVSQMAEGLREGLIECGAMEKDLYLYTVLILNPGRRTLVFTNSISAVRRLTPLLTNLNLTALPLHSQMAQKARHRSLERFTASRNSILIATDVAARGLDIKEVDQVLHYHVPRSADTYIHRSGRTARGESSGISVILCAPEEVLPTRRLASKVHAVRSAGVKREHFIQTLLIDRKAASRLKPRVDLAKKIADTILAKEKAHSDDTWLRNAADELGVEYDSDDLEEINAGGGKGGRGGGRKRKEQTAKQLTKAEMGALKAQLREELSRRVNLGVSERYITGGRVDVGALLREGQQGGMFLGNTDGLGFDL | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 84922
Sequence Length: 781
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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A4REU9 | MTTDTTKQKRKLDSKQNTSPKRRKVQANGKAQPKAKKPKRVVAADSLSWRSVEIPELFDDAEGFFGLEEVEGVDVIRDGGMVKFVTAAPAAEKEDEGDDFSGFDDNPESTSLVAAEEAKSEEPAKPQSQKKQQTKQPKSETKEKKEKPAKAKKNEKQTSKTDDDDLATGSFAALAEIDETDEGADVSEWEPLGLSEEIMSSIAKLKFAKPTAIQAATIPEILAGHDVVGKASTGSGKTLAFGIPIVEKWLSINASTQSKRVAEGETKTPIALVLSPTRELAHQLTDHIKNLCAGLATSPYVCSVTGGLSVHKQQRQLEKADIVVGTPGRLWEVLSSSTKLIQAFRGIKFLVVDEADRLLSEGHFKDAKDIFEGLDKVETDDDGIIRGGKARQTLVFSATFNKGLQQKLAGKGRFDLATDSQSMEYLLKKLKFREEIPKFIDVNPVSQMAEGLKEGIVECGAMEKDLYLYSLLLMHPTQRTLVFTNSISSVRRLTPMLQQLTLPVIALHSQMIQKARLRSVERFTSSKPGSASILIATDVAARGLDIRGIDVVIHYHVPRTADAYVHRSGRTARADSSGLSILICAPEEVTPTRRLVAKVHASAAAKGKKKGSAGGVFVHSVELDRRLVSKLRERVQLAKQIADSTLAKEKIGKEDNWMQKAAEELGVEYDSEDLEKASNWSGRGSGRKSKQKEAKEMSKAEVASLKAQLKQLLSKRINSGVNERYIANGNVDIDGLLSGAKGDFLGKVEGLGVSPLLATD | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 82752
Sequence Length: 760
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Subcellular Location: Nucleus
EC: 3.6.4.13
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O06992 | MKNLENKSFIIRCLKAAASPSGVCRYGNTFSWLQLSFLFLFLTACLMAPLAVSFVKMDRFSVSSFMPSAIQGVNDQFADQLQGFQIRNGKLTGGKSSERIEDGQNVMAVDMKHEYETSGENGRLKVTGFENAIIFQPDQLVITDQNETGFSVGYAKMDVKLEKPNVHDVEVLIDTLWLAQYKPMIMMLAYTVVSMIQLLLTFVLAGGLWITKISNMVSIASFKEAASIAICASALPAFAAAAIGMVHFDLITVLMIHSCGVTLMISFAFRYLTKTRRDNGNLHSGGNDDKSAVI | Function: Could have a role in maltodextrin utilization.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32330
Sequence Length: 294
Subcellular Location: Cell membrane
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Q45632 | MGAAFKWGAAARKTVFPLFYFLIFFAFGALFPLLSVYLQEEARLSGAAIGWIMSLPPIVTMAAQPLWGTAADYTRKPVGLLLAALVLAALFGVMYALAGSYRLFVVLTVLLSAMQSAIVPLSDSLALRHVHEQGGNYGAIRLWGSLGFAMAVLAVGWLSDHIAFAVIFYAFSLALLTAAALATRLPRYPMGAPGALTRQDVRGLLASRPFRLLLVATFLLFGPILANNSYFGLLIHELGGTLTGIGLAFLFAAGSEAPFMKAADRLIGRFGMVRLLLLAALISAARWLAYAADPPLWFVYMTTVVQGCSVGLAIPTALQYARRLAPERVQSTAVALYSAVGNGLGAWFCTLVGGYLLERWQIGAVYLFFSICTIVGVLVLLLLAKRERTAGEEK | Function: High affinity transport of maltose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42326
Sequence Length: 394
Subcellular Location: Cell membrane
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L8B068 | MHHPGPPRFVATGDEVELAPRDPDPTATYTWRLTQAPAQSTVSLGDDPVEHFVPDAPGRYVVRLTAPDGEHDLTVRAFPGTLESSGTHTSGRSGGHSGGVSGGRSGPGRSGSGEYTQAGDGSDGGGGGQPRLTLRPDIEGDEAVVRADCSPHPEGTETAADLAVEFLLDDRDDVDADAVTRDGTALRIPLDALPERARIHAVAVGNHGYSVPDAVEFTRGGDGVETVTSGAGVAARRPYDAPAWAEDSVIYEIYVRTFAGERDESPFDAITDRLDYLDSLGVDAIWLTPVLQNDHAPHGYNITDFFEIASDLGTRADYERFIEAAHDRGFKVLFDLVCNHSARTHPYFESAVEGPDADYREWYEWRSDTEPETYFEWEHIANFNFDHLPVRRHLLDAVAQWADLVDGFRCDMAWAVPNGFWREIHDYCKDRDSEFLLLDETIPYIPDFQAGLFDMHFDSTTYAALRQVGGGGDAEAILGAIEGRAEIGFPEHASFMLYAENHDETRYIVDYGREAAEAAAGALFTLPGAPLLYAGQEFGQRGRRDDLAWDHADETLQSFVSDLASARHDQPALSADADLVRIPYEVRDGPSDRVVAYARTTENDAAVVVLNFGSEPTTVGLPAGTDGTDLVSGEYRGAAGDGDATVTVDSVSVFPADENDLRQ | Function: Alpha-amylase that cleaves starch into oligosaccharides, the first step in starch degradation (By similarity). Endo-acting enzyme which prefers a linear polysaccharide to branched polysaccharides hydrolyzing alpha-1,4 glucosidic bonds efficiently. Has also transglycosylation activity, but does not act on alpha-1,6 bonds. Higher activities of 100%, 79% and 67.8% against amylose, soluble starch and amylopectin, respectively. Lower activity of 22% against glycogen and faint or no activity against alpha-, beta- and gamma-cyclodextrin.
Catalytic Activity: Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
Sequence Mass (Da): 72027
Sequence Length: 663
Pathway: Glycan degradation; starch degradation.
Subcellular Location: Cytoplasm
EC: 3.2.1.1
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L0E155 | MAPTPKYTFTERAAAGNLSDAEILNSNNPTGSELPDESDVVVGGAGIHGLIYALHASKYKPNNLKISVIEKNTRPGYKIGESTLPIFYTWCKLHGISAAYLLRLFGLKDGLCFYFLDRENQGQYTDFCSVGAPGLVLASLQIERPMSELLFTILAQRNGVNVYHGREVDFKSTVVQGGGQGNKIAVSRGKYDSTPKTIDSALFVDATGRFRQFCSKKAPRHRFDGWNCNAFWGYFTAPKDESKIPFDLYEGDHTNHLCFPEGWVWVIRLPSWEGSLIANLMDMVTYILECADAGVPGDELPSSEELARMFGLKFQWVTSIGFAVRNDVKYPEDLSAYGTREAEQKFNYFVQKYELLQQFMSNFELIENLYGPGTTWFIRKTLAYQSPVVSGPGWLAIGDACGFTNPLYSPGINVGMSTSTWAAQLSHRIVEIGKSAPADAAESSIRKLLVPYDDYCKSLVPALEQMNRFNYVCYRDTRLGPQVACLWQFFAGIERYLSDVNIETFAHYAIKWVWGAMVPEYQQVAQKCIEHIETVPLDERLPDAMVDELLAFSNRIKSAAVAADDFSLRWDAILRSFDRSLNFVEGKTSRDIYTRQCSGCGAWLQLRPDWKKCHSCGLLGTEPQTAVTFDPPLTAEEEALLYAAWNTAPKYDPSKELKLPTPTRPAA | Cofactor: Binds 1 FAD per subunit.
Function: Flavin-dependent halogenase; part of the gene cluster that mediates the biosynthesis of malbrancheamide, a dichlorinated fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of malbrancheamide biosynthesis involves coupling of L-proline and L-tryptophan by malG, a bimodular NRPS, to produce L-Pro-L-Trp aldehyde through reductive offloading . This compound undergoes spontaneous cyclization and dehydration to give a dienamine which is reverse prenylated at C-2 by malE . The other prenyltransferase present in the cluster, malB, displays modest activity, suggesting that may be a redundant gene in the pathway . Subsequently, a [4+2] Diels-Alder cyclo-addition catalyzed by the bifunctional enzyme malC forms the characteristic bicyclo[2.2.2]diazaoctane ring of premalbrancheamid . Finally, the flavin-dependent halogenase malA catalyzes the iterative dichlorination of the indole ring of premalbrancheamide to yield C-9 monochlorinated malbrancheamide B, C-8 monochlorinated isomalbrancheamide B, and dichlorinated malbrancheamide . MalA is also able to brominate premalbrancheamide at C-9 to yield malbrancheamide C, and, to a lesser extend, at C-8 to yield isomalbrancheamide C . Finally, malA can brominate C-9 monochlorinated malbrancheamide B at C-8 to yield malbrancheamide D, or C-8 monochlorinated isomalbrancheamide B at C-9 to produce isomalbrancheamide D .
Catalytic Activity: (+)-premalbrancheamide + 2 chloride + 2 FAD + 4 H(+) = (+)-malbrancheamide + 2 FADH2
Sequence Mass (Da): 74698
Sequence Length: 667
Domain: The very flexible region (621-646) acts as a substrate channel lid, having two main open/closed conformations.
Pathway: Alkaloid biosynthesis.
EC: 1.14.-.-
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L0E4F8 | MAPTRRSRDLLRGKNVLIIGGTSGIGFAVAQLVIEHGAMACIAGSNPTKLGKALDALKQHPDRDPIAIVQSATCDLFDVPNLEQNLDNLLKLAAGDSKIHHIVFTAADMVQPPPLASVTIEQIQRVGTIRFTAPMLVAKLLPKYMELCPENSYTLTSGSHAKQPDPGWSLVTGYCGGVEGLMRGLAVDMMPLRVNVVSPGAVLTPVLRDILGDSLEIALDAARKKSTTGRIARPEDVAEAYLYIMKDQNITGTVLETSAGMLLR | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of malbrancheamide, a dichlorinated fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of malbrancheamide biosynthesis involves coupling of L-proline and L-tryptophan by malG, a bimodular NRPS, to produce L-Pro-L-Trp aldehyde through reductive offloading . This compound undergoes spontaneous cyclization and dehydration to give a dienamine which is reverse prenylated at C-2 by malE . The other prenyltransferase present in the cluster, malB, displays modest activity, suggesting that may be a redundant gene in the pathway . Subsequently, a [4+2] Diels-Alder cyclo-addition catalyzed by the bifunctional enzyme malC forms the characteristic bicyclo[2.2.2]diazaoctane ring of premalbrancheamid . The first reaction catalyzed is a NADPH-dependent reduction reaction in which the nicotinamide cofactor is a stoichiometric reagent . Either NADH or NADPH is effective as a cofactor . NADP(+) is required for stereocontrolled formation of premalbrancheamide, however it does not appear to be required as a formal stoichiometric reagent because the second reaction performed by malC, the [4+2] cycloaddition, is a balanced chemical reaction without requirement for hydride transfer to balance the reaction . Finally, the flavin-dependent halogenase malA catalyzes the iterative dichlorination of the indole ring of premalbrancheamide to yield C-9 monochlorinated malbrancheamide B, C-8 monochlorinated isomalbrancheamide B, and dichlorinated malbrancheamide . MalA is also able to brominate premalbrancheamide at C-9 to yield malbrancheamide C, and, to a lesser extend, at C-8 to yield isomalbrancheamide C . Finally, malA can brominate C-9 monochlorinated malbrancheamide B at C-8 to yield malbrancheamide D, or C-8 monochlorinated isomalbrancheamide B at C-9 to produce isomalbrancheamide D .
Catalytic Activity: 1-hydroxy-3-{[2-(1,1-dimethylallyl)-indol-3-yl]methyl}-6H,7H,8H-5lambda(5)-pyrrolo[1,2-a]pyrazine + H(+) + NADPH = 1-hydroxy-3-{[2-(1,1-dimethylallyl)-indol-3-yl]methyl}-4H,6H,7H,8H-pyrrolo[1,2-a]pyrazine + NADP(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28233
Sequence Length: 264
Pathway: Alkaloid biosynthesis.
Subcellular Location: Membrane
EC: 1.1.-.-
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P0A4N1 | MKGVNMEKQQPSKAALLSIIPGLGQIYNKQKAKGFIFLGVTIVFVLYFLALATPELSNLITLGDKPGRDNSLFMLIRGAFHLIFVIVYVLFYFSNIKDAHTIAKRINNGIPVPRTLKDMIKGIYENGFPYLLIIPSYVAMTFAIIFPVIVTLMIAFTNYDFQHLPPNKLLDWVGLTNFTNIWSLSTFRSAFGSVLSWTIIWALAASTLQIVIGIFTAIIANQPFIKGKRIFGVIFLLPWAVPAFITILTFSNMFNDSVGAINTQVLPILAKFLPFLDGALIPWKTDPTWTKIALIMMQGWLGFPYIYVLTLGILQSIPNDLYEAAYIDGANAWQKFRNITFPMILAVAAPTLISQYTFNFNNFSIMYLFNGGGPGSVGGGAGSTDILISWIYRLTTGTSPQYSMAAAVTLIISIIVISISMIAFKKLHAFDMEDV | Function: Part of the binding-protein-dependent transport system for maltodextrin; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48302
Sequence Length: 435
Subcellular Location: Cell membrane
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Q7TQJ1 | MLPPPPRQPPPQARTARGSLRLQRAFLRGPLGVLRLLQLLAGAAFWITIATSKYQGPVHFALFVSVLFWLLTLGLYFITLLGKQELVPVLGSRWLVVNVAHDLLAAALYGAATGIMIDQTQRHSYCNLKNYRLPCAYHAFLAASVCGGLCLGLYLLSALYGCCRRYQGKEEVV | Function: Microtubule-associated protein that exhibits cell cycle-dependent localization and can inhibit cell proliferation and migration.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19087
Sequence Length: 173
Subcellular Location: Cell membrane
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Q8N4S9 | MSNDGRSRNRDRRYDEVPSDLPYQDTTIRTHPTLHDSERAVSADPLPPPPLPLQPPFGPDFYSSDTEEPAIAPDLKPVRRFVPDSWKNFFRGKKKDPEWDKPVSDIRYISDGVECSPPASPARPNHRSPLNSCKDPYGGSEGTFSSRKEADAVFPRDPYGSLDRHTQTVRTYSEKVEEYNLRYSYMKSWAGLLRILGVVELLLGAGVFACVTAYIHKDSEWYNLFGYSQPYGMGGVGGLGSMYGGYYYTGPKTPFVLVVAGLAWITTIIILVLGMSMYYRTILLDSNWWPLTEFGINVALFILYMAAAIVYVNDTNRGGLCYYPLFNTPVNAVFCRVEGGQIAAMIFLFVTMIVYLISALVCLKLWRHEAARRHREYMEQQEINEPSLSSKRKMCEMATSGDRQRDSEVNFKELRTAKMKPELLSGHIPPGHIPKPIVMPDYVAKYPVIQTDDERERYKAVFQDQFSEYKELSAEVQAVLRKFDELDAVMSRLPHHSESRQEHERISRIHEEFKKKKNDPTFLEKKERCDYLKNKLSHIKQRIQEYDKVMNWDVQGYS | Function: Plays a role in the formation of tricellular tight junctions and of epithelial barriers (By similarity). Required for normal hearing via its role in the separation of the endolymphatic and perilymphatic spaces of the organ of Corti in the inner ear, and for normal survival of hair cells in the organ of Corti .
PTM: Ubiquitinated by ITCH; but this ubiquitination does not lead to proteasomal degradation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64168
Sequence Length: 558
Subcellular Location: Cell membrane
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Q3UZP0 | MSSSDARSRIRDRGYSEVPRDTSCPDGTIRTFQSLHSSELAVSADPLPPPPLPLQPPFGPSFYSSDTEEPAVAPDLKPVRRFVPDSWKNFFRGKKKDPEWDNPVSDIRYISDGVECSPPASPARANHHPYKDPSRGSQGTFNSQHEADAMFAHDPYASLDRRTQTARTYSEKVEEYNLRYAYMKSWAGLLRILGVVELLLGAGVFACVTAYIHKDNEWYNLFGYTQPYGMGGLGSLGNTYGGYYYSGPKTPFVLVVAGLAWITTIIILVLGMSMYYRTILLDSNWWPLTEFGVNVALFILYMAAAIVYVNDTNRGGLCYYPLFNTPMNAMFCRVEGGQIAAMIFLFVTMIVYLVSALVCLKLWRHEAARRHREFLEQQEINDPSLSSKRKMCEAAISDRQRDQEVNVKDLRTTTKMTPELLSGHIPPGHIPKPIVMPDYVAKYPVIQTDDDRERYKAVFQDQFSEYKELSAEVQAILRKFDELDTVMSRLPHHSENRQEHERISRIHEEFRKKKNDPSFLEKKERCDYLKNKLSHIKQRIQEYDKVMNWDTQGYP | Function: Plays a role in the formation of tricellular tight junctions and of epithelial barriers . Required for normal hearing via its role in the separation of the endolymphatic and perilymphatic spaces of the organ of Corti in the inner ear, and for normal survival of hair cells in the organ of Corti .
PTM: Phosphorylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63662
Sequence Length: 555
Subcellular Location: Cell membrane
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P53051 | MTISSAHPETEPKWWKEATFYQIYPASFKDSNDDGWGDMKGIASKLEYIKELGADAIWISPFYDSPQDDMGYDIANYEKVWPTYGTNEDCFALIEKTHKLGMKFITDLVINHCSSEHEWFKESRSSKTNPKRDWFFWRPPKGYDAEGKPIPPNNWKSYFGGSAWTFDEKTQEFYLRLFCSTQPDLNWENEDCRKAIYESAVGYWLDHGVDGFRIDVGSLYSKVVGLPDAPVVDKNSTWQSSDPYTLNGPRIHEFHQEMNQFIRNRVKDGREIMTVGEMQHASDETKRLYTSASRHELSELFNFSHTDVGTSPLFRYNLVPFELKDWKIALAELFRYINGTDCWSTIYLENHDQPRSITRFGDDSPKNRVISGKLLSVLLSALTGTLYVYQGQELGQINFKNWPVEKYEDVEIRNNYNAIKEEHGENSEEMKKFLEAIALISRDHARTPMQWSREEPNAGFSGPSAKPWFYLNDSFREGINVEDEIKDPNSVLNFWKEALKFRKAHKDITVYGYDFEFIDLDNKKLFSFTKKYNNKTLFAALNFSSDATDFKIPNDDSSFKLEFGNYPKKEVDASSRTLKPWEGRIYISE | Function: Major isomaltase (alpha-1,6-glucosidase) required for isomaltose utilization. Preferentially hydrolyzes isomaltose, palatinose, and methyl-alpha-glucoside, with little activity towards isomaltotriose or longer oligosaccharides. Does not hydrolyze maltose.
Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.
Sequence Mass (Da): 68592
Sequence Length: 589
Subcellular Location: Mitochondrion
EC: 3.2.1.10
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P59213 | MSSKFMKSAAVLGTATLASLLLVACGSKTADKPADSGSSEVKELTVYVDEGYKSYIEEVAKAYEKEAGVKVTLKTGDALGGLDKLSLDNQSGNVPDVMMAPYDRVGSLGSDGQLSEVKLSDGAKTDDTTKSLVTAANGKVYGAPAVIESLVMYYNKDLVKDAPKTFADLENLAKDSKYAFAGEDGKTTAFLADWTNFYYTYGLLAGNGAYVFGQNGKDAKDIGLANDGSIVGINYAKSWYEKWPKGMQDTEGAGNLIQTQFQEGKTAAIIDGPWKAQAFKDAKVNYGVATIPTLPNGKEYAAFGGGKAWVIPQAVKNLEASQKFVDFLVATEQQKVLYDKTNEIPANTEARSYAEGKNDELTTAVIKQFKNTQPLPNISQMSAVWDPAKNMLFDAVSGQKDAKTAANDAVTLIKETIKQKFGE | Function: Part of an ABC transporter complex involved in the uptake of maltodextrins. Binds glycogen-derived linear maltooligosaccharides increasing in size from maltotriose to maltooctaose with the highest affinity for maltotriose. Has a very weak affinity for maltose. Has also a very low affinity for maltotetraitol, indicating that the binding is selective for maltooligosaccharides with an intact reducing end.
Location Topology: Lipid-anchor
Sequence Mass (Da): 45337
Sequence Length: 423
Subcellular Location: Cell membrane
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P21517 | MLNAWHLPVPPFVKQSKDQLLITLWLTGEDPPQRIMLRTEHDNEEMSVPMHKQRSQPQPGVTAWRAAIDLSSGQPRRRYSFKLLWHDRQRWFTPQGFSRMPPARLEQFAVDVPDIGPQWAADQIFYQIFPDRFARSLPREAEQDHVYYHHAAGQEIILRDWDEPVTAQAGGSTFYGGDLDGISEKLPYLKKLGVTALYLNPVFKAPSVHKYDTEDYRHVDPQFGGDGALLRLRHNTQQLGMRLVLDGVFNHSGDSHAWFDRHNRGTGGACHNPESPWRDWYSFSDDGTALDWLGYASLPKLDYQSESLVNEIYRGEDSIVRHWLKAPWNMDGWRLDVVHMLGEAGGARNNMQHVAGITEAAKETQPEAYIVGEHFGDARQWLQADVEDAAMNYRGFTFPLWGFLANTDISYDPQQIDAQTCMAWMDNYRAGLSHQQQLRMFNQLDSHDTARFKTLLGRDIARLPLAVVWLFTWPGVPCIYYGDEVGLDGKNDPFCRKPFPWQVEKQDTALFALYQRMIALRKKSQALRHGGCQVLYAEDNVVVFVRVLNQQRVLVAINRGEACEVVLPASPFLNAVQWQCKEGHGQLTDGILALPAISATVWMN | Function: May play a role in regulating the intracellular level of maltotriose. Cleaves glucose from the reducing end of maltotriose and longer maltodextrins with a chain length of up to 7 glucose units.
Catalytic Activity: Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
Sequence Mass (Da): 69041
Sequence Length: 604
Subcellular Location: Cytoplasm
EC: 3.2.1.20
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P21145 | MAPAAATGGSTLPSGFSVFTTLPDLLFIFEFIFGGLVWILVASSLVPWPLVQGWVMFVSVFCFVATTTLIILYIIGAHGGETSWVTLDAAYHCTAALFYLSASVLEALATITMQDGFTYRHYHENIAAVVFSYIATLLYVVHAVFSLIRWKSS | Function: Could be an important component in vesicular trafficking cycling between the Golgi complex and the apical plasma membrane. Could be involved in myelin biogenesis and/or myelin function.
PTM: Lipoprotein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16714
Sequence Length: 153
Subcellular Location: Membrane
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P40065 | MREKRTISNKDTNYLKFPNKLQRYSRFLSRKISNTSPEKQPKKNIKEHCLSSYHKEHSVKPKQNSGNVAAKEDKDTQHLQNNVANEEATECLTRSNLKKLQEKIFDRELNDIACDHCLCSTENRRDIKYSRLWFLFELEMSENWNENLRLSCYNKYVYSAIDESWKMENILLKEQEKHYEYFPIGQLLIPNNIDYTNKQKRKENIEDLTIEIDSIIETNHQKKRFLPQSVLIKREDEIAFDDFHLDARKVLNDLSATSENPFSSSPNTKKIKSKGKTLEVVPKKKNKKIIGALERKLHIDEN | Function: Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis.
PTM: Phosphorylated by CDC5. This phosphorylation is required for the location to the kinetochores during late pachytene.
Sequence Mass (Da): 35753
Sequence Length: 302
Subcellular Location: Nucleus
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Q54KN4 | MKNFYYFILILLFFNEVCYSLKDGEIKLHLIPHSHCDSGWTSTMNEYYMGQVKSIISSMVQSLNVESNPPRKFVWSEIGFLEQWWDDMPIEIKNDFIKHVKNDRIEFVNGGWVMNDEACASLESVIRQLSNGHKFIREKFGKQPESGWQIDPFGHSSLTPTLQAQFGYKHVVLNRIHYELKKKFKEEKNLQFKWRGSPEGVGPKSDILAHVFDDFYTSPPHMSFDGYNFLAYGLPRLTMEMIELARNRSVFYKSPHVLIPMGGDFAFKNAYKSFEQMDQLVASINGQHANGESNVICQYSTLADFFSDTINWHNENKVSFNYYDSDFFPYADDSNTYWTGYYTSRPLLKGYERHVSSKLRSAEILSALQNDEKYYPNQLLNASKQVSILQHHDAISGTSKKHVVQDYFSRLQKADILVSEQSEKLLASALSQHSPTKLDIIDIGGSLNFPKNNDAISFILFNQLSWSKEELISIKVQSVGDHGESLNSPTNNACPYVLAQEDFLNEIEIDCSPRSDFKSDQSDDHKEFIQIDFPAKLKPFSSKLYYLKRKSNPNKSNWVLPKTNHFNSIENSIYTANLDENYLIKSLKSKSSRHGGGANQITEINQQLLTYSDIGGAYIFRTNKQVFQPPRQVYSTFTYIGKFYQEAQSILQDTHQISNRNGYYYYYGNNQQQQQQQQTISTFNYNSIKLINTGNEMIDKKINFNFHIRGINGTTTINRFTTDIDNNRELYSDNGLEMMHRKSISSQSVEVGRETQSYYPTINSVYIESQSTGKRFVCNNDRSRGVSSQGQGCLEMALHRSLTYEDGKGLEIPAIDESSINARFECYLDEVPSNSQQSNGGGGGDDIRKQSINYQHKFQIYQGQDSSYMSSKSFMLKPLPEFIHILSMERSGPRSIKLRIHNIENNNQSPITFDLNGLFSFIKSIKSIKEYNLSLINRFVDNNIDNIISSHRSIVGKNLFPIKDTPTRFNPINTKQTKITLYPSEIKAIEITYH | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
Sequence Mass (Da): 114357
Sequence Length: 994
Subcellular Location: Secreted
EC: 3.2.1.24
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P55145 | MRRMWATQGLAVALALSVLPGSRALRPGDCEVCISYLGRFYQDLKDRDVTFSPATIENELIKFCREARGKENRLCYYIGATDDAATKIINEVSKPLAHHIPVEKICEKLKKKDSQICELKYDKQIDLSTVDLKKLRVKELKKILDDWGETCKGCAEKSDYIRKINELMPKYAPKAASARTDL | Function: Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain . Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra (By similarity). Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons (By similarity). Inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death . Retained in the ER/sarcoplasmic reticulum (SR) through association with the endoplasmic reticulum chaperone protein HSPA5 under normal conditions . Up-regulated and secreted by the ER/SR in response to ER stress and hypoxia . Following secretion by the ER/SR, directly binds to 3-O-sulfogalactosylceramide, a lipid sulfatide in the outer cell membrane of target cells . Sulfatide binding promotes its cellular uptake by endocytosis, and is required for its role in alleviating ER stress and cell toxicity under hypoxic and ER stress conditions .
PTM: May contain sialic acid residues.
Sequence Mass (Da): 20700
Sequence Length: 182
Domain: The N-terminal region may be responsible for neurotrophic activity while the C-terminal region may play a role in the ER stress response.
Subcellular Location: Secreted
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Q84DC4 | MRHPVDMPEKVGTDAKRLFAQPEHLWELTLTEASALVRHRRITSRQLVEAWLSRIADFSELNAFISVDAAAALKQADSYDHYLEAGGDPLPLGGVPIAVKDNIQVVGFANTAGTPALSKFFPTCNARVIEPLLKAGAIVVGKTNMHELAFGTSGYNTAYHIPGVIGVRNAFDHSCIAGGSSSGSGTAVGALLIPAALGTDTGGSVRQPGAVNGCVGFRPTVGRYPVDGITPISPTRDTPGPIARSVEDIVLLDSIITGALPAEVPAAESIRLGVVDQLWADLSEPVRKLTEDALRKLEQQGVQIVRVSMSEIFEMSHAVSMPLALHECRSALTEYLSANETGVSFDELVAGISSPDVRTIFEDYILPGRLGELEGQSVDLEQAYATAMKDARPKLIQSFEFLFKEHQLDAIIHPTTPDLAIKSNPAATSFEAFARMIRNADPASNAGMPGISLPAGLSQQEGLPVGIEIEGLPGSDARLLSIANFIESILGRGPTPTRSGVESKISM | Function: Hydrolyzes both the R- and the S-enantiomers of mandelamide, and phenylacetamide. Has lower activity on 3-phenylpropionaide and lactamide. Does not hydrolyze benzamide. Hydrolyzes esters and amides with little steric bulk. Preferentially hydrolyzes aromatic substrates.
Catalytic Activity: (R)-mandelamide + H2O = (R)-mandelate + NH4(+)
Sequence Mass (Da): 53814
Sequence Length: 507
EC: 3.5.1.86
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F2JVT6 | MSYPAFDSKTFLEAHIEKTMAFYFPTCIDPEGGFFQFFKDDGSVYDPNTRHLVSSTRFIFNFAQAYLHTNIAEYKHAAVHGIQYLRQRHQSQSGGYVWLLDGGTNLDETNHCYGLAFVILAYSNALQIGLSEAEVWIEVTYDLLETHFWENKHGLYLDEISSDWKTVSPYRGQNANMHMCEALMSAFDATQNPKYLDRAKLLAKNICQKQASLSNSNEVWEHYTNDWQIDWDYNKNDPKHLFRPWGFQPGHQTEWAKLLLMLDKRSPENWYLPKAKYLFDLAYKKAWDTKKGGLHYGYAPDGTVCDPDKYFWVQAESFAAAWLLYKATKDETYYKQYLTLWEFSWNHMIDHTFGAWYRILDENNAQYDNNKSPAGKTDYHTMGACYEVLKTLTL | Function: Catalyzes the reversible isomerization of D-mannose to D-fructose. Can also isomerize D-lyxose, with lower efficiency. In longer reaction with a higher concentration of enzyme, it can isomerize 4-OH D-mannose derivatives (D-talose and 4-O-monosaccharyl-D-mannose). Cannot use D-glucose.
Catalytic Activity: D-mannose = D-fructose
Sequence Mass (Da): 46113
Sequence Length: 394
Domain: The alpha7-alpha8 and alpha11-alpha12 loops of the catalytic domain may participate in the formation of an open substrate-binding site to provide sufficient space to bind 4-OH D-mannose derivatives.
EC: 5.3.1.7
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A0A0P9JFY5 | MDNNNHTFSSWLRSPAHHQWLALEGKRLLGFAKAAKLENGFGGLDDYGRLMVGATAGTMNTARMTHCFAMAHVQGIPGCAALIDHGIAALSGPLHDAEHGGWFSAALEDHGKTDKQAYLHAFVALAASSAVVAGRPAAQALLSDVIQVIQSRFWSDEEGAMRESFSQDWSDEEPYRGANSNMHSTEAFLALADVTGDAQWLDRALSIVERVIHQHAGANNFQVIEHFTSGWQPLPDYNRENPADGFRPFGTTPGHAFEWARLVLHLEAARRRAGRSNPDWLLDDARQLFANACRYGWDVDGAPGIVYTLDWQNKPVVRHRLHWTHCEAAAAAAALLQRTGEQQYEDWYRCFWEFNETLFIDIEHGSWRHELNERNEPSEDIWPGKPDLYHAYQATLLPVLPLAPSLASAMAGLD | Function: Catalyzes the reversible isomerization of D-mannose to D-fructose . Shows high specific activity towards mannose and fructose, and has no detectable activity towards other monosaccharides and disaccharides .
Catalytic Activity: D-mannose = D-fructose
Sequence Mass (Da): 46083
Sequence Length: 414
EC: 5.3.1.7
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A0A077LPS9 | MTLWTARAAHRAWLDAEARRLVDFAAAADHPEHGFAWLDGSGAPLPEQGVHTWITCRVTHVAALAHLEGIPGASALADHGLRALAGPLRDPEHDGWFTALDSRGTVADSRKEAYQHAFVLLAAASATVAGRPGARELLDAAAAVIEQRFWEEETGRCRESWDAAWHADEPYRGANSNMHLVEAFLAAFDATGDRVWAERALRIAHFFVHEVAAPRDWRLPEHFTPDWQVVADYNTDDRAHPFRPYGVTVGHVLEWARLLVHVEAALPDPPSWLLADAEAMFAAAVARGWSVDGTEGFVYTLDYDDTPVVRSRMHWVVAEAISAAAVLGQRTGDERYEHWYRTWWDHAATYFVDTVQGSWHHELDPTLAPPPGGTWSGKPDVYHAYQATRLPLLPLAPSLAGALATVG | Function: Catalyzes the reversible isomerization of D-mannose to D-fructose. Shows weaker activity on D-lyxose, but cannot use N-acetyl D-glucosamine.
Catalytic Activity: D-mannose = D-fructose
Sequence Mass (Da): 44917
Sequence Length: 407
EC: 5.3.1.7
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P11444 | MSEVLITGLRTRAVNVPLAYPVHTAVGTVGTAPLVLIDLATSAGVVGHSYLFAYTPVALKSLKQLLDDMAAMIVNEPLAPVSLEAMLAKRFCLAGYTGLIRMAAAGIDMAAWDALGKVHETPLVKLLGANARPVQAYDSHSLDGVKLATERAVTAAELGFRAVKTKIGYPALDQDLAVVRSIRQAVGDDFGIMVDYNQSLDVPAAIKRSQALQQEGVTWIEEPTLQHDYEGHQRIQSKLNVPVQMGENWLGPEEMFKALSIGACRLAMPDAMKIGGVTGWIRASALAQQFGIPMSSHLFQEISAHLLAATPTAHWLERLDLAGSVIEPTLTFEGGNAVIPDLPGVGIIWREKEIGKYLV | Cofactor: Divalent metal ions. Magnesium seems to be the preferred ion.
Catalytic Activity: (S)-mandelate = (R)-mandelate
Sequence Mass (Da): 38565
Sequence Length: 359
Pathway: Aromatic compound metabolism; (R)-mandelate degradation; benzoate from (R)-mandelate: step 1/4.
EC: 5.1.2.2
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Q01662 | MSTATTTVTTSDQASHPTKIYCSGLQCGRETSSQMKCPVCLKQGIVSIFCDTSCYENNYKAHKALHNAKDGLEGAYDPFPKFKYSGKVKASYPLTPRRYVPEDIPKPDWAANGLPVSEQRNDRLNNIPIYKKDQIKKIRKACMLGREVLDIAAAHVRPGITTDELDEIVHNETIKRGAYPSPLNYYNFPKSLCTSVNEVICHGVPDKTVLKEGDIVNLDVSLYYQGYHADLNETYYVGENISKEALNTTETSRECLKLAIKMCKPGTTFQELGDHIEKHATENKCSVVRTYCGHGVGEFFHCSPNIPHYAKNRTPGVMKPGMVFTIEPMINEGTWKDMTWPDDWTSTTQDGKLSAQFEHTLLVTEHGVEILTARNKKSPGGPRQRIK | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the active site region by the ZNG1 zinc chaperone.
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Plays the major role in N-terminal methionine removal. Less efficient when the second residue is Val.
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 43373
Sequence Length: 387
Subcellular Location: Cytoplasm
EC: 3.4.11.18
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Q9FV49 | MAIGNPEVATMGKENTEAESSNGNESQLSSDLTKSLDLAEVKEDEKDNNQEEEDGLKAEASTKKKKKKSKSKKKKSSLQQTDPPSIPVLELFPSGDFPQGEIQQYNDDNLWRTTSEEKREMERLQKPIYNSLRQAAEVHRQVRKYMRSILKPGMLMIDLCETLENTVRKLISENGLQAGIAFPTGCSLNNVAAHWTPNSGDKTVLQYDDVMKLDFGTHIDGHIVDSAFTVAFNPMFDPLLAASRDATYTGIKEAGVDVRLCDVGAAVQEVMESYEVEINGKVYQVKSIRNLNGHSIGRYQIHAEKSVPNVRGGEQTKMEEGELYAIETFGSTGKGYVREDLECSHYMKNYDVGHVPLRLPRAKQLLATINKNFSTLAFCRRYLDRLGETKYLMALKNLCDSGIIEPCPPVCDVKGSYISQFEHTILLRPTCKEIISKGDDY | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 49395
Sequence Length: 441
Subcellular Location: Cytoplasm
EC: 3.4.11.18
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Q4WAY7 | MTVDAPELLEKLRITDAGANGADMSSSTSAAANGTGKEVDDGSDDDGTENPPAVAAEHSTAKKKKNKKRKPKKKQPKVQTDPPSIPLSQLFPNNSYPKGEEVEYKDENRYRTTSEEKRHLDNLNSDFLSDYRQAAEAHRQVRQWAQRNIKPGQTLLEIANGIEESARCLVGHDGLTEGDSLIAGMGFPTGLNIDNIVAHYSPNAGCKTVLAQNNVLKVDIGIHVGGRIVDSAFTMAFDPMYDNLLAAVKDATNTGVREAGIDVRVGELGGYIQEAMESYECEIRGKTYPIKAIRNLCGHTILPYSIHGTKNVPFVKSNDMTKMEEGDVFAIETFGSTGSGRYVEGGEVSHYALRGDADRKDLTLSSARSLLTAIKKNFSTIPFCRRYLDRIGQEKYLLGLNYLVKSGIVEDYPPLNEKPGTYTAQFEHTILLRPTVKEVISRGDDY | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val) (By similarity). Part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) . Since fumagillin is known to inhibit eukaryotic type 2 methionine aminopeptidase, af410 encodes a self-resistant enzyme for A.fumigatus toward fumagillin .
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 48996
Sequence Length: 446
Subcellular Location: Cytoplasm
EC: 3.4.11.18
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Q5B4X6 | MAAQASEKLEKLDLNGQNGESAAGPAKAGQADAGEVEDESDDDADDAGAAADGAANGAAKKKKKRKSKKKKKGGAKVQSSPPRVPVSSLFANGQYPEGEIVEYKNENSYRTTNEEKRYLDRMNNDFLQEYRQGAEVHRQVRQYAQKNIKPGQTLTEIAEGIEDSVRALTGHQGLEEGDNIKGGMGFPCGLSINHCAAHYTPNAGNKMVLQQGDVMKVDFGAHINGRIVDSAFTMSFDPVYDPLLEAVKDATNTGIRSLQEAGIDVRMSDIGAAIQETMESYEIELNGTTYPIKPIRNLNGHNIDQHVIHGGKSVPIVKGSDQTKMEEGEVFAIETFGSTGKGYVREDMETSHYALVANAPQVPLRLSSAKSLLNVINKNFGTLPWCRRYLDRLGQDKYLLGLNNLVQSGIVQDYPPLCDIKGSYTAQFEHTIVLRPTVKEVISRGDDY | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Mass (Da): 48898
Sequence Length: 448
Subcellular Location: Cytoplasm
EC: 3.4.11.18
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Q9UEW3 | MRNKKILKEDELLSETQQAAFHQIAMEPFEINVPKPKRRNGVNFSLAVVVIYLILLTAGAGLLVVQVLNLQARLRVLEMYFLNDTLAAEDSPSFSLLQSAHPGEHLAQGASRLQVLQAQLTWVRVSHEHLLQRVDNFTQNPGMFRIKGEQGAPGLQGHKGAMGMPGAPGPPGPPAEKGAKGAMGRDGATGPSGPQGPPGVKGEAGLQGPQGAPGKQGATGTPGPQGEKGSKGDGGLIGPKGETGTKGEKGDLGLPGSKGDRGMKGDAGVMGPPGAQGSKGDFGRPGPPGLAGFPGAKGDQGQPGLQGVPGPPGAVGHPGAKGEPGSAGSPGRAGLPGSPGSPGATGLKGSKGDTGLQGQQGRKGESGVPGPAGVKGEQGSPGLAGPKGAPGQAGQKGDQGVKGSSGEQGVKGEKGERGENSVSVRIVGSSNRGRAEVYYSGTWGTICDDEWQNSDAIVFCRMLGYSKGRALYKVGAGTGQIWLDNVQCRGTESTLWSCTKNSWGHHDCSHEEDAGVECSV | Function: Pattern recognition receptor (PRR) which binds Gram-positive and Gram-negative bacteria . Also plays a role in binding of unopsonized particles by alveolar macrophages (By similarity). Binds to the secretoglobin SCGB3A2 .
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 52658
Sequence Length: 520
Subcellular Location: Cell membrane
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Q9WUB9 | MGNKKALKEEAFLGSAEEGADFDQAMFPVMETFEINDPMPKKRNWGSFCTAVMAIHLILLTAGTTLLTLKVLSLQKWILEKYLDNETLAAEDRSFFSLQLASPETHLVPRTPGLQALQVQLTQVRTSQEQLLQQVDNLTRNPELFRIKGERGSPGIPGLQGPPGIKGEAGLQGPMGAPREPGATGAPGPQGEKGSKGDKGLIGPKGEHGTKGDKGDLGLPGSKGDMGMKGVTGVMGPPGAQGNKGDPGKPGLPGLAGSPGVKGDQGQPGLQGVPGTPGAAGPSGAKGEPGHPGPPGPTGPQGISGSPGAAGLKGSKGDTGIQGQKGTKGESGVPGLAGRKGDTGNPGLAGPKGEPGRPGLKGDPGMKGSSGQQGQKGEKGEKGQSFKEVRIVGGTNRGRAEIFYNNAWGTICDDNWDNNDATVFCRMLGYSSGKGFTFGGGSGNIWLDDVNCQGTEDSLWNCRKNNWGSHNCNHNEDAGVECR | Function: Pattern recognition receptor (PRR) which binds Gram-positive and Gram-negative bacteria . Also plays a role in binding of unopsonized particles by alveolar macrophages . Binds to the secretoglobin SCGB3A2 (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 49622
Sequence Length: 483
Subcellular Location: Cell membrane
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P12624 | MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPAAAGSGAASPAAAEKDEPAAAAPDAGASPVEKEAPVEGEAAEPGSPTAAEGEAASAASSTSSPKAEDGATPSPSNETPKKKKKRFSFKKSFKLSGFSFKKNKKEAGEGGEAEGAAGASAEGGKDEASGGAAAAAGEAGAAPGEPTAAPGEEAAAGEEGAAGGDPQEAKPEEAAVAPEKPPASEEAKAVEEPSKAEEKAEEAGVSAAGCEAPSAAGPGVPPEQEAAPAEEAAAAPASSACAAPSQEAQPECSPEAPPAEAAE | Function: MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 31665
Sequence Length: 333
Subcellular Location: Cell membrane
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P29966 | MGAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAESGAKEELQANGSAPAADKEEPAAAGSGAASPSAAEKGEPAAAAAPEAGASPVEKEAPAEGEAAEPGSPTAAEGEAASAASSTSSPKAEDGATPSPSNETPKKKKKRFSFKKSFKLSGFSFKKNKKEAGEGGEAEAPAAEGGKDEAAGGAAAAAAEAGAASGEQAAAPGEEAAAGEEGAAGGDPQEAKPQEAAVAPEKPPASDETKAAEEPSKVEEKKAEEAGASAAACEAPSAAGPGAPPEQEAAPAEEPAAAAASSACAAPSQEAQPECSPEAPPAEAAE | Function: MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 31555
Sequence Length: 332
Subcellular Location: Cytoplasm
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P30009 | MGAQFSKTAAKGEAAAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPASGGAATPAAADKDEAAAAPEPGAATADKEAAEAEPAEPGSPSAETEGASASSTSSPKAEDGAAPSPSSETPKKKKKRFSFKKSFKLSGFSFKKSKKEAGEGAEAEGATADGAKDEAAAAAGGDAAAAPGEQAGGAGAEGAEGGESREAEAAEPEQPEQPEQPAAEEPRAEEPSEAVGEKAEEPAPGATADDAPSAAGPEQEAPAATDEPAASAAPSASPEPQPECSPEAPPAPVAE | Function: MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 29795
Sequence Length: 309
Subcellular Location: Cytoplasm
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Q13YU3 | MTQMNPRGGLQVAANLDQFVETEALPGTGLDSAAFWSGFDALVHELAPKNRALLAERDRLQTELDNWHRANPGPVRDLRAYRAFLEGIGYIVPVPASVKATTDHVDTEIAEQAGPQLVVPLSNQRYALNAANARWGSLYDALYGTDAIPEANGAEKQKAFNPVRGAAVIAYARRFLDQAAPLANGSHADATRYGVEGGKLVVTLKNGTSELKTPAQFIGYQGEESAPSAVLLKHNGLHFEIQIDANDSIGKTDSAHVKDVVVEAAVSTIIDCEDSVAAVDADDKVQLYRNWLGLMNGDLTEEVTKNGKTFTRRLNADRVYTAANGTAPVVLHGRSLLFIRNVGHLMTNPAVLTKDGHEIPEGILDAVITSLCALHDRKHKLNSRTGSIYIVKPKMHGPAEVAFASELFARVEDLLKLPRNTIKMGIMDEERRTSVNLLACINEARERVAFINTGFLDRTGDEMHTAMEAGPMLRKGDMKSSAWIAAYERSNVLVGLSAGLRGRSQIGKGMWAMPDLMHAMLEQKIAHPKAGANTAWVPSPTAATLHALHYHQVDVQAVQQELERTDYAKVRDELLDGLLTIPVVAEAKWSDDEIRSEIDNNAQGILGYVVRWIDQGVGCSKVPDIHNVGLMEDRATLRISSQHIANWLYHGVVKRELVEETFRRMARVVDEQNAGDPLYKPMAPGFDTIAFKAAQALVFEGRQQPSGYTEPLLHKFRLEVKKEA | Function: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
Catalytic Activity: acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+)
Sequence Mass (Da): 79450
Sequence Length: 724
Pathway: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.3.9
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Q9I636 | MTERVQVGGLQVAKVLFDFVNNEAIPGTGVSADTFWTGAEAVINDLAPKNKALLAKRDELQAKIDGWHQARAGQAHDAVAYKAFLEEIGYLLPEAEDFQAGTQNVDDEIARMAGPQLVVPVMNARFALNASNARWGSLYDALYGTDVISEEGGAEKGKGYNKVRGDKVIAFARAFLDEAAPLESGSHVDATSYSVKNGALVVALKNGSETGLKNAGQFLAFQGDAAKPQAVLLKHNGLHFEIQIDPSSPVGQTDAAGVKDVLMEAALTTIMDCEDSVAAVDADDKVVIYRNWLGLMKGDLAEEVSKGGSTFTRTMNPDRVYTRADGSELTLHGRSLLFVRNVGHLMTNDAILDKDGNEVPEGIQDGLFTSLIAIHDLNGNTSRKNSRTGSVYIVKPKMHGPEEAAFTNELFGRVEDVLGLPRNTLKVGIMDEERRTTVNLKACIKAAKDRVVFINTGFLDRTGDEIHTSMEAGAVVRKGAMKSEKWIGAYENNNVDVGLATGLQGKAQIGKGMWAMPDLMAAMLEQKIGHPLAGANTAWVPSPTAATLHALHYHKVDVFARQAELAKRTPASVDDILTIPLAPNTNWTAEEIKNEVDNNAQGILGYVVRWIDQGVGCSKVPDINDVGLMEDRATLRISSQLLANWLRHGVISQEQVVESLKRMAVVVDRQNASDPSYRPMAPNFDDNVAFQAALELVVEGTRQPNGYTEPVLHRRRREFKAKNGL | Function: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
Catalytic Activity: acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+)
Sequence Mass (Da): 78660
Sequence Length: 725
Pathway: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from isocitrate: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.3.3.9
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P0C794 | MNSKHSYVELKDKVIVPGWPTLMLEIDFVGGTSRNQFLNIPFLSVKEPLQLPREKKLTDYFTIDVEPAGHSLVNIYFQIDDFLLLTLNSLSVYKDPIRKYMFLRLNKEQSKHAINAAFNVFSYRLRNIGVGPLGPDIRSSGP | Function: Plays a crucial role in virion assembly and budding.
PTM: Not glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16258
Sequence Length: 142
Subcellular Location: Virion
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Q9E785 | MLTLFKKGKPKGGSVDDRNSSYRESDPMLVWGTAPPAYLDVYHDERDKNELQFNTKSYLIQANLEVISSKPIERTTEMLKVLDVMVDEYDGSYLSKALIITSYLTIGTHLRRMMSSVKNNHKYNNGFTEVIEFTGTAEIHPRDQEIKYNKYLMTSHMGEPVSISYQFSGKKSKRRGKNILDAYNLELGNGSKPPDLKDLLESYEINLCYNLKGEHGFTNLVKS | Function: Plays a major role in assembly and budding of virion. Completely covers the ribonucleoprotein coil and keep it in condensed bullet-shaped form. Inhibits viral transcription and stimulates replication (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25494
Sequence Length: 223
Subcellular Location: Virion membrane
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P24615 | METYVNKLHEGSIYTAAVQYNVIEKDDDPASLTIWVPMFQSSISADMLIKELINVNILVRQISTPKGPSLKIMINSRSAVLAQMPSKFTISANVSLDERSKLAYDITTPCEIKACSLTCLKVKNMLTTVKDLTMKTFNPTHEIIALCEFENIMTSKRVVIPTFLRSINVKAKDLDSLENIATTEFKNAITNAKIIPYAGLVLVITVTDNKGAFKYIKPQSQFIVDLGAYLEKESIYYVTTNWKHTATKFSIKPIED | Function: Plays a crucial role in virus assembly into filaments and budding. Early in infection, localizes in the nucleus where it may inhibit host cell transcription. Later in infection, traffics to the cytoplasm through the action of host CRM1 to associate with inclusion bodies, the site of viral transcription and replication. During virus assembly and budding, acts as a bridge between the nucleocapsid and the lipid bilayer.
PTM: Phosphorylation is important for oligomerization.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28714
Sequence Length: 256
Subcellular Location: Virion
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P38300 | MSVLRSTCLFFPPRSLLISFNKRRLFSTSRLILNKESETTKKKDKSKQQDFNPRHLGVAAEIFIPSAYKNLPNVFAHPLIVANALIRRLYTFGLNSVQVALFRFQSGIKPSFLLWKNKAIETYINVNTSFAHKNLSDIKGLVSLWVQEALEARSRQLPGNATLDWQLIKFNAVPKLVSVQPIMIPGMPLEHLQLVYKFDTKQRLIKVNQQTKKTETLDRDVVDYIAFLCDATTNDMILMGSLFESKPNDKLPKSYEDDAKVAIHRMKVNGDIYRLPPS | Function: Mitochondrial inner membrane-associated mitoribosome receptor that spatially aligns the mitoribosome exit tunnel with the membrane insertion machinery and allows cotranslational protein membrane insertion.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31811
Sequence Length: 278
Subcellular Location: Mitochondrion inner membrane
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Q9KU26 | MKLNHRILLLIAPVILLSAAASSYIIYTSQKNALLKRTDSYLQLNIEKLASHYRQAQSLVSSYAFTLAKSDIIRHYFSLEKNPYRELELVDNLRETLQILQPNEKQLVSLSILNGHEELLYYAENSSDPFAELDPKVMAYIKQRFASTQKNSDISYTVNSAGEDILVRYDMLDTQTLSTPLSYNRQDVFFVVVYVVLEQFSQLRKKIEFDNQSPIFFTHSPPSYRTGLLQSVELQPGFYAILDPAPKLINAQLHSIQRELLLSFGVSALVTVLMLLLLLYRHVINPILHLDKQLEEVENNQRKNIEKLNTDDEIGRLSSRFYAMYSELHSTYQRTKALAENDHLTKLANRYQFQVQADLLLSRCYDTQHIWVMYIDLDNFKYVNDKYGHQIGDSLLVSFATHVRQLCKNFEASHNTYSIAARLSGDEFAILLVSPKRFNDCAKIFAQRLLAPIQNKDNSPLSHFPITASIGIATFPKDGEHIEKLLLNADTAMYQAKNAGKNQVAYYSQALDQIVQRRNNIERALRLGLFDQEFNLAYQPYFTCSGKRLVGFEVLLRWQSELLGEVSPEEFIPIAEQTGLFGTIDRWVISKAFQEISTLQAIVKEPIQVSINLSSAELNSLKLAQFIHRQAEQFGVSPAWIDFEITETFAADSQSFPLLHELSRLGYGLTIDDFGSGYTSITQLVQYPVQKIKFDRHFLDTLIATNKQNVIRPLIDLCHSQSMKVTAEGIESETMHQWLADYECDYMQGFYFGYPMSLSEISPWLHASNHKKKSYAQDHYCFTEPSQSECR | Function: Plays an essential role in the maintenance and the formation of the three-dimensional structure of the biofilms at the later stages of their development. Absence of mbaA promotes the accumulation of larger amount of biomass on the surfaces at later stage of development, results in the overproduction of an extracellular polymeric substance that accumulates in the matrix of biofilms. This yields biofilms lacking the typical structure consisting of pillars of cells separated by fluid filled channels.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 90794
Sequence Length: 791
Subcellular Location: Cell inner membrane
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Q9FS88 | MHKLFAVRSLSSAIVKSFKSLQNQQAAFSTSLLLDDTQKQFKESVAKFAQENIAPYAEKIDRTNSFPKEINLWKLMGDFNLHGITAPEEYGGLNLGYLYHCIALEEISRASGAVAVSYGVQSNVCINQLVRNGTPDQKQKYLPKLISGDHIGALAMSEPNAGSDVVSMKCRADRVDGGYVLNGNKMWCTNGPVANTLIVYAKTDTTAGSKGITAFIIEKEMPGFSTAQKLDKLGMRGSDTCELVFENCFVPNENVLGQEGKGVYVLMSGLDLERLVLAAGPVGIMQACMDIVIPYVRQREQFGRPIGEFQLIQGKLADMYTALQSSRSYVYAVAKDCDNGKIDPKDCSGTILLAAERATQVALQAIQCLGGNGYINEYPTGRLLRDAKMYEIAAGTSEIRRLVIGRELFKHQ | Function: Short/branched-chain acyl-CoA dehydrogenase (SBCAD). Uses 2-methylbutanoyl-CoA as substrate. Minor activity with the straight-chain substrates, butanoyl-CoA, valeryl-CoA, hexanoyl-CoA, and octanoyl-CoA but no activity with isovaleryl-CoA.
Catalytic Activity: 2-methylbutanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 45086
Sequence Length: 412
Subcellular Location: Mitochondrion
EC: 1.3.8.5
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