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E3YBA4 | MTVKIAQKKVLPVIGRAAALCGSCYPCSCM | Function: Chalkophore involved in scavenging, uptake and suppression of toxicity of copper. Each apo-methanobactin (apo-mb) complexes 1 Cu(2+) or Cu(1+) ion to form Cu(1+)-mb (Cu-mb) which is then taken up by the cell. Enhances growth rate in the presence of copper and reduces growth lag upon exposition to elevated levels of copper. Cu-mb contributes to the switchover from soluble methane monooxygenase (sMMO) to the membrane-bound particulate MMO (pMMO) by inducing transcription of pMMO subunit A. It also stimulates the enzymatic activity of pMMO. In the absence of copper, binds other metal ions, like Zn(2+), Ag(1+), Au(3+), Co(2+), Cd(2+), Fe(3+), Hg(2+), Mn(2+), Ni(2+), Pb(2+) or U(6+), but not Ba(2+), Ca(2+), La(2+), Mg(2+) or Sr(2+). Uptake is an active process, which may involve TonB-dependent transporters, and as such does not involve porins. Cu-Mb can be taken up by other methanotrophic bacteria but not by E.coli. Has Cu-dependent superoxide dismutase-like activity. Shows reductant-dependent oxidase and hydrogen peroxide reductase activities. Reduces copper-levels in liver in a rat model of Wilson disease.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 3143
Sequence Length: 30
Subcellular Location: Secreted
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P64908 | MSDALDEGLVQRIDARGTIEWSETCYRYTGAHRDALSGEGARRFGGRWNPPLLFPAIYLADSAQACMVEVERAAQAASTTAEKMLEAAYRLHTIDVTDLAVLDLTTPQAREAVGLENDDIYGDDWSGCQAVGHAAWFLHMQGVLVPAAGGVGLVVTAYEQRTRPGQLQLRQSVDLTPALYQELRAT | Function: Toxic component of a type II toxin-antitoxin (TA) system. Degrades NAD(+) by phosphorolysis. Neutralized by its cognate antitoxin MbcA.
Catalytic Activity: NAD(+) + phosphate = ADP-alpha-D-ribose 1''-phosphate + H(+) + nicotinamide
Sequence Mass (Da): 20281
Sequence Length: 186
EC: 2.4.2.-
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Q9XI36 | MENTDELVSIELPAPASWKKLFYPKRAGTPRKTEIVFVAPTGEEISSRKQLEQYLKAHPGNPVISEFEWTTGETPRRSSRISQKVKATTPTPDKEPLLKKRRSSLTKKDNKEAAEKNEEAAVKENMDVDKDGKTENAEAEKEKEKEGVTEIAEAEKENNEGEKTEAEKVNKEGEKTEAGKEGQTEIAEAEKEKEGEKAEAENKEAEVVRDKKESMEVDTSELEKKAGSGEGAEEPSKVEGLKDTEMKEAQEVVTEADVEKKPAEEKTENKGSVTTEANGEQNVTLGEPNLDADAEADKGKESKEYDEKTTEAEANKENDTQESDEKKTEAAANKENETQESDVKKTEAAVAEEKSNDMKAEDTNRSLEANQVQQQQGAAASVSC | Function: Probable transcriptional regulator (By similarity). Required for nucleolar dominance that consist in the silencing of rRNA genes inherited from one progenitor in genetic hybrids.
Sequence Mass (Da): 42358
Sequence Length: 384
Domain: The methyl-CpG-binding domain (MBD) functions both in binding to methylated DNA and in protein interactions.
Subcellular Location: Nucleus
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Q9LW00 | MGGEEEVVSVELPAPSSWKKLFYPNKVGSVKKTEVVFVAPTGEEISNRKQLEQYLKSHPGNPAIAEFDWTTSGTPRRSARISEKTKATPSPDKEPPKKRGRTKSPVSKKDAEGEKSEGGGEENSHVKDTEMNPPEGIAENENVTDKNGSGETERVNDAKENIVAEETPNAAPVQEEGESMKEKALDSVDDKSKETDKEKDTGSIEKNSVDVEKKTVEASDEKKNSEAETRNHEENGLTTEAEGKEKTAEGEATG | Function: Transcriptional regulator that binds DNA independently of its methylation status. Required during plant organogenesis and development.
Sequence Mass (Da): 27642
Sequence Length: 254
Domain: The methyl-CpG-binding domain (MBD) functions both in binding to methylated DNA and in protein interactions.
Subcellular Location: Nucleus
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Q73XV3 | MTEVSVETTSAGSESPSIPLPVHIDPADLAAELAVVLSERAGEEYLLYERGGEWVLATGVRAMIELDSDELRVIRDGVTQRQHWSGRPGPVLGEAIDRLLLETDQLFGWIAFEFGVYRYGLQQRLAPGTALARVFWPNGRIVVTREAIQLFGTSTGRRDDVLGVLGDGVPGLRDASAVDVVTDPSNYRDRVASAVAEIAAGRYHKVILSRCLQVPFAVDFPSTYRLARRHNTPVRSFLLRLGGIRAVGYSPELVAAVRHDGVVVTEPLAGTRAFGRGALHDRQARDDLESNSKEIVEHAISVRSSLQEMAEIAEPGTAVVTDFMTVRERGSVQHLGSTVSGRLGTSNDRMDALEALFPAVTASGIPKAGGVEAILRLDEGPRGLYSGAVVMVSADGALDAALTLRAAYEHDGKTWLRAGAGIIEESTPEREFEETCEKLSTLAPYLIARQ | Function: Involved in the incorporation of salicylate into the virulence-conferring salicylate-based siderophore mycobactin. Catalyzes the initial conversion of chorismate to yield the intermediate isochorismate (isochorismate synthase activity), and the subsequent elimination of the enolpyruvyl side chain in a lyase reaction to give salicylate (isochorismate pyruvate-lyase activity). In the absence of magnesium, MbtI displays a chorismate mutase activity and converts chorismate to prephenate.
Catalytic Activity: chorismate = isochorismate
Sequence Mass (Da): 48635
Sequence Length: 450
Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
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P64820 | MTKPTSAGQADDALVRLARERFDLPDQVRRLARPPVPSLEPPYGLRVAQLTDAEMLAEWMNRPHLAAAWEYDWPASRWRQHLNAQLEGTYSLPLIGSWHGTDGGYLELYWAAKDLISHYYDADPYDLGLHAAIADLSKVNRGFGPLLLPRIVASVFANEPRCRRIMFDPDHRNTATRRLCEWAGCKFLGEHDTTNRRMALYALEAPTTAA | Function: Acyltransferase required for the direct transfer of medium- to long-chain fatty acyl moieties from a carrier protein (MbtL) on to the epsilon-amino group of lysine residue in the mycobactin core.
Sequence Mass (Da): 23799
Sequence Length: 210
Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
EC: 2.3.1.-
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Q73ZP9 | MSDAPAESAPAQIDPAQTDPAEQPVQILPRERSDIPDAVARIPRPPVPHLDPPFALRVARLGDADMVAEWMNRPHLAAAWEYDWPTPRWRRHLGAQLQGSYSLPLIGSMRGVDLAYLELYWAAKDLISRYYDAEPYDLGLHAAIADVKLVNRGLGPMLLPRIVASVFATEPRCRRVMFDPDHRNTTARRLCEYAGCRFLGEHDTTNRRMALYALDAPTTDR | Function: Acyltransferase required for the direct transfer of medium- to long-chain fatty acyl moieties from a carrier protein (MbtL) on to the epsilon-amino group of lysine residue in the mycobactin core.
Sequence Mass (Da): 24906
Sequence Length: 221
Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
EC: 2.3.1.-
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P63453 | MTSSPSTVSTTLLSILRDDLNIDLTRVTPDARLVDDVGLDSVAFAVGMVAIEERLGVALSEEELLTCDTVGELEAAIAAKYRDE | Function: Acyl carrier protein involved in the formation of acyl-S-ACP intermediates within the mycobactin biosynthesis process. The aliphatic chains carried by ACP are subsequently transferred on to the mycobactin core by MbtK (By similarity).
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP, leading to the activated holo-ACP form.
Sequence Mass (Da): 8969
Sequence Length: 84
Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
Subcellular Location: Cytoplasm
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Q73ZP6 | MPAGSPENHVSAELLGILRDDLNVDVSRVTPDARLVDDVGLDSVAFAVGMVAIEERLGVTLTEEELLSCETVGDLQAAIAAEPRETRDE | Function: Acyl carrier protein involved in the formation of acyl-S-ACP intermediates within the mycobactin biosynthesis process.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP, leading to the activated holo-ACP form.
Sequence Mass (Da): 9475
Sequence Length: 89
Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
Subcellular Location: Cytoplasm
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Q1BBA1 | MQTSNSESVSAALTEILRDDMNVDIRRVTRESRLIDDVGLDSVAFAVGMVAIEDRLGVALTEEDLLSCDTVGDLEAAIQAKVPSSPSGQ | Function: Acyl carrier protein involved in the formation of acyl-S-ACP intermediates within the mycobactin biosynthesis process.
PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP, leading to the activated holo-ACP form.
Sequence Mass (Da): 9466
Sequence Length: 89
Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
Subcellular Location: Cytoplasm
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A0QUA1 | MNVLSAALTEAMTTSSADLVVFEPETRTWHRHPWGQVHLRAQNVAERIGQDGSSAVGIVGEPTVEGVAAILGALLAGSAVSILPGLVRGADPDQWADSTLNRFANIGVTTVFSHGSYLEQLRTRDSSLVIHDDAEVAHAQRSTTLELGAPLGEFAVLQGTAGSTGTPRTAQLRPDAVLANLRGLAERVGLAGSDIGCSWLPLYHDMGLTFLLSAAVGGTETWQAPTTAFASAPFSWVHWLTESRATLTAAPNMAYGLIGKYSRRLTDVDLSAMRFALNGGEPVDIDGTARFGTELSRFGFDPGALSPSYGLAESSCAVTVPVPGVGLKVDEITVTTEAGSSTQKLAVLGHAIAGMEVRLQPGDEDAGVVDREVGEVEIRGTSMMSGYRGEAPLDPGEWFPTGDLGYLTDDGLVICGRKKELITVAGRNIFPTEIERIAARVKGVREGAVVAVGTNERAVRPGLVIAAEFRGPDEAGARSEVVQRVASECGVVPADVVFLAPGSLPRTSSGKLRRLEVKRQLEESKG | Function: Activates lipidic moieties required for mycobactin biosynthesis . Converts medium- to long-chain aliphatic fatty acids into acyl adenylate, which is further transferred on to the phosphopantetheine arm of the carrier protein MbtL . Shows a strong preference for palmitic acid (C16) and cannot use short-chain fatty acids . Proceeds via a Bi Uni Uni Bi ping-pong mechanism. During the first half-reaction (adenylation), fatty acid binds first to the free enzyme, followed by ATP and the release of pyrophosphate to form the adenylate intermediate. During the second half-reaction (ligation), holo-MbtL binds to the enzyme followed by the release of products AMP and acylated MbtL .
PTM: Acetylated on Lys-511 and Lys-260 by Pat. Lys-511 is the major acetylation site. Acetylation results in the inactivation of the enzyme.
Catalytic Activity: a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate
Sequence Mass (Da): 55359
Sequence Length: 526
Pathway: Siderophore biosynthesis; mycobactin biosynthesis.
EC: 6.2.1.20
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Q7XJE6 | MYPPPPSSIYAPPMLVNCSGCRTPLQLPSGARSIRCALCQAVTHIADPRTAPPPQPSSAPSPPPQIHAPPGQLPHPHGRKRAVICGISYRFSRHELKGCINDAKCMRHLLINKFKFSPDSILMLTEEETDPYRIPTKQNMRMALYWLVQGCTAGDSLVFHYSGHGSRQRNYNGDEVDGYDETLCPLDFETQGMIVDDEINATIVRPLPHGVKLHSIIDACHSGTVLDLPFLCRMNRAGQYVWEDHRPRSGLWKGTAGGEAISISGCDDDQTSADTSALSKITSTGAMTFCFIQAIERSAQGTTYGSLLNSMRTTIRNTGNDGGGSGGVVTTVLSMLLTGGSAIGGLRQEPQLTACQTFDVYAKPFTL | Function: Cysteine protease that cleaves specifically after arginine or lysine residues. Does not cleave caspase-specific substrates. Acts as a positive regulator of cell death. Required for both oxidative stress cell death response and hypersensitive cell death response mediated by immune response.
PTM: Proteolytically processed; by an autocatalytic mechanism.
Sequence Mass (Da): 39792
Sequence Length: 367
EC: 3.4.22.-
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A0A7R7ZDZ6 | MFKHTKMLQHPAKPDRPDPLFAKKMQEILGGQFGEISVAMQYLFQGWNTRGNEKYKDLLMDTATEELGHVEMIATMIARLLEDAPLDQQEKAAEDPVIGSILGGMNPHHAIVSGLGAMPESSTGVPWSGGYIVASGNLLADFRANLNAESQGRLQVARLFEMTDDKGVKDMLSFLLARDTMHQNQWLAAIKELEAQEGPVVPGTFPKALEKQEFSHQLINFSEGEESAKQNWLNEKAPDGEAFEYVKEAKTFGEKPELKPAPPCVHNTLPGRE | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Catalyzes the decomposition of hydrogen peroxide into water and oxygen . No significant activity could be detected with any of the other tested substrates, including glutathione, pyrogallol, NADH, NADPH and o-dianisidine .
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 30242
Sequence Length: 273
EC: 1.11.1.6
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Q97FE0 | MFKHEKQLLNGMQVKVERENPQYAVLMQEQLGGANGELKAAMQYLSQSFRVKDQALKDLFLDIGTEELSHMEIVAETINLLNGHSVNYEVVGVGEVESHVLSGLTPFLVNSSGEPWTANYVSVTGDIVADLLSNIASEQRAKVVYEYLYRQINDKEVRRTIDFLLNREEAHNALFREALNKVKNEGSNKDFGVTEDSKLYFDLSTPGRYVQDPNPTEPSFSNPRR | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Catalyzes the decomposition of hydrogen peroxide into water and oxygen.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 25444
Sequence Length: 225
EC: 1.11.1.6
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O43772 | MADQPKPISPLKNLLAGGFGGVCLVFVGHPLDTVKVRLQTQPPSLPGQPPMYSGTFDCFRKTLFREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKKLQQKHPEDVLSYPQLFAAGMLSGVFTTGIMTPGERIKCLLQIQASSGESKYTGTLDCAKKLYQEFGIRGIYKGTVLTLMRDVPASGMYFMTYEWLKNIFTPEGKRVSELSAPRILVAGGIAGIFNWAVAIPPDVLKSRFQTAPPGKYPNGFRDVLRELIRDEGVTSLYKGFNAVMIRAFPANAACFLGFEVAMKFLNWATPNL | Function: Mediates the electroneutral exchange of acylcarnitines (O-acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-carnitines) with free carnitine ((R)-carnitine or L-carnitine) across the mitochondrial inner membrane, via a ping-pong mechanism (Probable). Key player in the mitochondrial oxidation pathway, it translocates the fatty acids in the form of acylcarnitines into the mitochondrial matrix, where the carnitine palmitoyltransferase 2 (CPT-2) activates them to undergo fatty acid beta-oxidation (Probable). Catalyzes the unidirectional transport (uniport) of carnitine at lower rates than the antiport (exchange) .
Catalytic Activity: (R)-carnitine(out) + O-acetyl-(R)-carnitine(in) = (R)-carnitine(in) + O-acetyl-(R)-carnitine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32944
Sequence Length: 301
Subcellular Location: Mitochondrion inner membrane
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P60355 | MFKHTRKLQYNAKPDRSDPIMARRLQESLGGQWGETTGMMSYLSQGWASTGAEKYKDLLLDTGTEEMAHVEMISTMIGYLLEDAPFGPEDLKRDPSLATTMAGMDPEHSLVHGLNASLNNPNGAAWNAGYVTSSGNLVADMRFNVVRESEARLQVSRLYSMTEDEGVRDMLKFLLARETQHQLQFMKAQEELEEKYGIIVPGDMKEIEHSEFSHVLMNFSDGDGSKAFEGQVAKDGEKFTYQENPEAMGGIPHIKPGDPRLHNHQG | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Catalyzes the decomposition of hydrogen peroxide into water and oxygen.
Catalytic Activity: 2 H2O2 = 2 H2O + O2
Sequence Mass (Da): 29743
Sequence Length: 266
Domain: Each subunit is composed of three distinct structural regions: an N-terminal polypeptide, a central four-helix bundle that serves as the scaffolding for the catalytic active site, and a C-terminal tail.
EC: 1.11.1.6
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Q9Z2Z6 | MADEPKPISPFKNLLAGGFGGMCLVFVGHPLDTVKVRLQTQPPSLSGQPPMYSGTLDCFRKTLMREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKKLQQKSPEDELSYPQLFTAGMLSGVFTTGIMTPGERIKCLLQIQASSGENKYSGTLDCAKKLYQEFGIRGFYKGTVLTLMRDVPASGMYFMTYEWLKNLFTPEGKSVSDLSVPRILVAGGFAGIFNWAVAIPPDVLKSRFQTAPPGKYPNGFRDVLRELIREEGVTSLYKGFNAVMIRAFPANAACFLGFEIAMKFLNWIAPNL | Function: Mediates the electroneutral exchange of acylcarnitines (O-acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-carnitines) with free carnitine ((R)-carnitine or L-carnitine) across the mitochondrial inner membrane, via a ping-pong mechanism. Key player in the mitochondrial oxidation pathway, it translocates the fatty acids in the form of acylcarnitines into the mitochondrial matrix, where the carnitine palmitoyltransferase 2 (CPT-2) activates them to undergo fatty acid beta-oxidation. Catalyzes the unidirectional transport (uniport) of carnitine at lower rates than the antiport (exchange).
Catalytic Activity: (R)-carnitine(out) + O-acetyl-(R)-carnitine(in) = (R)-carnitine(in) + O-acetyl-(R)-carnitine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33027
Sequence Length: 301
Subcellular Location: Mitochondrion inner membrane
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P97521 | MAEEPKPISPLKNLLAGGFGGVCLVFVGHPLDTVKVRLQTQPPSLPGQPPMYSGTIDCFRKTLFREGITGLYRGMAAPIIGVTPMFAVCFFGFGLGKRLQQKSPEDELTYPQLFTAGMLSGVFTTGIMTPGERIKCLLQIQASSGKNKYSGTLDCAKKLYQEFGIRGFYKGTALTLMRDVPASGMYFMTYEWLKNLFTPQGKSVHDLSVPRVLVAGGFRGIFNWVVAIPPDVLKSRFQTAPPGKYPNGFRDVLRELIREEGVTSLYKGFNAVMIRAFPANAACFLGFEIPMKILNWIAPNL | Function: Mediates the electroneutral exchange of acylcarnitines (O-acyl-(R)-carnitine or L-acylcarnitine) of different acyl chain lengths (ranging from O-acetyl-(R)-carnitine to long-chain O-acyl-(R)-carnitines) with free carnitine ((R)-carnitine or L-carnitine) across the mitochondrial inner membrane, via a ping-pong mechanism . Key player in the mitochondrial oxidation pathway, it translocates the fatty acids in the form of acylcarnitines into the mitochondrial matrix, where the carnitine palmitoyltransferase 2 (CPT-2) activates them to undergo fatty acid beta-oxidation (Probable). Catalyzes the unidirectional transport (uniport) of carnitine at lower rates than the antiport (exchange) .
PTM: The N-terminus is blocked.
Location Topology: Multi-pass membrane protein
Catalytic Activity: (R)-carnitine(out) + O-acetyl-(R)-carnitine(in) = (R)-carnitine(in) + O-acetyl-(R)-carnitine(out)
Sequence Mass (Da): 33154
Sequence Length: 301
Subcellular Location: Mitochondrion inner membrane
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A0R2W9 | MSELRLMAVHAHPDDESSKGAATTARYAAEGARVMVVTLTGGERGDILNPAMDLPEVHGRIAEVRRDEMAKAAEILGVEHHWLGFVDSGLPEGDPLPPLPDGCFALVPLEEPVKRLVRVIREFRPHVMTTYDENGGYPHPDHIRCHQVSVAAYEAAADHLLYPDAGEPWAVQKLYYNHGFLRQRMQLLQEEFAKNGQEGPFAKWLEHWDPDNDVFANRVTTRVHCAEYFHQRDDALRAHATQIDPKGDFFHAPIEWQQRLWPTEEFELARARVPVTLPEDDLFKGVEP | Cofactor: Binds 1 zinc ion per subunit.
Function: A mycothiol (MSH, N-acetyl-cysteinyl-glucosaminyl-inositol) S-conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine conjugate and the MSH precursor. Involved in MSH-dependent detoxification of a number of alkylating agents and antibiotics. Activity is specific for the mycothiol moiety.
Catalytic Activity: H2O + mycothiol S-conjugate = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + an N-acetyl-L-cysteine-S-conjugate
Sequence Mass (Da): 32674
Sequence Length: 288
EC: 3.5.1.115
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P9WJN0 | MSELRLMAVHAHPDDESSKGAATLARYADEGHRVLVVTLTGGERGEILNPAMDLPDVHGRIAEIRRDEMTKAAEILGVEHTWLGFVDSGLPKGDLPPPLPDDCFARVPLEVSTEALVRVVREFRPHVMTTYDENGGYPHPDHIRCHQVSVAAYEAAGDFCRFPDAGEPWTVSKLYYVHGFLRERMQMLQDEFARHGQRGPFEQWLAYWDPDHDFLTSRVTTRVECSKYFSQRDDALRAHATQIDPNAEFFAAPLAWQERLWPTEEFELARSRIPARPPETELFAGIEP | Cofactor: Binds 1 zinc ion per subunit.
Function: A mycothiol (MSH, N-acetylcysteinyl-glucosaminyl-inositol) S-conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine conjugate (AcCys S-conjugate, a mercapturic acid) and the MSH precursor. Involved in MSH-dependent detoxification of a number of alkylating agents and antibiotics.
Catalytic Activity: H2O + mycothiol S-conjugate = 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + an N-acetyl-L-cysteine-S-conjugate
Sequence Mass (Da): 32732
Sequence Length: 288
EC: 3.5.1.115
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P05528 | MVTLKMAIIFLMEQIRTPFSLIWTIMSPTVLFFFLHFNEIELHYGDTAWLGKQISWFVGYISFSVVLFNYCLYLVGRRESGFIATFVHNMDGRLLFIRSQLIASLIMSILYVFFFILVVLTGFQASPDYQIVMIILKSIYINAFMMVSLTFMASFRVTFQTASTIYSVLITVCMVSGIVSLKYNEGIVYWINQVNPIAIYSTILQSDQELSLMTIFFYSIMLIISIISALTFKTEPVWSSQ | Function: Together with two further proteins McbF and McbG this protein causes immunity to the peptide antibiotic microcin B17 (MccB17), which inhibits DNA replication in enterobacteriaceae. Immunity is determined by two different mechanisms. McbE is involved in the production of extracellular MccB17 and, in a complex with McbF it also serves as 'pump' for the export of active MccB17 from the cytoplasm to the periplasmic space.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27801
Sequence Length: 241
Subcellular Location: Cell membrane
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P10911 | MAEANPRRGKMRFRRNAASFPGNLHLVLVLRPTSFLQRTFTDIGFWFSQEDFMLKLPVVMLSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIENFALTVKEMAQMLQSFGTELAETELPDDIPSIEEILAIRAERYHLLKNDITAVTKEGKILLTNLEVPDTEGAVSSRLECHRQISGDWQTINKLLTQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQQLVTEVEFLLNQQAELADVTGTIAQVKQKIKKLENLDENSQELLSKAQFVILHGHKLAANHHYALDLICQRCNELRYLSDILVNEIKAKRIQLSRTFKMHKLLQQARQCCDEGECLLANQEIDKFQSKEDAQKALQDIENFLEMALPFINYEPETLQYEFDVILSPELKVQMKTIQLKLENIRSIFENQQAGFRNLADKHVRPIQFVVPTPENLVTSGTPFFSSKQGKKTWRQNQSNLKIEVVPDCQEKRSSGPSSSLDNGNSLDVLKNHVLNELIQTERVYVRELYTVLLGYRAEMDNPEMFDLMPPLLRNKKDILFGNMAEIYEFHNDIFLSSLENCAHAPERVGPCFLERKDDFQMYAKYCQNKPRSETIWRKYSECAFFQECQRKLKHRLRLDSYLLKPVQRITKYQLLLKELLKYSKDCEGSALLKKALDAMLDLLKSVNDSMHQIAINGYIGNLNELGKMIMQGGFSVWIGHKKGATKMKDLARFKPMQRHLFLYEKAIVFCKRRVESGEGSDRYPSYSFKHCWKMDEVGITEYVKGDNRKFEIWYGEKEEVYIVQASNVDVKMTWLKEIRNILLKQQELLTVKKRKQQDQLTERDKFQISLQQNDEKQQGAFISTEETELEHTSTVVEVCEAIASVQAEANTVWTEASQSAEISEEPAEWSSNYFYPTYDENEEENRPLMRPVSEMALLY | Function: Guanine nucleotide exchange factor (GEF) that modulates the Rho family of GTPases. Promotes the conversion of some member of the Rho family GTPase from the GDP-bound to the GTP-bound form. Isoform 1 exhibits no activity toward RHOA, RAC1 or CDC42. Isoform 2 exhibits decreased GEF activity toward CDC42. Isoform 3 exhibits a weak but significant activity toward RAC1 and CDC42. Isoform 4 exhibits significant activity toward RHOA and CDC42. The truncated DBL oncogene is active toward RHOA, RAC1 and CDC42.
PTM: Phosphorylation by TNK2 enhances guanine nucleotide exchange factor (GEF) activity toward Rho family proteins.
Sequence Mass (Da): 107673
Sequence Length: 925
Domain: The CRAL-TRIO domain is involved in interaction with inositol phospholipids.
Subcellular Location: Cytoplasm
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Q54EV4 | MVINNQNNNNQNNNQNNNNKNDNLNNSTTTTTTTATTTKSSTLFHSNDFFSGLIAGIVSRTLTAPLERIKILNQVEVILKDGTKYNRIIPAFKVIIKEEGIAGLFRGNFVNIIKAGPQSAIRFYSYGAFKRMASEPDGSISVINRMWAGASSGVVSVALTHPLDVIKTHITVIAPTAATIKNVTKGIYRDLGIIGFFRGLSAGILNIAPFAALNFTFYETIKEKTQQYILKSPPLYAPSIYGAISGGLTMTILYPLDVVKRRIMLQHFDRNQLPIYKNFIDAIIKITKTEGISALYKGIRPAYLKVIPTVSINFLIYEGAITLFEKK | Function: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36132
Sequence Length: 327
Subcellular Location: Mitochondrion inner membrane
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Q54MZ4 | MSNNNNNNNNNNNNNNNNNNNNNNNNNNDKNNNNNIDSSIKEKKLKEWFDKFDVDKDGSLDSNELKKGFKLHANIDMKDEQITKMMERADSNKNHRIEWDEFLKVASDSSSPEIEDIAEHWLQYSTKPIVHAPADVPSWKLLLSGGVAGAVSRTCTSPLERLKILNQVGHMNLEQNAPKYKGRGIIQSLKTMYTTEGFIGFFKGNGTNVIRIAPYSAIQFLSYEKYKNFLLNNNDQTHLTTYENLFVGGAAGVTSLLCTYPLDLIRSRLTVQVFGNKYNGIADTCKMIIREEGVAGLYKGLFASALGVAPYVAINFTTYENLKKTFIPKDTTPTVVQSLTFGAISGATAQTLTYPIDLIRRRLQVQGIGGKDILYNGTFDAFRKIIRDEGVLGLYNGMIPCYLKVIPAISISFCVYEVMKKILKIDSKKISYQS | Function: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48684
Sequence Length: 434
Subcellular Location: Mitochondrion inner membrane
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B0G159 | MVLNENDKEFVKKLFDSLDKDNNGKLTREEIKEGFFKLRIPSSEKDIESFLTNVDKDKDGSVSFKEFEDFTIENIKKLKIVFEELDTNKSGTLDIHEIEESIKKLNIPLYSEQELIRLFHRIDKNRDNQIDFNEWRELLVLLPNSNLQLIISFWKDSQILDAGFDNGGFIPPMVEKKEKASSLRNTITYMLAGSVAGFASRTSTAPLERVKIMCQLNHGKPISLISAFKACYKDGGIKGFFRGNLANIIKVSPESAVKFGTYEYVKKLFAENDCELTSAQRFISGSVAGVVSHTTLFPLEVVRLRLSAEIAGTYNGIFDCFKKIAISEKSIRPFYRGLGASITATIPHSGVNMMVYEFLKHKVIKMTGNEFPTAGQLLVCASTSSVCGQLVGYPFHVVKSRLITQGSSVNQEKYTGLFDGLTKIIKKEGPIGLYKGIVPSFMKSIPSHSITFIVYEGFKKAFDVNLKEKKHH | Function: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53100
Sequence Length: 472
Subcellular Location: Mitochondrion inner membrane
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Q8NI22 | MTMRSLLRTPFLCGLLWAFCAPGARAEEPAASFSQPGSMGLDKNTVHDQEHIMEHLEGVINKPEAEMSPQELQLHYFKMHDYDGNNLLDGLELSTAITHVHKEEGSEQAPLMSEDELINIIDGVLRDDDKNNDGYIDYAEFAKSLQ | Function: The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins. Plays a role in the secretion of coagulation factors.
Sequence Mass (Da): 16390
Sequence Length: 146
Domain: Essentially unstructured in the absence of calcium ions. Requires calcium ions for folding.
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment
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Q55E85 | MDSTKTNNKWAAAGILNSVGKDFVAGSVGGMSSIMAGHPFDTIKVMLQDASGNLPKFKNGFQALKYIMKVDGIKGIYRGLSVPLFSVSFTNSVFFATNNFCQSYFHPPCKDENGEDILIPYHKAAAAGAIAGGVISLLITPRDLVKSKLQVQCRPFGSTNVSLQYKGPIDVIRQTIKRDGIKGMFKGIRSTFCRDIPGDAVYFVVYEFMKRKLLALSKNNNNNNNNNDNNDNSSPKAGVPAWVAIGAGGCAGMSFWMSIYPMDVVKTRIQTQPDHLPPQYTSVLQTITKIYREEGISVFFRGFSATILRAFPTSAVNFLMYETTRNLLNSKDPFYNNNDHYNAE | Function: Calcium-dependent mitochondrial solute carrier. Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37959
Sequence Length: 344
Subcellular Location: Mitochondrion inner membrane
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Q55E45 | MENKKESSLLYILTGATSGLLADSIMHPVDTVRARVQIEKVGKSQYKGTFNALNQIIKNEGVSYLYKGFPIVATATVPAHALYFLGYEYSKQWVTDRYGKKWGESTITHFSAGFVADALGSLIWVPMDIIKQRLQVQTNTQKLNPNQTYYKGSFHAGKIILQEEGIRGLYRGFMPALATYGPFVGIYFSVYEKCKSTISSLLSKEKDQYLPIPYQLGSGFFAGAFAAAVTCPLDVIKTRIQVQRSTEKQIYKGMWDSFKTILKEEGPKAFVKGMGARIWWIAPGNALTIASYEQLKYLFKDLI | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34018
Sequence Length: 303
Subcellular Location: Mitochondrion inner membrane
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Q54BM3 | MASNNKDSQLMIALKDIVAGSIGGVGQVFTGHPLDTIKVRLQTQSVGNPIYSGTMDCLKKTISQEGFAGLYKGVASPLVGLSIMNSVMFLAYGQSKTLIQKLSDNPNEALDLKGLTAAGALAGIAIGFVDAPVDLFKSQMQVQQGDKNQYKSTADCAKQIWKVGGVRGVFQGLGATLVRDIPANACYFGAYELCRDFLASKDNISVNQLSSLQIMAAGGAGGVSYWTLTYPADVVKSTMQTDAIVKSQRKYKNMIDCASKIYKQQGIAGFYKGFTPCFIRSVPANAACFVLYEKARQIMS | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Mediates the transport of acylcarnitines of different length across the mitochondrial inner membrane from the cytosol to the mitochondrial matrix for their oxidation by the mitochondrial fatty acid-oxidation pathway (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32112
Sequence Length: 300
Subcellular Location: Mitochondrion inner membrane
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Q86I81 | MVNGEEYVETPNLIHDEETRKDVKFNLGIELLAGTLAGVSSCILFYPLECVEAKLQVQSSSTAVAATMLGLKKNGGSGSGSSSSSSISHQTPNGPIAMAKSILRNEGFKGFYQGVSPTILGNAVNWGVYFSIYRATNHWWNSTDINGNQYQGPAWVGHSVSAITAGVITTAIVNPFWVLKIRLATSKKYSGMKHAFQSILRSEGVGGFWKGVGVSFIGVSEGLFQFVSYEYILNQMKESNLKMNGGELSVGNYLFAGGTARLIAGVLTYPYLLIRSSLQSETCPYKSMSEAVKGIYKTNGIKGFYKGIGPNLARSIPPAAFMLYIVEFFRDTLTNFSQ | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Transports folate across the inner membranes of mitochondria (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36655
Sequence Length: 338
Subcellular Location: Mitochondrion inner membrane
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Q54VX4 | MSSSHTIQETKEVHTKTNKRIQWDDLDPKRYYFYNFLLGGSIDLLMFPLDVIRTRLQVQGSQNVIQSFPQYNGTFDGFKKLIRLEGKRALYKGFLTSECGYLCSRAIYFGSYEFVKQGFLKGRSDSDSDLLFVTTISGAISEALASVIWVPFDVATQSVQIQGSLSKPKYKGGSDVFKKIYGERGIKGLYKGFGATIIRNVPYSGIWWGTYEISKSKLTQFNIRQKLGLKERSSHSLAVSAEIDKNNPSHEVENEDPIIHFISGFFAAVFATSITNPLDVAKTRLQTGVFPENEKPNFYTIIKSTIRKEGIRALWKGLVPSLLTSTPYSMISIFLYEEVKKLSLK | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39012
Sequence Length: 345
Subcellular Location: Mitochondrion inner membrane
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Q54W11 | MIASKETKEKIRNFIGGFASGAASTLAGHPFDTLKVRLQTEGSTGRFRGLAHCFTTTIKEEGFFALYKGVTPPLLGMSIINSCMFGAMNIVKSKIHTDKSTPISLGEIMVSGAITGWIVSFVACPIETVKSKLQVQYTGVKLYNGPIDCIKKIGIRGLYKALIPTGFQRNSLYAYFGCYELAQRYLRREDGSMTMGRSFIAGGIAGTGFWLTNFPFDVIRSRIMTMPYNESPPRYKGMIDCAKHIYRVDGLKGFWKGFSPCLLRTFPANGATFVAYECVMKFFPM | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31583
Sequence Length: 285
Subcellular Location: Mitochondrion inner membrane
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Q54QN2 | MRYILNNNVEGTSALLGSTVATAFLQPFDFLKIRLQGSGFASGGDLNKFKRVGVIDTCKNVLKNEGIKQFWRGSSPTIVASGIAWGTYMHFYEAYKNILKSKYNVTQLNTFDHFICAVGASATQVFITNPIFLIKTRMQLQTPGSANYYTGIFDGIKKTVKVEGFKGLYKGVIPSLWLTFHGGIQMSSYEHIKFYFSSNSGKSLDSLNASEIFIASSISKFLASTILYPFQVVKTRLQDERNIPNQNNVRVYNGTKDVIFKILKNEGIIGFYRGLVPNTLKVIPNTSITLLLYEEIKKSFNYIINE | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Transports folate across the inner membranes of mitochondria (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34343
Sequence Length: 306
Subcellular Location: Mitochondrion inner membrane
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Q54BF6 | MAGDLTPSLFLKYGFGGALSCSITHSLVVPLDVVKTLLQTNPGKYTGMMNGFSTVIKEQGPSGLLQGLGPTAVGYALQGFLKFGFYEVFKKTYADAVGEKADQFRIPIWLAASATAEVIADIALCPNEAVRIRLVAEPTFAKSPVEAFGKIFKQEGVLGFYKGLPPILLKQVPYTMAKFAVFEFTAENVYKGLAASGKPKESLTDGQKLSVSLGSGIVAGIVAAIVSQPADTILSKINQEKTDGGVVKAIGNIMRRLGVRGLFLGLPTRCFMVGTLTAGQFFIYDGIKQMLGLTPAKK | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Transports phosphate groups from the cytosol to the mitochondrial matrix. Phosphate is cotransported with H(+) (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31687
Sequence Length: 298
Subcellular Location: Mitochondrion inner membrane
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Q54DU1 | MATTSVSSPKSKPSWVSFLSGGLAGVTAKSAVAPLERVKILYQIKSELYSLNSVYGSMLKIVENEGIKGLWRGNSATILRVFPYAAVQFLSYETIKNHLVADKSSSFQIFLAGSAAGGIAVCATYPLDLLRARLAIEIHKKPTKPHHLLKSTFTKDGVKGIYRGIQPTLIGILPYGGISFSTFEFLKRIAPLNEIDENGQISGTYKLIAGGIAGGVAQTVAYPFDVVRRRVQTHGFGDAKAVVNLEHGTLRTIAHILKEEGILALYKGLSINYVKVIPTASIAFYTYEYLSNFFNKL | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Required for the accumulation of coenzyme A in the mitochondrial matrix (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32323
Sequence Length: 297
Subcellular Location: Mitochondrion inner membrane
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Q54QI8 | MTVHGNTKTSPMVTLLAGGVSGVIAKSTIAPLERVKILYQVKSKMYSFNSVYGLMKNIIKNEGLAGLWKGNTATILRIFPYSAIQWTSYDYLKNNFVTDKKSSVQIFIAGSLGFSCAILLTYPLDVIRARLALSYSNNNNNNSINSKNLNSSTQPPKVLKNGIGAVNIEKSIDFNGYKTKGLFKGIWRGILPTLYGSIPYAGVGYSSFEYFKRIAPDSFRNEKGDVIGIYKLISGGVAGGLGQTAAYPLDVVRRRIQTTGYGDGKGVENLKHSTLKTMFTIFQKEGIYALFKGISINYIKVIPTNGVAFLTYETLCDYFNSKLNKN | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. May be involved in the accumulation of coenzyme A in the mitochondrial matrix (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35861
Sequence Length: 326
Subcellular Location: Mitochondrion inner membrane
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O86028 | MTEKTIKDWEALAEKELRVSPEGLVWHTPEGIDVKPLYTSDDMSGIGHLNSLPGFEPFVRGPRATMYAGRPWTVRQYAGFSTAEASNAFYRRNLAAGQQGVSVAFDLATHRGYDSDHPRVQGDVGKAGVAIDSVEDMKILFDGIPLDRISVSMTMNGAVIPILASFIVAGEEQGVSRDKLSGTIQNDILKEFMVRNTYIYPPEPSMRIVADIIEYTAKEMPKFNSISISGYHMQEAGATLVQELAFTLADGREYVRAALAKGLNVDDFAGRLSFFFAIGMNFFMEAAKLRAARLLWTRIMQEFKPEKASSLMLRTHCQTSGVSLQEQDPYNNIVRTAFEAMSAVLGGTQSLHTNSFDEAMALPTDFSARIARNTQLILQHETGVTKVVDPLAGSYYVESLTNELAEKAWGLIEEVEALGGMTKAVNAGLPKRLIEEAATRRQAAVDRAEEVIVGVNKYRLENEQPIDILQIDNAAVRTAQVKRIEETRRRRDSQKMKQALDALADVARSGKGNLLAAAVEAARARATVGEITDAMREAFGDYTAIPEVVTDIYGKAYEGDPELGVLAGRLGEATKRLGHKPKIMVAKLGQDGHDRGAKVIASAFGDIGFDVVAGPLFQTPEEAADLALAEEVTVIGVSSLAAGHRTLMPQLAEALKKRGGEDIIVVCGGVIPRQDYDYLMENGVAAVFGPGTQVLDAARAVLDLIEGKRRNV | Cofactor: Monovalent cations such as NH4(+), Rb(+), Cs(+), K(+), Li(+) or Na(+) are required for enzyme activity.
Function: Radical enzyme that catalyzes the transformation of methylmalonyl-CoA to succinyl-CoA. Is required for growth on the polyhydroxyalkanoate degradation pathway intermediates 3-hydroxybutyrate and acetoacetate as sole carbon source.
Catalytic Activity: (R)-methylmalonyl-CoA = succinyl-CoA
Sequence Mass (Da): 77501
Sequence Length: 712
Pathway: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 3/3.
EC: 5.4.99.2
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Q9UXG1 | MEIPSKQIDYRDVFIEFLTTFKGNNNQNKYIERINELVAYRKKSLIIEFSDVLSFNENLAYEIINNTKIILPILEGALYDHILQLDPTYQRDIEKVHVRIVGIPRVIELRKIRSTDIGKLITIDGILVKVTPVKERIYKATYKHIHPDCMQEFEWPEDEEMPEVLEMPTICPKCGKPGQFRLIPEKTKLIDWQKAVIQERPEEVPSGQLPRQLEIILEDDLVDSARPGDRVKVTGILDIKQDSPVKRGSRAVFDIYMKVSSIEVSQKVLDEVIISEEDEKKIKDLAKDPWIRDRIISSIAPSIYGHWELKEALALALFGGVPKVLEDTRIRGDIHILIIGDPGTAKSQMLQFISRVAPRAVYTTGKGSTAAGLTAAVVREKGTGEYYLEAGALVLADGGIAVIDEIDKMRDEDRVAIHEAMEQQTVSIAKAGIVAKLNARAAVIAAGNPKFGRYISERPVSDNINLPPTILSRFDLIFILKDQPGEQDRELANYILDVHSGKSTKNIIDIDTLRKYIAYARKYVTPKITSEAKNLITDFFVEMRKKSSETPDSPILITPRQLEALIRISEAYAKMALKAEVTREDAERAINIMRLFLESVGVDMESGKIDIDTIMTGKPKSAREKMMKIIEIIDSLAVSSECAKVKDILKEAQQVGIEKSNIEKLLTDMRKSGIIYEAKPECYKKV | Function: Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 77428
Sequence Length: 686
EC: 3.6.4.12
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Q46970 | MSFLNFAFSPVFFSIMACYFIVWRNKRNEFVCNRLLSIIIISFLICFIYPWLNYKIEVKYYIFEQFYLFCFLSSLVAVVINLIVYFILYRRCI | Function: Probably able to protect the producing cell against microcin N (microcin 24).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11426
Sequence Length: 93
Subcellular Location: Cell inner membrane
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Q46971 | MRELDREELNCVGGAGDPLADPNSQIVRQIMSNAAWGAAFGARGGLGGMAVGAAGGVTQTVLQGAAAHMPVNVPIPKVPMGPSWNGSKG | Function: Active against E.coli and Salmonella, but not Listeria or Campylobacter . Channel-forming microcin (By similarity). Probably neutralized by its immunity protein McnI (Probable).
PTM: Mass spectrometry suggests 3 of the 4 Met residues of the mature peptide are oxidized.
Sequence Mass (Da): 8896
Sequence Length: 89
Subcellular Location: Secreted
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Q69HT9 | MMDMKENDQKRNDMMDMKSHDERKNLNSSQGKNEITFPKVLDPKKDNNGYKSYTLKAQKGKTEFYKGNFSNTLGYNGNLLGPTLKLKKGDKVKIKLVNNLDENTTFHWHGLEIDGKVDGGPSQVIKPGKEKTIKFEVKQEAATLWYHPHPSPNTAKQVYNGLSGLLYIEDDKKNNYPSNYGKNDLPIIIQDKTFVSKKLNYTKTKDEDGTQGDTVLVNGKVDPKLTTKEGKIRLRLLNGSNARDLNLKLSNNQSFEYIASEGGHLEKTKKLKEINLAPSARKEIVIDLSKMKEDKVNLVDNDETVILPIINKEKSTNKDTTPKVDKKIKLEGMDDNVTINGKKFDPNRIDFTQKVNRKETWEIENVKDKMSGMKHPFHIHGTQFKVLSVDGKKPSEDMRGKKDVISLEPGQKAKIEVVFKNTGTYMFHCHILEHEDNGMMGQIKVTK | Cofactor: Binds 4 Cu cations per monomer.
Function: May be involved in copper homeostasis and oxidative stress response. Oxidizes the substrate 3,3'-dimethoxybenzidine in vitro. Also possesses low levels of phenoloxidase and ferroxidase activities.
Sequence Mass (Da): 50840
Sequence Length: 447
Subcellular Location: Cytoplasm
EC: 1.-.-.-
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Q8CQF6 | MMNMKEDKKNTMDMKNMKHHDERKKLNSSQGKNEIIFPEVAESKKDNNGYKNYTLKAQEGKTEFYKNNFSNTLGYNGNLLGPTLKLKKGDKVKIKLINNLDENTTFHWHGLEINGKVDGGPSQVIKPGKEKTIKFEVNQDSATLWYHPHPSPNTAKQVYNGLSGLLYIEDSKKNNYPSNYGKNDLPIIIQDKTFVSKKLNYSKTKDEDGTQGDTVLVNGIVNPKLTAKEEKIRLRLLNGSNARDLNLKLSNNQSFEYIASDGGQLKNAKKLKEINLAPSERKEIVIDLSKMKGEKISLVDNDKTVILPISNKEKSSNKGNTPKVSKKIKLEGMNDHVTINGNKFDPNRIDFTQKLNQKEVWEIENVKDKMGGMKHPFHIHGTQFKVLSVDGEKPPKDMRGKKDVISLEPGQKAKIEVVFKNTGTYMFHCHILEHEENGMMGQIKVTN | Cofactor: Binds 4 Cu cations per monomer.
Function: May be involved in copper homeostasis and oxidative stress response.
Sequence Mass (Da): 50683
Sequence Length: 447
Subcellular Location: Cytoplasm
EC: 1.-.-.-
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Q2W8M7 | METTLGSYARTLSLGMLVPSAICLLAGTFGLLGGSSIALWVVIAVSLLGVVGGVKIGGSARRMAGDLSTAIHVLSRSASGDLNARILDVRGSGGIGALQHSINRLLDLAEAFGKEAFAAVESANHGRYYRRIITTGLRGDFVLYAKTINQALKRMEARDAEFIAFANNQVKPVVNAVAAAATELEASSGAMSAQSTDTSHQAMTVAAAAEQASVNVQAVASAVEEFSASIKEISTQVHRAAAVASEAAGVASRTDTTVHGLSDAAQRIGAIVSLINDIAAQTNLLALNATIEAARAGDAGKGFAVVANEVKNLANQTARATEDITSQVAHIQEVAAEAIKAIQEITRTVSQIEETSSAVAGAVEEQNAVTVEIARNVAEAATGTSSVSSAIITVQATAAEATESAGQVADAASELSRQSENLSREVDGFIARIGGR | Function: Probable methyl-accepting taxis protein. May be the receptor that senses the torque generated from the interaction between the magnetosome dipole moment and the external magnetic field (Probable). Overproduction interferes with magnetotaxis, cells respond more slowly to changes in the magnetic field; requires the MamK-interacting C-terminus of the protein. The effect of magnetic sensing is to control flagellar rotation .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44582
Sequence Length: 436
Domain: Only the C-terminus (residues 321-436) is necessary to interact with MamK; its addition to MCP25 confers the ability to interact with MamK.
Subcellular Location: Cell inner membrane
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P02942 | MLKRIKIVTSLLLVLAVFGLLQLTSGGLFFNALKNDKENFTVLQTIRQQQSTLNGSWVALLQTRNTLNRAGIRYMMDQNNIGSGSTVAELMESASISLKQAEKNWADYEALPRDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAGKINEFFDQPTQGYQDGFEKQYVAYMEQNDRLHDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQRETSAVVKTVTPAAPRKMAVADSEENWETF | Function: Receptor for the attractant L-serine and related amino acids. Is also responsible for chemotaxis away from a wide range of repellents, including leucine, indole, and weak acids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59443
Sequence Length: 551
Subcellular Location: Cell inner membrane
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Q9WYR0 | MSLRKKVFLLMIVVVAGLLLSFFLIYRSVSNSIINSVRSNTENQAKALSKFVVEKLNNVTNVARSAATYLGSQFFEAYMITNQLKTTVEKEKSTFAFAFSALSFNKSAALTDGNRVDRVDFADYEKYIKAVEGKDIFFMPETFQGTPVLTVVVPIETMNTRTGIVGFGINLSENSDLWKAVVEEGKASKSGYGLLVTSDGKVLIHKDMGNFMKDVKELGGFEKAFEEAKSGGEKYVEYEYNGEKKYTVWEKVPGYDFYIFSTGYLEELLAEGRKATLGTIVTYVVFGGVIFAVLFVSMMPVVKRMRQQVEKVKRFGEGDLTVEFEAKGRDELTQIEESLKEAALSLKEMIVSIIEAAKELSGASEEIKVLSEESHKMSENLHEEAKKILDEANNMSSALTEVTSGVEEVAASAQNISKITQDLTERSEAVTKAAREGTERVEAVGGVINKLKGSAERQRDYLRELVDSAKTIGEIVDTISSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEIRKLAEESQRATEDIAKMLSSLRTTIEHVENGSKEMFEGVDEIAVMGEEVTKRFREILGRIEEINSMIENTAATAQEQGAAAEEMASAMDNVTKIVEGVVESLNRMESLIEDQTTSAAKVSQAAERLSELSEQLSTLVQKFKV | Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72217
Sequence Length: 656
Subcellular Location: Cell membrane
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Q9HUB1 | MYDWWVLQLAKLSVSRKLMVGFGVLLALLLLVVISSNRTLTHQTALSEQLAEVASLMEQTQQAEQGRLAFEAGSDPRQAEQVRQTLAGMLQRLQALRDSELDPAALAHQVEAIEAYRKAFDDLAAADQQRSAARGVLVGTAQQALDSFARLEELMDASLAQQAGDPQALQRSRAVADLHQQLLMVRYQVRGYVFERSDKAEQAAFAAFDALRQAATTLRGQLPGEADAALEQAMGSLQGYRGGIEQFRAGVIRTRQAQQAMQSSTQDMARAGRTLTEAGRQLRESTASRDRASLWLIAALALAFGCVAGWAINRQIVRPLDEALAQAEAIAAGDLGKRPQNPLTLQRRDELGQLQRVMQRMGDSLRELVGRISDGVSQLASSAEELSAVTEQTRAGVNSQKVETDQVATAMHEMAATVQDVARNAELASQAARQADEEARQGDAVVDQAVTRIERLASEMDVSSEAMARLKNESEQIGSVLDVIKSVAEQTNLLALNAAIEAARAGDAGRGFAVVADEVRGLAQRTQQSTAEIEGLIQRLQQGAGEAAERLENSRSLTASTVELARRAGAALDSITRTVSDIQNMNLQIATAAEQQSTVAEEINRSVLSVRDVAEQSAAASEQTAASSGELARLGTQLQAQVGRFRL | Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. McpK is a chemoreceptor that specifically binds and mediates chemotaxis to alpha-ketoglutarate (alphaKG).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69701
Sequence Length: 647
Subcellular Location: Cell inner membrane
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Q9I055 | MNESVARVFDRILRGLGLKTLNAQFLLSYALMFGLAACASVALYLSMSISPETINVAGAQRMLSQKMAREALQLRLGAGDPKALAATIAQYERSAADLDAGNAERNVSRMGAPEIAAQRQKVAQIWGRYRAMLDQVAQPASQVDLRGFSQYSTELLGELNNLVSLMSARADSVQHTQMWIAFGCLLAILVLVVLGRQFGLAPLMRQLRGLEVALTEVGAANFTHALAAGHADNEIGRIVAGYERMRQDVSGLLANVKRSAAETDKDVAEALEQALGAGDQVARQHQDLDQVATAMNEMSATVAEVARHANHAAHSTRDAAALAHEGRRLVEHASSQTGALAEELEQTALALNTLHQHAGSVGQVLTVISSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRSLANRTQQSTQEIQGLIEQLQDGANDAVAAMRGSASHAQSNLVEADSAAQALGRIVATVEELDGLNQQIATAAEEQSQVAQDIDRNITNVSGLSEQAHEGTAAVLSANQRVKEHMAGLRVVLGRFRT | Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. McpN is a chemoreceptor that recognizes specifically nitrate and mediates chemoattraction. Binds nitrate specifically and shows no affinity for other ligands such as nitrite. McpN-mediated taxis occurs only under nitrate starvation conditions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56389
Sequence Length: 531
Domain: A single nitrate molecule is bound to a site on the dimer symmetry axis.
Subcellular Location: Cell inner membrane
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Q88IY8 | MNTLRSMSISRRLWLILVVAVAMLVVLGLLMLRQIHGDLYQAKAEKTRHVVQTAAGVLAYYQGLEAAGTLSREAAQQQALQVVRALRYDHDDYFWINDLGPKMIMHPANPKLDDQDLSAIRDPDGFAVFNEMVALARQQDAGPVNYRWPKPGASEPVAKTSYIQLFKPWGWIIGSGVYVDDVQAEFARQLRDASLVGVGIALLMALVVMLIARSIARPLQEAVQAMGNIASGESDLTRRLDTHGSDEITHLGEHFNRFNGKLQGVVGQLQGAAHALAQSAGHVGDNAGAAQQRSAQQSLQMDQVATAVNEVTYAVQDVAKTAEQAAGEMRTAQQQVTHGQQAIHGSLAQIDRLSLTIDEAVQVIRDLAGHSTRIGGVLDVIRSIAEQTNLLALNAAIEAARAGEQGRGFAVVADEVRLLAQRTAQSTAEIHTMIEHLQSQSDAAVKAIDTSSEASRQTVEQAREAGASLDAINQVLNNLTALNASIASATLQQSHVVEEINRNVLDTAGLSQQTADAARQSSDAGVALGRLSEELEQLLRQFRV | Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. McpP is a chemoreceptor that responds specifically to some C2 and C3 carboxylic acids. Recognizes acetate, pyruvate, propionate, and L-lactate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58659
Sequence Length: 544
Subcellular Location: Cell membrane
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Q88D09 | MYQWLAQSLGNVSVNRKLGLGFGLVLLLTLAITLTGWHGMDSIIDRGDKLGNISVIQQYTQELRIARQQYDRRRDDASLAELEKALSNLDRQVQLMLGQIEQPADHQRLEQQREAVRIYQQAFNELKQADQRREASRDVLGSSADKAVDLIGRVQRSLLQGANINQYQHAVDVSALLQQARFQVRGYTYSGNADYQQTALKAIDQALAELRALPAKVPAEHAASLDDAATAMGGYRDAVTQFGNAQLASEQALQRMVEQGTVLLQASQMMTASQTEVRDAAAAQAKTLLTVATVLALALGLLAAWAITRQIIIPLRQTLRAAERVASGDLTQSLQVQRRDELGQLQASMHRMTQGLRELIGGIGDGVTQIASAAEELSAVTEQTSAGVNNQKVETDQVATAMNQMTATVHEVARNAEQASEAALMADQQAREGDRVVGEAVAQIERLASEVVNSSEAMNLLKTESDKIGSVLDVIKSVAQQTNLLALNAAIEAARAGEAGRGFAVVADEVRSLAQRTQQSTEEIEELIAGLQSGTQRVASVMDNSRQLTDSSVELTRRAGSSLETITRTVSSIQAMNQQIATAAEEQTAVAEEINRSVMNVRDISDQTSAASEETASSSVELARLGTHLQGLVGRFRL | Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. McpQ recognizes specifically citrate and citrate/metal(2+) complexes. Binds citrate/metal(2+) complexes with higher affinity than free citrate, and mediates preferentially chemotaxis toward citrate/metal(2+) complexes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69017
Sequence Length: 638
Subcellular Location: Cell membrane
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P21822 | MFNRIKVVTSLLLVLVLFGALQLISGGLFFSSLKSDKENFTVLQTIRQQQLLLSESRVDLLQARNSLNRAGIRYMMDTNKIGSGATIDELLAKAKEELARAERNYTAYEKIPQDPRQDPQATEKLKQQYGILYGALSELIQLLGEGKINAFFDQPTQKYQDDFEQTYNAYLQQNGKLYQIAVDASNSSYSSAIWTLIVVIIVVLAAIVGVWMGIHHILVRPLNRMIEHIKRIASGDLTQPIPVTSRNEIGVLAASLKHMQNELIETVSGVRQGADAIYSGASEIAAGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASQLALSASETAQKGGKVVANVVETMHDIASSSQKIADITGVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAKEIKALIEDSVNRVDMGSVLVESAGDTMGDIVNAVTRVTDIMGEIASASDEQSRGIDQVGQAVAEMDRVTQQNASLVEESASAAAALEEQASLLTQSVAVFRLKSEGQEEYKAPVSNKTAPAAIATHKKTSASDYQDNWETF | Function: Receptor for the attractant L-serine and related amino acids.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60038
Sequence Length: 556
Subcellular Location: Cell inner membrane
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Q88E10 | MNSWFANISVNLKLGLGFGLVLVLTGLLALTGWTSLGSLIDRSNWMGDIGQLNKDLTDLRIARLQYMIANGDDTAAANTLAKLDAFSKQQAYLATTFKSPENVKLLGELGDTISAYKLSLNKMRQGYDATRAARVSMDSSAIRADQAMDALSQEVMARPEADSVRLAQYQLISKARQQLLQVRIDVRGYIAENSSANEQAALRQLDAALADTDNLKRQLPSEDARLQQFENAVLAYRDAVRQFRDAVANITTSRAEMTVQGADIVKRSDALYQIQLERRDIESTQARSLQAIATLLALLVGVLAAVLITRQITRPLQDTLVAVEKIASGDLTQHMRVTRRDELGVLQQGIARMGTTLRELISGIRDGVTQIASAAEELSAVTEQTSAGANSQKVETDQVATAMHEMAATVQEVARNAEQASHAATGADDEARAGDRVVGEAIGQIERLAEDMHRSTEAMNLLQQESQKIGSVMDVIKSVAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRGLAQRTQKSTEEIEELIASLQHGTQQVANAMQGSRALTDSSVELARKAGSSLESITSTVSSIQSMNQQIAAAAEQQSAVAEEISRSILNVRDVSEQTAAASDETAASSVELARLGGQLQTLVSQFRV | Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. McpS is a specific chemoreceptor for 6 tricarboxylic acid (TCA) cycle intermediates (succinate, fumarate, malate, oxaloacetate, citrate and isocitrate), butyrate and acetate. Malate, succinate, fumarate and oxaloacetate cause the strongest chemotactic response.
PTM: Methylated by CheR2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68764
Sequence Length: 639
Subcellular Location: Cell membrane
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Q0TML0 | MVQWISPLDNSIVIASKVKILRNIKGIKFTKLLNEEEFNDLLSMVLGRLKEIDILDKCYVVKLKDGEEKIIDYYKENFGLIKYFENKDNLIFIMNKNGEFNILLNEEEHIGIECTNSGLSLREVYSKVDNLDDLIEEKIHYSFDSELGYLTSNIKNLGTALRAKVFIHLPLLSSNNLIRIIKNALKEEGITLKSIYNSGNKDVGNIYEVSNIKTLGMSEKDILDSLISITNKLILREKNQRDNLSKDEYIELKDDILRSLGVLRNTYSIDRDEALKYLSYVRLGVELGIIEDLSLKSVNSAMIEIQPDMINNSSIKKRDIQSLKIERAKIIRNALNT | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 38686
Sequence Length: 337
EC: 2.7.14.1
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A4J0X5 | MSLKETVSNPYSKWLEATGPENDVIISSRVRLARNLMGYPFPHVLGHENADKVLYAVQSAVAQKSLQEAVGNLELSRMTELSSIERQILVEKHLISPDMLEQPEKRGVVLRDDEVISIMVNEEDHLRIQCLLPGLQLKECWDLANTVDDGLEQIIDYAFAKEQGYLTSCPTNIGTGLRASVMLHLPALVMTRQINAVLTTLSKLGLTVRGLYGEGTQATGNLFQVSNQVTLGLTEEEIIDNLITVALQLVTQERAARRALHKEQLHQIEDKVWRAYGLLKYARTMTSNETMTLLSDMRLGVDLGVITGIPPGIIMELIILSRPAFLSKVKGADLNPYQRDIFRATLIRERLNSLSNE | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 39884
Sequence Length: 357
EC: 2.7.14.1
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C4KZS5 | METFLTHPLGPKMKERAKLDDLVVSTRIRLARNVKDTVFSPVLSKEGERQLCDRLEGRLRGLKGFEYLHMRDYDEVTRQALMEKHLISPAVAANEESAVFLSEDETISVLINEEDHLRIQTLLPGYQVKEAFELANQVDALCAESLSYAFDEQLGYLTTCPSNIGTGLRASVMLHLPGLTLTGRISPILRELRKLGYTIRGRYGEGSDAAGRLFQLSNQRTLGSHESQLLADFMEVTEQVIQAERHAREELIAHRQEELEDRFYRSYGILRYAKLLSSTEAIERLSDLHLASDLGILSDWSPPKFHELIVRLQSGFLQKHFGKTLSTQERDRERATLVRRTLDQGLV | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 39508
Sequence Length: 347
EC: 2.7.14.1
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P0DMM5 | MSFGKFFNTAVSAWMSQEGPNSDIVLSSRIRLARNIVDFRFPTLFSSEEAKQIVALFERAFVHRPYGEAGRFELLKMSELQPIEKRVLVEKHLISPHLAEDSPFGACLLSENEEISIMINEEDHIRIQCLFPGLQLAEALEAASELDDWIEGHVNYAFDERLGYLTSCPTNVGTGLRASVMMHLPALVLTQQINRIIPAINQLGLVVRGTYGEGSEALGNIFQISNQITLGKSEEDIVADLHTIVEQLIAQERAARQALVKTLGIQLEDKVFRSYGILANCRVIDSKEAAQCLSDVRLGIDLGYIKNVSRNILNELMILTQPGFLQQYAGGVLRPEERDVRRAALIRERLRMETRRKMEGDER | Function: Catalyzes the specific phosphorylation of arginine residues in a large number of proteins. Is part of the bacterial stress response system, where it is involved in regulating the global heat shock repressor CtsR; phosphorylates arginine residues in the winged helix-turn-helix domain of CtsR, thereby preventing its binding to DNA and consequently inducing the expression of repressed genes. Protein arginine phosphorylation has a physiologically important role and is involved in the regulation of many critical cellular processes, such as protein homeostasis, motility, competence, and stringent and stress responses, by regulating gene expression and protein activity. Acts exclusively on Arg residues, since it cannot phosphorylate Tyr, Ser, Thr, His, Asp and Lys. Has no free arginine kinase activity.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 40853
Sequence Length: 363
Domain: In the 3D-structure the McsB dimer adopts a flat 'domino tile' shape, with the two active sites opening on the same side. Individual subunits are composed of the N-terminal catalytic, ATP:guanido phosphotransferase domain (PD, residues 1-263) and the C-terminal dimerization domain (DD, residues 264-355), which are linearly organized in a PD-DD-DD*-PD* manner (asterisk denotes the partner protomer). The PhK-like catalytic phosphotransferase domain is structurally adapted to target protein substrates. The C-terminal DD of McsB contains a pArg-binding pocket that allows pArg-carrying proteins to allosterically enhance McsB kinase activity.
EC: 2.7.14.1
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B8D093 | MSLKDLINKNLSHWVAGQGPERDIVLSSRIRLARNLDTIPYPNRADKDSKEEVTKRVLDATSKQGKIKLHYIKMDDLPEVEREVLVEKHLISPAHAKAGEGKGVLLNDNETISIMINEEDHLRLQVLIPGLQLEGAWETASELDDLLEEKLDFAFSQKWGYLSACPTNVGTGLRASVMVHLPALNLTNNINKMLGAISKVGLTVRGIYGEGSEYVGNLYQISNQVTLGHTEKEIIANLKSVTSQIIEQERQARNLLLKEKEIEVRDRVNRSFGILSHAYQISSEEALRMLSNVKLGIDMGIITDVDTGVLSELMVLIRPAHLQKLEGKELTPTERDIKRAELIKTRLNM | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 39109
Sequence Length: 349
EC: 2.7.14.1
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Q48759 | MNVFEPRLSSWLENAGDDDDVVLSSRIRLARNLKDEQFPIYEQKEEIVDNIAEVFDDNFILIKMNQISLLQKALLVEKHLISPYMMNKSEYGAVLLNEEENVSIMLNEEDHLRIQCMTPGLRLFDALEAALQIDGYVEEKLSYAFDKEFGYLTSCVTNIGTGMRASVMVHLPGLVTTKRIKSVIEAIRSLGFVVRGIYGEGSMPASNIFQVSNQVTLGKTEAEIVEDLTQVMEQIIMQERVARTTLKQKFHIALEDRVFRSYGLLMNCRIISMKEAADAISDIRFGVELGFFEHISRQKMNELVLFSQPAFLRREAGRDMDELEEKVIRAKVIREILGDK | Function: Catalyzes the specific phosphorylation of arginine residues in proteins.
Catalytic Activity: ATP + L-arginyl-[protein] = ADP + H(+) + N(omega)-phospho-L-arginyl-[protein]
Sequence Mass (Da): 38855
Sequence Length: 340
EC: 2.7.14.1
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Q89XN9 | MEDLSFRHPVRARADGARRSAIVGIVASGNLEVLVERVLPDAECAIDIKTAAVGFGEVWRAVIGDFVERYSPGGLKFSINDGGARPDTVSLRLAQAVRSIAENGQ | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence Mass (Da): 11207
Sequence Length: 105
Subcellular Location: Cytoplasm
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O32712 | MEQITLSFPASRALSGRALAGVVGSGDMEVLYTAAQSATLNVQITTSVDNSQARWQALFDRLNLINGLPAGQLIIHDFGATPGVARIRIEQVFEEAAHA | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence Mass (Da): 10537
Sequence Length: 99
Subcellular Location: Cytoplasm
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O06925 | MEGMLNELNFKFKSENPVDVVLPKHHYGVVGSGDLEVLLKKHELEGAVEIRVVSPVRGFDHVWEKVLEKVISDAEVGNVAIEINDNNATPVVVALRLAQALSEAKSAEQSVN | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence Mass (Da): 12256
Sequence Length: 112
Subcellular Location: Cytoplasm
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Q48PD1 | METLSFEFPAGQPPKGRALVGVVGSGDLEVLLEPGSPGKLSIQVVTSVNGASLRWKHLFERMFDGQTPPALSIDIHDFGATPGVVRLRLEQGFEEIGHD | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence Mass (Da): 10639
Sequence Length: 99
Subcellular Location: Cytoplasm
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A6UY05 | METLTFEFPAGAPARGRALAGCVGSGDLEVLLEPAAGGALSIEVVTSVNGSGPRWQQLFARVFAAATAPAAAIRIHDFGATPGVVRLRLEQALEEAGHD | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence Mass (Da): 10155
Sequence Length: 99
Subcellular Location: Cytoplasm
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Q87V56 | METLSFEFPAGQPPKGRALVGVVGSGDLEVLLEPGQPGKLSIQVVTSVNGASLRWKHLFERMFDGQTPPALSIDIHDFGATPGVVRLRLEQGFEEIGHD | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence Mass (Da): 10680
Sequence Length: 99
Subcellular Location: Cytoplasm
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B4SNX3 | METLDYRFDGTTHAHFPTNAVLVGVLASGNLEILLEPAALDGAMTVRIITAAQGFGSVWQAVITDFARRHPLRDVRISINDAGATPAVVSLRLDQAVETLLGGGTP | Function: Subunit of malonate decarboxylase, it is an acyl carrier protein to which acetyl and malonyl thioester residues are bound via a 2'-(5''-phosphoribosyl)-3'-dephospho-CoA prosthetic group and turn over during the catalytic mechanism.
PTM: Covalently binds the prosthetic group of malonate decarboxylase.
Sequence Mass (Da): 11211
Sequence Length: 106
Subcellular Location: Cytoplasm
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Q5HM62 | MKFLKNKSYHLLVTLIVLTIFVISGAIFLTFLGFGLYGLSRILIYLHLGDFSYNKGFYDNLIYYGSYIVLGYFTLFSIEHLMDYFKKNLPKNPYFQGINFHLISYIVTTIMFYFIVHIHYVHVNIHFWVIMIIIGFLFVCKEVFYPESKNLNNKK | Function: Involved in multidrug efflux.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18447
Sequence Length: 155
Subcellular Location: Cell membrane
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P17505 | MLSRVAKRAFSSTVANPYKVTVLGAGGGIGQPLSLLLKLNHKVTDLRLYDLKGAKGVATDLSHIPTNSVVKGFTPEEPDGLNNALKDTDMVLIPAGVPRKPGMTRDDLFAINASIVRDLAAATAESAPNAAILVISNPVNSTVPIVAQVLKNKGVYNPKKLFGVTTLDSIRAARFISEVENTDPTQERVNVIGGHSGITIIPLISQTNHKLMSDDKRHELIHRIQFGGDEVVKAKNGAGSATLSMAHAGAKFANAVLSGFKGERDVIEPSFVDSPLFKSEGIEFFASPVTLGPDGIEKIHPIGELSSEEEEMLQKCKETLKKNIEKGVNFVASK | Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 35650
Sequence Length: 334
Subcellular Location: Mitochondrion matrix
EC: 1.1.1.37
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Q8H1E2 | MAMAELSTPKTTSPFLNSSSRLRLSSKLHLSNHFRHLLLPPLHTTTPNSKISCSVSQNSQAPVAVQENGLVKTKKECYGVFCLTYDLKAEEETRSWKKLINIAVSGAAGMISNHLLFKLASGEVFGPDQPIALKLLGSERSIQALEGVAMELEDSLFPLLREVDIGTDPNEVFQDVEWAILIGAKPRGPGMERADLLDINGQIFAEQGKALNKAASPNVKVLVVGNPCNTNALICLKNAPNIPAKNFHALTRLDENRAKCQLALKAGVFYDKVSNMTIWGNHSTTQVPDFLNARINGLPVKEVITDHKWLEEGFTESVQKRGGLLIQKWGRSSAASTAVSIVDAIKSLVTPTPEGDWFSTGVYTDGNPYGIEEGLVFSMPCRSKGDGDYELVKDVEIDDYLRQRIAKSEAELLAEKRCVAHLTGEGIAYCDLGPVDTMLPGEV | Function: The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells (Probable). Plays an essential role in the regulation of catalase activity and the accumulation of a hydrogen peroxide-dependent signal by transmitting the redox state of the chloroplast to other cell compartments .
Catalytic Activity: (S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate
Sequence Mass (Da): 48316
Sequence Length: 443
Subcellular Location: Plastid
EC: 1.1.1.82
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Q9SN86 | MATATSASLFSTVSSSYSKASSIPHSRLQSVKFNSVPSFTGLKSTSLISGSDSSSLAKTLRGSVTKAQTSDKKPYGFKINASYKVAVLGAAGGIGQPLSLLIKMSPLVSTLHLYDIANVKGVAADLSHCNTPSQVRDFTGPSELADCLKDVNVVVIPAGVPRKPGMTRDDLFNINANIVKTLVEAVAENCPNAFIHIISNPVNSTVPIAAEVLKKKGVYDPKKLFGVTTLDVVRANTFVSQKKNLKLIDVDVPVIGGHAGITILPLLSKTKPSVNFTDEEIQELTVRIQNAGTEVVDAKAGAGSATLSMAYAAARFVESSLRALDGDGDVYECSFVESTLTDLPFFASRVKIGKNGLEAVIESDLQGLTEYEQKALEALKVELKASIDKGVAFANKPAAAAAN | Function: Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments (Probable). Plays a key role in the metabolism of dark chloroplasts and non-green plastids. Essential for embryo viability . Plays an essential role in heterotrophic metabolism in embryos, and autotrophic metabolism in photosynthetic tissues as well .
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 42406
Sequence Length: 403
Subcellular Location: Plastid
EC: 1.1.1.37
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P46489 | MAVVKLSPWANYSSSKSEIKSSSSSSSSKSSLSAYVINVSSSPRLSFYNPYPRRLHHQRLSSPASIRCSVTSSDQIQAPLPAKQKPECFGVFCLTYDLKAEEETKSWKKIINVAVSGAAGMISNHLLFKLASGEVFGPDQPISLKLLGSERSFAALEGVAMELEDSLYPLLRQVSIGIDPYEIFQDAEWALLIGAKPRGPGMERADLLDINGQIFAEQGKALNAVASPNVKVMVVGNPCNTNALICLKNAPNIPPKNFHALTRLDENRAKCQLALKAGVFYDKVSNVTIWGNHSTTQVPDFLNAKIHGIPVTEVIRDRKWLEDEFTNMVQTRGGVLIKKWGRSSAASTAVSIVDAIRSLVTPTPEGDWFSTGVYTNGNPYGIAEDIVFSMPCRSKGDGDYEFVKDVIFDDYLSKKIKKSEDELLAEKKCVAHLTGEGIAVCDLPEDTMLPGEM | Function: The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells.
Catalytic Activity: (S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate
Sequence Mass (Da): 49515
Sequence Length: 453
Subcellular Location: Plastid
EC: 1.1.1.82
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P15719 | MGLSTVYSPAGPRLVPAPLGRCRSAQPRRPRRAPLATVRCSVDATKQAQDGVATAVATEAPASRKECFGVFCTTYDLKAEDKTKSWRKLVNVAVSGAAGMISNHLLFKLASGEVFGQDQPIALKLLGSERSFQALEGVAMELEDSLYPLLREVSIGIDPYVVFQDVDWALLIGAKPRGPGMERAALLDINGQIFADQGKALNAVASRNDEVLVVGNPCNTNALICLKNAPNIPAKNFHALTRLDENRAKCQLALKAGVFYDKVSNVTIWGNHSTTQVPDFLNAKIDGRPVKEVIKDTKWLEEEFTLTVQKRGGVLIQKWGRSSAASTAVSIVDAIRSLVTPTPEGDWFSTGVYTTGNPYGIAEDIVFSMPCRSKGDGDYELASDVLMDDFLWERIKKSEAELLAEKKCVAHLTGEGNAFCDLPEDTMLPGEV | Function: The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells.
Catalytic Activity: (S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate
Sequence Mass (Da): 46860
Sequence Length: 432
Subcellular Location: Plastid
EC: 1.1.1.82
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O48902 | MALTQLNNTCSKTQLHSSSQLSFLSRTLPRHHHCTLAPLHRTQHARISCSVAPNQVQAPAVQTQDPKSKPDCYGVFCLTYDLKAEEETKSWKKLITIAVSGAAGMISNHLLFKLASGEVFGPNQPIALKLLGSERSLQALEGVAMELEDSLFPLLREVVISIDPYEVFQDAEWALLIGAKPRGPGMERAALLDINGQIFAEQGKALNAVASRNVKVIVVGNPCNTNALICLKNAPNIPAKNFHALTRLDENRAKCQLALKAGVFYDKVSNMTIWGNHSTTQVPDFLNARIDGLPVKEVIKDHKWLEEEFTEKVQKRGGALIQKWGRSSAASTSVSIVDAIRSLIIPTPEGDWFSTGVYTTGNPYGIAEDIVFSMPCRSKGDGDYELVKDVIFDDYLRQKLAKTEAELLAEKKCVAHLTGEGIAVCDLPGDTMLPGEM | Function: The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells (By similarity).
Catalytic Activity: (S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate
Sequence Mass (Da): 47835
Sequence Length: 437
Subcellular Location: Plastid
EC: 1.1.1.82
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P32419 | MVKVAILGASGGVGQPLSLLLKLSPYVSELALYDIRAAEGIGKDLSHINTNSSCVGYDKDSIENTLSNAQVVLIPAGVPRKPGLTRDDLFKMNAGIVKSLVTAVGKFAPNARILVISNPVNSLVPIAVETLKKMGKFKPGNVMGVTNLDLVRAETFLVDYLMLKNPKIGQEQDKTTMHRKVTVIGGHSGETIIPIITDKSLVFQLDKQYEHFIHRVQFGGDEIVKAKQGAGSATLSMAFAGAKFAEEVLRSFHNEKPETESLSAFVYLPGLKNGKKAQQLVGDNSIEYFSLPIVLRNGSVVSIDTSVLEKLSPREEQLVNTAVKELRKNIEKGKSFILDSSKL | Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 37186
Sequence Length: 343
Subcellular Location: Peroxisome
EC: 1.1.1.37
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O82399 | MDPNQRIARISAHLNPPNLHNQIADGSGLNRVACRAKGGSPGFKVAILGAAGGIGQPLAMLMKMNPLVSVLHLYDVANAPGVTADISHMDTSAVVRGFLGQPQLEEALTGMDLVIIPAGVPRKPGMTRDDLFNINAGIVRTLSEAIAKCCPKAIVNIISNPVNSTVPIAAEVFKKAGTFDPKKLMGVTMLDVVRANTFVAEVMSLDPREVEVPVVGGHAGVTILPLLSQVKPPCSFTQKEIEYLTDRIQNGGTEVVEAKAGAGSATLSMAYAAVEFADACLRGLRGDANIVECAYVASHVTELPFFASKVRLGRCGIDEVYGLGPLNEYERMGLEKAKKELSVSIHKGVTFAKK | Function: Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments (Probable). Peroxisomal NAD-dependent malate dehydrogenase involved in fatty acid beta-oxidation. Reoxidizes NADH from the beta-oxidation and provides NAD for the conversion of fatty acyl-CoA to acetyl-CoA. Does not participate directly in the glyoxylate cycle . Required for maintenance of photosynthetic rates under photorespiratory conditions, and carbon flow during photorespiration. Supplies NADH reductant to the peroxisomal hydroxypyruvate reductase (HPR), which reduces hydroxypyruvate into glycerate in the photorespiratory cycle .
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 37466
Sequence Length: 354
Subcellular Location: Peroxisome
EC: 1.1.1.37
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Q9ZP05 | MEFRGDANQRIARISAHLTPQMEAKNSVIGRENCRAKGGNPGFKVAILGAAGGIGQSLSLLMKMNPLVSLLHLYDVVNAPGVTADVSHMDTGAVVRGFLGAKQLEDALTGMDLVIIPAGIPRKPGMTRDDLFKINAGIVKTLCEGVAKCCPNAIVNLISNPVNSTVPIAAEVFKKAGTYDPKKLLGVTTLDVARANTFVAEVLGLDPREVDVPVVGGHAGVTILPLLSQVKPPSSFTPQEIEYLTNRIQNGGTEVVEAKAGAGSATLSMAYAAAKFADACLRGLRGDANVVECSFVASQVTELAFFATKVRLGRTGAEEVYQLGPLNEYERIGLEKAKDELAGSIQKGVEFIRK | Function: Catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis between organelle compartments (Probable). Peroxisomal NAD-dependent malate dehydrogenase involved in fatty acid beta-oxidation. Reoxidizes NADH from the beta-oxidation and provides NAD for the conversion of fatty acyl-CoA to acetyl-CoA. Does not participate directly in the glyoxylate cycle . Required for maintenance of photosynthetic rates under photorespiratory conditions, and carbon flow during photorespiration. Supplies NADH reductant to the peroxisomal hydroxypyruvate reductase (HPR), which reduces hydroxypyruvate into glycerate in the photorespiratory cycle .
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 37369
Sequence Length: 354
Subcellular Location: Peroxisome
EC: 1.1.1.37
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A0L5T9 | MADPIRVAVTGAAGQIAYSLLVRLASGQLFGKDRKVELKLLEIPQAMGPLEGVMMELQDCAFPTLAKVEAFDNPEQAFDGINWCLMVGSRPRGPGMERSDLIKINGPIFVNQGKALNRAAQDVRAVVVGNPCNTNCMIAAHNSDVPHERFSAMMRLDQNRAKYLLASKAGAQVIDVTNVVIWGNHSNNQVPDFEFAKIGGKPVPEVIADAAWLENAFMPTVQNRGAAVIKARGASSAASAANAALDHVRSLITPTPAGDTFCAAVMANGAYGVDAGLIAGMPLTSTGHGDWSIVEGVPMSPFIKGKFDAVLDELRREREMVKDLLPG | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 34833
Sequence Length: 327
EC: 1.1.1.37
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P16142 | MIISPEEERSLIIKILNALGVSEEHAKITADVIVDADLKGFTSHGIGRFPQYVEGIKLGTIKTSGNIEIEKETDSVALINGNHLLGQVVAYKGMKLAIEKAKNTGVGIVGIHDSNHFGIAGYYSDMAMKNDMIGITMTNTEPAVAPLGGKIPVLGTNPIAISIPSNEYYVAVDMSTAAVARGKLLEAARKNEKIPEGIAVDKNGNPTTDPNEALNGSILPFGGHKGYALCFMIEILAGPLVKAEFGSKVKGTVDPSQMCTKGDLLIAIDPSKFYDIEEFKRNVDEFVKEIKSTGKDVLIPGDRERMNIKKREKEGIELDKKLVEKLKEIADELNIELTW | Function: Acts on oxaloacetate, sulfopyruvate but not on pyruvate. Has a higher selectivity for the coenzyme NADH than for NADPH.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 36762
Sequence Length: 339
Subcellular Location: Cytoplasm
EC: 1.1.1.310
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Q60176 | MKVTIIGASGRVGSATALLLAKEPFMKDLVLIGREHSINKLEGLREDIYDALAGTRSDANIYVESDENLRIIDESDVVIITSGVPRKEGMSRMDLAKTNAKIVGKYAKKIAEICDTKIFVITNPVDVMTYKALVDSKFERNQVFGLGTHLDSLRFKVAIAKFFGVHIDEVRTRIIGEHGDSMVPLLSATSIGGIPIQKFERFKELPIDEIIEDVKTKGEQIIRLKGGSEFGPAAAILNVVRCIVNNEKRLLTLSAYVDGEFDGIRDVCIGVPVKIGRDGIEEVVSIELDKDEIIAFRKSAEIIKKYCEEVKNL | Function: Catalyzes the reversible oxidation of (S)-malate and (S)-sulfolactate to oxaloacetate and sulfopyruvate, respectively. Can use both NADH and NADPH, although activity is higher with NADPH. Oxidation of (S)-sulfolactate is observed only in the presence of NADP(+). Can also oxidize tartrate. Cannot reduce pyruvate, nor alpha-ketoglutarate.
Catalytic Activity: a (2S)-2-hydroxycarboxylate + NAD(+) = a 2-oxocarboxylate + H(+) + NADH
Sequence Mass (Da): 34609
Sequence Length: 313
Subcellular Location: Cytoplasm
EC: 1.1.1.375
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Q8TWG5 | MSKVAVIGATGRVGSTAAARLALLDCVNEVTLIARPKSVDKLRGLRRDILDSLAAAQKDAEITIGCERDDYVDADVIVMTAGIPRKPGQTRLDLTKDNAAIIKKYLEGVAEENPEAIVLVVTNPVDVLTYVALKVSGLPKNRVIGLGTHLDSMRFKVLIAKHFNVHMSEVHTRIIGEHGDTMVPVISSTSVGGIPVTRMPGWEDFDVEEAVREVKEAGQRIIETWGGSQFGPAQAITNLVRTILQDERRVLTVSAYLDGEIDGIRDVCIGVPARLGREGVLEIVPIELEEDEMRAFRRSVKVVKEATREAMEAISER | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate
Sequence Mass (Da): 34609
Sequence Length: 317
EC: 1.1.1.299
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Q8PVJ7 | MVKISVIGAGNVGSTTVQRLAELEPGEIVMTDIVEGMPQGKALDLMQAGAINGYDTRITGTNDYADIANSDLVIITAGIARKPGMSREDLIKTNSKIIGDVAGNIAKYAPNSIVINVTNPLDIITYVAMKATGFDPEKVFGMSGVLDAGRFASFIAEELKCSKRDVEAMVIGGHGDLMVPLPQYTTVSGIPLPELLPEKTIDRLVERTVNGGAEIVELLKQGSAFYAPSAAIVRMAEAVIKDSRRVLPASAYLEGQYGQKGIYFGVPVKLGANGIEEILELKLEDSQCEILKKSSETIRKGISKLEI | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 32786
Sequence Length: 307
EC: 1.1.1.37
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Q55383 | MNILEYAPIACQSWQVTVVGAGNVGRTLAQRLVQQNVANVVLLDIVPGLPQGIALDLMAAQSVEEYDSKIIGTNEYEATAGSDVVVITAGLPRRPGMSRDDLLGKNANIVAQGAREALRYSPNAILIVVTNPLDVMTYLAWKVTGLPSQRVMGMAGVLDSARLKAFIAMKLGACPSDINTLVLGGHGDLMLPLPRYCTVSGVPITELIPPQTIEELVERTRNGGAEIAALLQTGTAYYAPASSAAVMVESILRNQSRILPAATYLDGAYGLKDIFLGVPCRLGCRGVEDILEVQLTPEEKAALHLSAEAVRLNIDVALAMVSDG | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 34346
Sequence Length: 324
EC: 1.1.1.37
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P33163 | MSILPLVHAMANVRGDIEYLTEA | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 2544
Sequence Length: 23
EC: 1.1.1.37
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P61977 | MKAPVRVAVTGAAGQIGYSLLFRIAAGEMLGKDQPVILQLLEIPQAMKALEGVVMELEDCAFPLLAGLEATDDPKVAFKDADYALLVGAAPRKAGMERRDLLQVNGKIFTEQGRALAEVAKKDVKVLVVGNPANTNALIAYKNAPGLNPRNFTAMTRLDHNRAKAQLAKKTGTGVDRIRRMTVWGNHSSTMFPDLFHAEVDGRPALELVDMEWYEKVFIPTVAQRGAAIIQARGASSAASAANAAIEHIRDWALGTPEGDWVSMAVPSQGEYGIPEGIVYSFPVTAKDGAYRVVEGLEINEFARKRMEITAQELLDEMEQVKALGLI | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 35426
Sequence Length: 327
EC: 1.1.1.37
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A0A0S3QTC6 | MGKRAKITVVGAGHVGEHVAMFCAIKELGDVVLIDIVEDMPQGKALDMFEATPLEGWDSRIVGTNDYADTADSDIVVITAGSPRKPGMSRDDLLEINAKIIKAVTEQVAKYSPNAVIIVVTNPLDAMTQLAWNVSGFPKNRVLGQAGNLDSARFRAFIAMELGVSVKEISAMVLGGHGDDMVPLPRFTTVSGIPITELIPPDRIEALVQRTRVGGGEIVKLLKTGSAYYAPALATVEMVEAILKDQKRIQPCAALCEGEYGINGVYCGVPCLLGANGVEKIIELKLTDDELKALQASAGRVKGLIDKLTEWGYIK | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 33717
Sequence Length: 315
EC: 1.1.1.37
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Q8J0L4 | MLDFMDYIQLAFAEGTQRNCDNSYSSLTATTQNLLDFTTPERVRIHLSSLSTPNFATSYTLGTVGLIEGSISYLYSNISFDNTPSKSALIPLRKLAPGYRQVQAPIAPPSSKGQKATLLHATLHLPPPTTLNALFLRRISPTMQLSLAVSSTRGPPLSKSAPQATLLTQLTHDTGKYSNEYLFSTDNSLFGWRGLWNFGPDPRFNNNAQRLSLLSAGAEAYYSPVSSLIGMSTGLRFCTLPAATSSTPNPNTPISTFPYTLTLTLTPLTGSLSTSYSVRASPNLSFSSRFGFNVYSWESEMVAGFELWRQSRKAAIVDNDGLEWARNKARIWDIPASSQVPEPITPSEEETQESVLKVRVDQSWNVRLLWEGRVKELLVSAGVGLGPSSFSPSSYANSQATAGAQGSSGGPPTSYWRGVGVSVSYSS | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the tom40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of tom40 with the receptor tom22 and small TOM proteins. Can associate with the SAM(core) complex as well as the mdm12-mmm1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the tom40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46345
Sequence Length: 427
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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C4QWJ4 | MLEYMEYLEQCFAKNSQWDYNNLYEHVLDSSASILQFKIPHGFKFSVSSSSSPYNYNSISFENRGKGRLNGSLAYFYTTQELSNYKTSKNIPLQDVIDSYRLVNIPKNDRSYTDNEESKRPWLLYGRMYLPSQSMEAMAIKRLTANTQLMLKGVNILNPTPTPFNNKLTSLSFYLQSNYYKWSREAIFLSSDALFGLRFLYNFGNSTNPQCTPSIDSNNISTLSLGTELWYGAMNMTPGLSTTLRYTSFSVTGNPLTFTLACNPILGSVSTTYSIKTNVFTTLCSKFDFNFYSYESDLTIGCDLWRFGNNEDVPDSNPTPLPSKERELFIPLHDHQLVFPEQEKAKTISNEPKDYESDLLLKFLEIQGIKTARQSVATINNFTQKIKNAPFTSALKLNTSLKNHTVNLMWEGKYNDFLLSTGCSLNLDLKRPNVDGFGLQIQYSS | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50755
Sequence Length: 445
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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B0DK33 | MHPFASYVLRSYYKATGWNEDNLYANLTRSSNAILDFTVPRGLHLTVSKSPNALFKTTYSMTAMPSLHGSVGYIFTSCDLDVKSSGNVRFKNMIERFKVYDQPRRPEPKEEEWLAGEQVQKRDYLLYGRFYLPTGRLDALYSTRLSPTVQALVAAISDPPSNIPSELRDRNGDPSNIMLNLQHDVGKWCTEYTWSAEDGMWGVRVLHNFGRLGMSDAVEDGGGGKGDRTVKVKRVDEEDAVEGGLKGRVSMGAELYFSAKERSAGVSTGIRFTTLPDATPPSFQVPSSSSSSSNPVSPSTSQPPTTITALFNPMLGHMSGAYTARVSRDLALSSRFDFNVYSYESEWTMGAEWWLRRSLTPRPSEDGEIHPPTPPPFPPPVEDVQGVVKARASTNNDVSLMWEGRLRNMLVSLGVVSDFSSRSKPIKAIGLEVSYFSSE | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48646
Sequence Length: 439
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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Q7SBE0 | MREFMNYITNAFYGATGWNEDNKYNELNATSRELIDFPLPRGLRLTLSSLATPHFATSYQLGSVGVVDGSISYLHSSIPLTHIAAQSDKIPLPALLRCYRRLHDLRSPGQQHYILDADPLSGLPPPPQSARALLGAASDAAVAGGALDGGNTDQDLGIYTHSLLYGRLYLPKSLLEGMIIKRFTQALQVQVRAVSEQSLRNGGTILGLVQYDKGKYGLEGLYSTDGGLLGFRGLYNFGGDASSSTCDPWTPTPGENNNNNNNNNNNNNGNAQAGEKERIYGRFSVGGELYYGTLNKSGGMSLGARFATLPAHRGTPLTATLTINPLMGNINATYALLAREYCSLATRVDFNVYSYESEWAVGMELWSNRRPAGFLLGASPSNDFEPEPHPPRKKERSFQAKMEWRLDDPEPEPEPQPTPKTRKNDEYKGVLKARLDNNLRMGLLWEGRAKSLIFSIGTGIDLHKLGEPFRSLGLEVQYSS | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the tom40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of tom40 with the receptor tom22 and small TOM proteins. Can associate with the SAM(core) complex as well as the mdm12-mmm-1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the tom40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52714
Sequence Length: 480
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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Q0TWV0 | MLDFMDNVQHAFYEASHWNVDNSYGALNATARALLDFDSPRGLRLQISSLAAPNFATSYTLGSVGVVDGSVSYLYSSLPLRKDFKSSRIDLHHVIRGFKHLQELRKPDEKWSWEQWHAGRRVDRKDTLLYGRIFLPQSRLEALYLRRLAPTRQLRIAAVSDSNLNNGGTILTLLQTDSGKYSTEYMYSTDSALMGLRGLYNFGPDPRVAPTEPTRPEQVEPVHGRFSAGAELYYGILNKSGGMSTGLRFTTLPNHPGFPYTMTLTLNPLMGNLSSTYAVKAGPSLALCSRFDFNFYSYESELQLGCELWRRRGNTDTEWAVKKLRPDWKRPAASPDDDVAGVLKAKVDQDGRVGLLWEGRIKELLFTLGASLDLKKREQIFRSVGIELQYSS | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44179
Sequence Length: 392
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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A5DCL4 | MYTYMEYLQKCFFHATRWNEDNIYSNITASSHALLEFLVPSGLKMDVSSRSSPNSASSFTLSNHHSLNGSLAYMYSSTQLKGTPGTRRIPLQDAIAGFKIVEPNEMRPSASGTIAPSSLLYGRMYFPGAALEAMVIRRFSPHTQLLIKCIHNPQLDKNGTLIAYFQKNTQRYSREVIYSTNDALVGFRGLYNIGSTPSWSPSPPNFDRSVVSVGAELWYAARTMSPGLSTGLRYSTRSTSTGKPLTMTLACNPILGHISSTYTVKTSVASTFCSRYDFNLFSYASNLSLGFELFNFDKNAAVERNPQLPTPTTNPSASKQNLINPIRDHSYYQTTPSTNATTYQSSQTISDSFQKLVNRSEFSSVVKVSTSLNDRLVRLLWEGRFKDFLVSSGVKVSLNPATNAVELNRFGISFSYAS | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46383
Sequence Length: 418
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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O13498 | MREFMQYVRNAFYGATGWSEDNSYKDLNVTARELIDFPLPRGIRLSLSSLATPHFATSYQLCNVGVVDGSISYLHSSVPLAAVPAQSNKIPLGALMRSYRGLHQLGSRGGTPWSWETGPQIGTIPQVPAVADMGQIPNKDKSSLLYGRLYLPQSLLEAMVIKRFSPALQVQISAVSEQSLRNGGTMLSVVQYDRGKYGVEGLYSTDGGLLGLRGLYNFGGDASVAVMSSQNGTGSPESTEKERIYGRFSAGGEMYYGTLNKSGGMSLGARFATLPTHKGTPLTATLTINPLMGNINTTYAVLAKDFLAMATRMEFNAYSYESDWAVGLELWSNRRPAGFLLGAEPSLDLESDQPELPSKKERSFQAKMEWRLDDPEPEPEPVKIAEKPTEGKEEYLGVFKARLSSNLDLGLVWEGRAKSLIFSLGTGVDLQRLGEPFRSLGLEVQYSS | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48963
Sequence Length: 448
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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B8P366 | MHPFASYVLRSYYRGTGWNEDNLYANLTRSSNAILDFSVPRGLHFSISKSPNPLFKTTYSMNALPSLNGSIGYIFTSCELDVKGSGDVRFKDMVDRFRVYDQPRRPEGKEEEWLAGERVDTRDYLLYGRVYIPTGRLDALYSTRLSPTLQAMVAAISDPRSSLFAESPRGIAAPSSNIMFSLQHDTGKWCTEYTWSAEDGMWGVRCLHNFGKVGGPSEPVEDSEKSTAAPTKTRSGVKRIDEEDAMEGGLKGRISAGAEFYFSAKEKSAGVSTGIRFTTLPDATPPSFQLPSSSPTQPSLLAHGAPSQPPTTITALFNPMLGHMSGAYSARVSRDLSMSSRFDFNVYSYESEWSIGAEWWTRRGRGMFTSNPPAADTSEKTPSSPPALEAVGDVTGVVKARASTTTDFSLMWEGRLHNMLVSLGIVSNLTSRSKPIKAIGLELSYFSSG | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the TOM40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of TOM40 with the receptor TOM22 and small TOM proteins. Can associate with the SAM(core) complex as well as the MDM12-MMM1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the TOM40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49240
Sequence Length: 449
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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B6K463 | MNSFTRALFDEYLRKTGWNRGNLYTNLTQSADEVLNLEIPSGINCDLSSIPSPNFASNWEIQMLPILNGSVSYLYSNVDLRLPQNVFGHFAQHQQKFQHLLPPYRHLKTELTDMGFERKPYLMFGKLHLPTAKLEAIFAKRISPPNNLIIRMCHTKRGILTSTSTLLHWQRDTGRSCTEILYSTDEAMIGFRKLWNSGRLQPSLFESANLTKFDPFWSVGAEVYYGALTKCVGASIGARLYSCANGVHNPYSVTCTLNPIVGHLVSTFATSHNDTRVLCSQFEFNLYSYESRLRLGMELFQRKRLLTNEDNHSDDIRQQGNDGVLRLSVSTDGDLVVAWNGQLRDFLYTVGTKVHMLSINPVFFGIHFQYSH | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the tom40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of tom40 with the receptor tom22 and small TOM proteins. Can associate with the SAM(core) complex as well as the mdm12-mmm1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the tom40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42407
Sequence Length: 372
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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O13814 | MMSFNDYIFYEYLKKTNWNIHNLYCNLTQTADNILNFEIPSGVSCQLSSLTSSNFASGCKISAMPILNGSMSYVYTNVNLENLNRNITYNLQHFYEGYKHVDVPFVHYVNEFQDKKLPLRPTLLYGRMHLPSQHLDAIFATRLSPWLLFFIQGVNEIEDGVGDNLCFNWQYDTGKRCLEFVYESSGAMLGVRGLWNLNYRELNTKINMENKAPSNMRWSLGFETYYGVLTKCAGASLGMRLHSGPSHPYAPFILTCTLNPIVGHITSTFSTAEPRTKAFSAQYDFNIYSYESQLKLGIELWRSKQEMSQSTNDPTANSMSSLLKGTCSTSGDVSISWQARIRNFLLTIGTEAQLTKIDPLFFGVHFEYSK | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the tom40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of tom40 with the receptor tom22 and small TOM proteins. Can associate with the SAM(core) complex as well as the mdm12-mmm1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the tom40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42199
Sequence Length: 370
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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A7TES0 | MSFKFNEESFLDNSFNETLREKLTKMLNSRKSMDIKIDDHLSYANNRGSTSCSNNFDNSSSIKARDSKLDILKSDVKVCEVNFPTIPNLEILDLDVSGQPRALAKGICKISCRDALLQIQTEIEANSLLLYTNISPDFTTPLMIANDTFTIPITMTFSQIQLEAITNVFVKNSGVGISFNDVSLDFQFDCSIKLLQPHIAKRLRKSMQLVFKDVLPSALFNMSRSWFTHDGSSSQTTTDHSQEEGSRLIRLHRLTVEDLDLQDLSPVNMLKLSTLTSSRQTLSLHSTMPKYFSTIPGCLDRQNFRNFTSRMPCLSNYGGGSDDGDKHVPHIHNLQNKNLLPEEALEENDIDLKAILSIQTKIYERGISTNNDVIRPRRRKIRIKRAKKSIVNKATETSSNLNADSEITPVSSSHNATSSVNTITSLTTSSLGSTAGSSNSKNTNRSSSFTSSIMPITPLAQSSMNKKDGNLITLRQDSKVLDSMKYFTKIQDLHNIHASFNSSRETQDSNNRFRIASEMLPTKREISPIPTLNSFIEPNRRFSFVGLNHKTSHDNSWSVDEQPPPYY | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63691
Sequence Length: 567
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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Q6C7W0 | MSFKFDWESLRDESFYERAKTILADALNSDSKPPIIVDDITVKDLDLGDESPFLEILEIGDMADDRFRGIFKLNYTGNASLTLTTKVQANPLNVYRQSFDQSSFVAPQFLAAGSSLAIPLNLTLSDIRLSGIIILVFSRAKGLTLVFRNDPLESIKVSSTFDAIPPLAKFLQVQIENQIRGLFRELLPGIIHRLSQKWVTRDETKSNSNTVMSPHVTQPPSPKLKPVSIMDINPDLPALSPTNMLKISALCASQRTLSLFTPSISDAVYRSNLEQFDVVDEESQFQSEDPYDIVRIQSRNYYRHNHQAPKRRTIKYKRKSKKTDEGDNASTEVTTRETTPLPTSSTPLETSTPSREVIREVKEKLLAEPSSVVMSPSEEKTTLRSIPPPLELSPPSLDLSIDTSLRPYASRNNTPEKKEKPQRPAGPSKRNTLPAPTKKGPGFFSSNLAGYDVPPPAYSG | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51281
Sequence Length: 460
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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A6ZTX2 | MSFRFNEAVFGDNSFNERIREKLSTALNSPSKKKLDILKSGIKVQKVDFPTIPQLEILDLDIITQPKSLAKGICKISCKDAMLRIQTVIESNLLLINEQDTPSFTMPQLINNGSFTIPITMTFSSIELEAITNIFVKNPGIGISFNDVDLDFKFDCSVKILQSTIERRLKESMHVVFKDVLPSLIFNTSQNWFTNRGESTSTIPGKREHHHQQTTMSRNVILDGSDFQELSPINMLRLSSIVSSRSTLSLHSTVMNSLSAIPGCLERQNLYRFISRMPSLNNYYSSQSFPQPKSSTVSSKQLVKPFYCSHNLLPKTVLDSSQYDLATITKIQSRLFDRSNSNDDNAKPRRRKIKCKKTRTPSNLQSQGEQAVDDSTAIETVTSTPVQTPIPELEEQSPPYLKTTVSIRDKYVIPEKISLNLDSKKDTSKKKPFYFIGLNSQEPSNNWKWGMEDSPPPYH | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
PTM: Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex containing the F-box protein MDM30. Ubiquitination is important for mitochondrial integrity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51990
Sequence Length: 459
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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C5E4T8 | MSFRFNSQAFEDNSFNEKIREKLTQALNSSSSDSRSPKVTKTTMGEGSTSKKDSGSGGKSRKFDILKSGITVSKVNFPTTPQLEILDLDISAQPRSLVKGICKISCKDAMLQIQTEVEANLLLVYSECSPSFATPNMICNDSFTIPITMVFSEIRLEAITNIFVKHSGIGISFNDVNLDFKFDCSMKILQSTIERRLKNSMHHLFKEVLPSVIFSMSQSLFLSEAARNQEMHNESRGDSRPSPRVVLEESDLQELSPANMLRLSTLISSRQTLSLHGTVLNVPSTIPGCLERQNLHRFNSRIPSLSNYYASYKEEEKSRQVEVKKSVGSSVPLPHTSFAANPNLLPVRTLQEGAYDLPTITGIQNRIFERSTDENERPRRRKLKIKMSGRKQQPQAPKEEEPKQAEQQPETEPQQQRLLPTPEIPSREQASTPVDIDPTVSTPDSPDTEITSPKPLSIRNPILSDVEKMDSEDASAKSFVAPLKLPVSITSKYFNYPADHISAQTPRRYSPQRINWEDALFNTSELSNLRTSLYSPIARGSLLNPTKERPDRGRILDNRRLSFVGLNFKGGKWGDDDDPPPYSG | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65471
Sequence Length: 584
Domain: Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin.
Subcellular Location: Mitochondrion outer membrane
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Q08179 | MLNFASRASCVTRRQASLYFVKNQGPRLIASTIPSCHWPLRAQGVQPNYPLSLRFYSTDKSKSVTKPVAPTSTDAPAKPKETLMVKVKHALKHYANGTKLLGYEIKVSTKLLIKFAQGYELSRRERNQLRRTMGDVFRLIPFSAFLIIPFAELFLPFALKLFPNLLPSTYESGKDKQAKRNKLIEIRKKTSEFLHETLEESNLITYNTIENAEKKQKFLNFFRKLYSAKEGKIMTFQHDEISAIAQMFKNDSVLDNLSRPQLAAMSKFMSLRPFGNDNMLRYQIRSKLKDIMNDDKTIDYEGVESLSQEELYQACVSRGMKAYGVSKEDLVDNLKVWLELRLRQKIPSVLMVLSSTFTFGGLPKENYSKAFSPLAEKKETKSKYDDLLDLYYDGILQVLSSIPDPVYNVAKLDVSESKSSAAETEAEKQVAEKKIKTEEKPEETAIPKEEATAKESVIATTASAVTPKLVVVNEKAETAKTEEISQEKENAEPTDSAEATEAEEKKTSDDNEFKLNVLKEQEELIKKEEEEAKQRASREHVPDDINLDEEEEAKSVPPIPADQAAKTFVIKKD | Function: Involved in mitochondrial potassium homeostasis through the mitochondrial K(+)/H(+) exchange regulation . With MBA1, plays a role in ribosomal translation and protein insertion into the inner membrane .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65005
Sequence Length: 573
Domain: The matrix-exposed C-terminus contains a 14-3-3-like domain which is necessary and sufficient for interaction with mitochondrial ribosomes.
Subcellular Location: Mitochondrion inner membrane
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O15151 | MTSFSTSAQCSTSDSACRISPGQINQVRPKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGELLGRQSFSVKDPSPLYDMLRKNLVTLATATTDAAQTLALAQDHSMDIPSQDQLKQSAEESSTSRKRTTEDDIPTLPTSEHKCIHSREDEDLIENLAQDETSRLDLGFEEWDVAGLPWWFLGNLRSNYTPRSNGSTDLQTNQDVGTAIVSDTTDDLWFLNESVSEQLGVGIKVEAADTEQTSEEVGKVSDKKVIEVGKNDDLEDSKSLSDDTDVEVTSEDEWQCTECKKFNSPSKRYCFRCWALRKDWYSDCSKLTHSLSTSDITAIPEKENEGNDVPDCRRTISAPVVRPKDAYIKKENSKLFDPCNSVEFLDLAHSSESQETISSMGEQLDNLSEQRTDTENMEDCQNLLKPCSLCEKRPRDGNIIHGRTGHLVTCFHCARRLKKAGASCPICKKEIQLVIKVFIA | Function: Along with MDM2, contributes to TP53 regulation . Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions.
PTM: Phosphorylated. Phosphorylation at Ser-367 promotes interaction with YWHAG and subsequent ubiquitination and degradation. Phosphorylation at Ser-342 also induces ubiquitination and degradation but to a lower extent.
Sequence Mass (Da): 54864
Sequence Length: 490
Domain: Region I is sufficient for binding TP53 and inhibiting its G1 arrest and apoptosis functions. It also binds TP73. Region II contains most of a central acidic region and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc mediates the heterooligomerization with MDM2.
Subcellular Location: Nucleus
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O35618 | MTSHSTSAQCSASDSACRISSEQISQVRPKLQLLKILHAAGAQGEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGDLLGCQSFSVKDPSPLYDMLRKNLVTSASINTDAAQTLALAQDHTMDFPSQDRLKHGATEYSNPRKRTEEEDTHTLPTSRHKCRDSRADEDLIEHLSQDETSRLDLDFEEWDVAGLPWWFLGNLRNNCIPKSNGSTDLQTNQDIGTAIVSDTTDDLWFLNETVSEQLGVGIKVEAANSEQTSEVGKTSNKKTVEVGKDDDLEDSRSLSDDTDVELTSEDEWQCTECKKFNSPSKRYCFRCWALRKDWYSDCSKLTHSLSTSNITAIPEKKDNEGIDVPDCRRTISAPVVRPKDGYLKEEKPRFDPCNSVGFLDLAHSSESQEIISSAREQTDIFSEQKAETESMEDFQNVLKPCSLCEKRPRDGNIIHGKTSHLTTCFHCARRLKKSGASCPACKKEIQLVIKVFIA | Function: Inhibits p53/TP53- and TP73/p73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Inhibits degradation of MDM2. Can reverse MDM2-targeted degradation of TP53 while maintaining suppression of TP53 transactivation and apoptotic functions. The short isoform is a more potent inhibitor of TP53 activity than the long isoform.
PTM: Phosphorylated. Phosphorylation at Ser-367 promotes interaction with YWHAG and subsequent ubiquitination and degradation. Phosphorylation at Ser-341 also induces ubiquitination and degradation but to a lower extent (By similarity).
Sequence Mass (Da): 54963
Sequence Length: 489
Domain: Region I is sufficient for binding TP53 and inhibiting its G1 arrest and apoptosis functions. It also binds TP73. Region II contains most of a central acidic region and a putative C4-type zinc finger. The RING finger domain which coordinates two molecules of zinc mediates the heterooligomerization with MDM2.
Subcellular Location: Nucleus
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