ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8IQ70 | MSRNRAAMVSAFRLFLRPATTTTHRSLALRLAPGTTFALHLRPCHELQQHRSFASTAEDGETDKHKKPTTGEDIYVEYVNGMPHMTVRLPSRNELCQFALKPISHNVGDLLAMLRAEDRGIDRAAVINKHGVRIASSCTIESLLDDSFSIQINNRTLDVNPPKRDKVTLESMDKVGDVRKVIAQLYEAFNVGEYQLEKSNQLAKELETLRYELEPLEEKKLELSKKAARRTNFMTWMGLGLMSVQFGILARLTWWEYSWDIMEPVTYFVTYGTTMAMYAYYCVTKREYMMEDVKNREFSLSLYRNAKKVQFDVEHYNELK... | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria . Constitutes a pore-forming and calcium-conducting subunit . Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of c... |
Q8NE86 | MAAAAGRSLLLLLSSRGGGGGGAGGCGALTAGCFPGLGVSRHRQQQHHRTVHQRIASWQNLGAVYCSTVVPSDDVTVVYQNGLPVISVRLPSRRERCQFTLKPISDSVGVFLRQLQEEDRGIDRVAIYSPDGVRVAASTGIDLLLLDDFKLVINDLTYHVRPPKRDLLSHENAATLNDVKTLVQQLYTTLCIEQHQLNKERELIERLEDLKEQLAPLEKVRIEISRKAEKRTTLVLWGGLAYMATQFGILARLTWWEYSWDIMEPVTYFITYGSAMAMYAYFVMTRQEYVYPEARDRQYLLFFHKGAKKSRFDLEKYNQL... | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria . Constitutes the pore-forming and calcium-conducting subunit of the uniporter complex (uniplex) . Activity is regulated by MICU1 and MICU2. At low Ca(2+) levels MCU activity is down-regulated by MICU1 and MICU2; at ... |
P53206 | MSCSQNKTSVSLAWRECISIASVLIGAYASYKYYKLFKTRDIPRPKEGVEELIGNTPLVKIRSLTKATGVNIYAKLELCNPAGSAKDRVALNIIKTAEELGELVRGEPGWVFEGTSGSTGISIAVVCNALGYRAHISLPDDTSLEKLALLESLGATVNKVKPASIVDPNQYVNAAKKACNELKKSGNGIRAVFADQFENEANWKVHYQTTGPEIAHQTKGNIDAFIAGCGTGGTITGVAKFLKERAKIPCHVVLADPQGSGFYNRVNYGVMYDYVEKEGTRRRHQVDTIVEGIGLNRITHNFHMGEKFIDESIRVNDNQA... | Function: Putative cysteine synthase that catalyzes the conversion of O-acetyl-L-serine (OAS) into cysteine, the last step in the cysteine biosynthesis pathway. However, this CS-like protein is unlikely to function in cysteine biosynthesis. It seems that in S.cerevisiae cysteine biosynthesis occurs exclusively through ... |
B9KIH0 | MRSSRSAKVSLVGAGNIGGALAHMLGASQVVKELVLVDVAGGMTEGKVLDVGQALALLGSDVYITGGSDYAAIEHSDAVVVTAGIPRKEGMSREDLLNTNAAVVRNIAENIAKYSPGALVIVVTNPLDAMVWCMYKYSGLPANRVVGMAGVLDSARFSFFLARHMNVSVSSVSAMVLGGHGDLMLPLLRYSTVGGVPVESLIESGRLNRGDIAAIVERTRKGGEEIVKLLKTGSAYCAPAASCAHMLESYVRDKRSIMPCSAYLDGQYGVRDLFVGVPVIIGEKGVEEVVEFPLTAEEQAVFDQSVELIRGSVSAIS | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 33320
Sequence Length: 317
EC: 1.1.1.37
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O08349 | MKLGFVGAGRVGSTSAFTCLLNLDVDEIALVDIAEDLAVGEAMDLAHAAAGIDKYPKIVGGADYSLLKGSEIIVVTAGLARKPGMTRLDLAHKNAGIIKDIAKKIVENAPESKILVVTNPMDVMTYIMWKESGKPRNEVFGMGNQLDSQRLKERLYNAGARNIRRAWIIGEHGDSMFVAKSLADFDGEVDWEAVENDVRFVAAEVIKRKGATIFGPAVAIYRMVKAVVEDTGEIIPTSMILQGEYGIENVAVGVPAKLGKNGAEVADIKLSDEEIEKLRNSAKILRERLEELGY | Function: Catalyzes the reversible oxidation of malate to oxaloacetate. Can also oxidize tartrate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 31874
Sequence Length: 294
Subcellular Location: Cytoplasm
EC: 1.1.1.37
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O84381 | MVSQTVSVAVTGGTGQIAYSFLFSLAHGDVFGLDCGIDLRIYDIPGTERALSGVRMELDDGAFPLLQRVQVTTSLHDAFDGIDAAFLIGSVPRGPGMERRDLLKKNGEIFATQGKALNTTAKRDAKIFVVGNPVNTNCWIAMNHAPRLLRKNFHAMLRLDQNRMHSMLSHRAEVPLSAVSQVVVWGNHSAKQVPDFTQALINDRPIAETIADRDWLENIMVPSVQSRGSAVIEARGKSSAASAARALAEAARSIYQPKEGEWFSSGVCSDHNPYGLPEDLIFGFPCRMLATGEYEVIPRLPWDAFIRGKMQISLDEILQE... | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 35708
Sequence Length: 326
EC: 1.1.1.37
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P61974 | MTESVKKIAVTGAAGQIAYSLLWRIANGDVYGKNTPVELQLLEIPQAIGGAEGVAMELLDSAFPLLKNIVVTDKAEVAFDGTNAAFLVGAKPRGKGEERADLLTANGKIFGPQGKALNDNAADDIRVLVVGNPANTNALIAQHAAKDIPADRFNAMMRLDHNRGIAQLSEKLGRDKNDIEKFVVWGNHSAGQFPDITYATIGGEAISGLVDHDWYTGEFIPRVAKRGAEIIEVRGKSSAASAASSAIDHMHDWINGTDGQWRTAAIPSDGSYGVPEGLIFGFPTISEDGQWKIVQDLELSDFQKDGIARNVTELEEEREA... | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 34976
Sequence Length: 326
EC: 1.1.1.37
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Q8NN33 | MNSPQNVSTKKVTVTGAAGQISYSLLWRIANGEVFGTDTPVELKLLEIPQALGGAEGVAMELLDSAFPLLRNITITADANEAFDGANAAFLVGAKPRGKGEERADLLANNGKIFGPQGKAINDNAADDIRVLVVGNPANTNALIASAAAPDVPASRFNAMMRLDHNRAISQLATKLGRGSAEFNNIVVWGNHSATQFPDITYATVGGEKVTDLVDHDWYVEEFIPRVANRGAEIIEVRGKSSAASAASSAIDHMRDWVQGTEAWSSAAIPSTGAYGIPEGIFVGLPTVSRNGEWEIVEGLEISDFQRARIDANAQELQAE... | Function: Catalyzes the reversible oxidation of malate to oxaloacetate. Exhibits higher catalytic efficiency for oxaloacetate reduction than for malate oxidation in vitro. Almost equally active both for NADH and NADPH on the bases of the kcat values at pH 6.5, but catalytic efficiency for oxaloacetate reduction is 50-f... |
P61897 | LRRKPGMDRSDLFNVNAGIVRNLVEQIAVTCPKACIGIITNPVNTTVAIAAEVLKKAGVYDKNKLFGVTTLDIIRSNTFVAELKGKQPQDINVPVIGGHSGVTILPLLSQVPGISFSEQEVADLTKRIQNAGTEVVEAKAGGGSATLSMGQVPG | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 16149
Sequence Length: 154
EC: 1.1.1.37
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P19980 | SKTPIRVAVTGAAGNIGYHLLFRIA | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 2626
Sequence Length: 25
EC: 1.1.1.37
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Q6L0C3 | MARSKISVIGAGAVGATVAQTLAIRQTGDIYIFDIVDGLAEGKALDILEGAPHWGYDLDIKGFCTADESKYAEMKGSDVIVVTAGLARKPGMSRDDLLLKNIGIMKSVGEAIKKYSPESKIVVVTNPADIMAYAIYKASGISPERIIGLGGSLDSTRFRTFLAQELNVSFEDVNAFVIGGHGDDMVPFIRYSNVSGIPIEDLLPREKIDEIVKRTRFGGGEIVNLYKTGSAFYAPGISIAVMVESIVNDRKRVIPCAAYITGEHSKTYLVNNLFIGVPIKIGKNGVEKIYDLKFNEDELEAWKKSVESVKKNSAIADDYF... | Function: Catalyzes the reversible oxidation of malate to oxaloacetate.
Catalytic Activity: (S)-malate + NAD(+) = H(+) + NADH + oxaloacetate
Sequence Mass (Da): 35215
Sequence Length: 324
EC: 1.1.1.37
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C0LGU7 | MGCRWNPIGFQFSCFMFLIITLQSRSSLSLESEGFVLLKFRARVDSDPHGTLANWNVSDHDHFCSWFGVTCVDNKVQMLNLSGCSLGGTLAPELSQLSELRSLILSKNKLSGDIPNEFASFAKLEFLDLRDNNLNGVVPPELNKVLTPENLLLSGNKFAGFMTVKFLRLQSLYKVQMNKNRELSSVSADVLDCVNRKLGYCVSRRSLITRNKAKAFVLRIRATSRHYMVRRESHGKNYVVNYHPSENETSIFKRRELLEETSNLAAMPAPDTPSPSPEIITIVFPRSSGSFPALTNAKKRIPPLIPPSSPPPLPTNNTIA... | Function: Involved in the pollen tube perception of the female signal.
PTM: Phosphorylated by MIK1.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 78476
Sequence Length: 695
Subcellular Location: Cell memb... |
Q9Y7M7 | MDPIRFGLSRVPFAHCYNKRVIFRANYLVPLTWLKNNVAYKSTNTLLLPTPNAEYYSTSKLSSQVNVSLNSLSQKASSGSKIYPFKNSFPLPFSRSILPIRSLAFLKLCVRHNSTVPSKDEQAQDISKINTNGTLQTPNKKVNVFRLFTLARGQGWNFFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMGIPSGTFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAF... | Function: Mediates export of peptides generated upon proteolysis of mitochondrial inner membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79020
Sequence Length: 726
Subcellular Location: Mitochondrion inner membrane
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P33310 | MIVRMIRLCKGPKLLRSQFASASALYSTKSLFKPPMYQKAEINLIIPHRKHFLLRSIRLQSDIAQGKKSTKPTLKLSNANSKSSGFKDIKRLFVLSKPESKYIGLALLLILISSSVSMAVPSVIGKLLDLASESDGEDEEGSKSNKLYGFTKKQFFTALGAVFIIGAVANASRIIILKVTGERLVARLRTRTMKAALDQDATFLDTNRVGDLISRLSSDASIVAKSVTQNVSDGTRAIIQGFVGFGMMSFLSWKLTCVMMILAPPLGAMALIYGRKIRNLSRQLQTSVGGLTKVAEEQLNATRTIQAYGGEKNEVRRYAK... | Function: Mediates export of peptides with molecular masses of 2100 to 600 daltons generated upon proteolysis of mitochondrial inner membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75950
Sequence Length: 695
Subcellular Location: Mitochondrion inner membrane
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Q945K2 | MEKSTMSAILLVLYIFVLHLQYSEVHSLATTSDHDFSYLSFAYDATDLELEGSYDYVIVGGGTSGCPLAATLSEKYKVLVLERGSLPTAYPNVLTADGFVYNLQQEDDGKTPVERFVSEDGIDNVRGRVLGGTSIINAGVYARANTSIYSASGVDWDMDLVNQTYEWVEDTIVYKPNSQSWQSVTKTAFLEAGVHPNHGFSLDHEEGTRITGSTFDNKGTRHAADELLNKGNSNNLRVGVHASVEKIIFSNAPGLTATGVIYRDSNGTPHQAFVRSKGEVIVSAGTIGTPQLLLLSGVGPESYLSSLNIPVVLSHPYVGQ... | Function: Involved in cyanogenesis, the release of HCN from injured tissues. Catalyzes the stereospecific addition of HCN to a variety of aldehydes in vitro. Has no oxidase activity. The redox properties of the FAD cofactor appear to be unimportant for catalysis.
PTM: Glycosylated. Deglycosylation does not affect the e... |
P57551 | MKLFNQLRWFFVREWKRYLGAILLLIIIATLQLLPPKIVGVLIDLIIKKNMHGVQILPWILIIFLVAVIVYILRYLWRILLFGASYQLATELRVKFYTYLSQQSQIFFLKNRTGDLIARATNDVDRVVFAAGEGVLTLVDSLVMGFSVLIVMSTQISFLLTIISLIPMPIMAILIKKYGKELHETFRHAQISFSLLNNQTQEILTSIRMIRAFGLEKNQSNKFNIITRNTGKKNMEVAKIDARFDPVIYLSVAFSNLLAIIGGGWLVWNNQISIGQLTSFIMYLGLMIWPMLALAWMFNIVERGSAAWDRIHSIINKKLY... | Catalytic Activity: ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67522
Sequence Length: 589
Subcellular Location: Cell membrane
EC: 7.6.2.2
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Q5BH33 | MTHFPVNIASDKQEFDPERWAKTPTTESSVNGENGTAPTSGLPSRHPSTGISVLIVGAGMGGLMTALECWRKGHDVAGILERSEGPVYSGDIIVMQPSAVSIIRHWPDMLHDMKAEQVHAVVSYETHDGRHIYGPTVPSFNDPEHLETRKGPFVAPAQVRRKFYRMLLRQVARCGLRVEYGKTVKSYFEDEKDGKGGVIIATTGEAEVRVADIVVAADGLKSPSEILIAGQHVPPRSSGLSIYRTAFPKDLAMQNELVRKRWSDSPPIWEYWLGPGMYLGVFVGDDIISFGFTPRDDIVEGTATESWEPDTDPETVAQAM... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG . The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioe... |
Q5BH31 | MAQPQQHKGGYKQINKALNICAFEDYLSAQLKHLPQLADVEQLSPRVIRVLGQNAGKGTNTYIVGTGPQRLIIDTGQGIPEWADILDATLKERSISLSHVFLSHWHGDHTGGVPDLLRLYPNLAGAIYKNSPGSDQQPIDDGQVFRVEGATIRAVHGPGHSHDHMCFILEEENAMFTGDNVLGHGTSAVEELGVYMETLRKLNSHHCAVGYPAHGDVITNLPAKIAGELAQKMRREKQVLLTLDRINKESRRTGQVVLVHGDGIDEEVRKMALEPFIDEVLRKLAEDGKVAFEMRGGVKRWFGVGVL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Atrochrysone carboxyl ACP thioesterase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG . The atrochryson... |
P9WEV9 | MASLTTLKNTAIVTGSFLSGAMITLSTITVPVLLETSTHPPQLLHQWVRTYHYGHISLPTISIATAILYFYIAAYQGAREQPWRKAALVGFLTIVMVPFTWIVMSSTNGMLFGLEAGNRDHSQFFEQGANRSGLKGANSSQSHGLGNVSVGIGVEMATLEGVRELLVRWKWMHLVRSLFPLMAAVLGVGICV | Function: Anthrone oxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG . The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond... |
A8AGX5 | MFYWILLALAIAAEITGTLSMKWASVSNGNTGFILMLVMITLSYIFLSFAVKKIALGVAYALWEGIGILFITLFSVLLFDEALSAMKIAGLVTLVFGIALIKSGTRKPVNAAKEATHAAV | Function: Catalyzes the excretion of spermidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12860
Sequence Length: 120
Subcellular Location: Cell inner membrane
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Q6FT96 | MTDQISHLGKTLSTAASVLIGSQDIEKNVENNLLSNSPRNPYRKTLQESLTAADFMNHETFDKLRKTRAIASTLSEDSKGLYSQRSREKYFTNKVSDKKTTFKVLSHLSDDLLKDLPETAESKSNTRDQGETKLLKESDSTDASQERIFSLYQGFEASIPVINRSVEKEHLLLEQNNQESAAQILPQMGNKPRIRSGPWEDLLESKEDTYISLDFNPERISNIKSKKELERINELANNNLVMLDIRKKLSADEIDEIKKQIQDLQLKQNLLVKKIAAIEENELFLEDIIRLIGHRSADFSNDTQIEFDQAKSLSGLNNPE... | Function: Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division... |
P0CS45 | MANHHDHDKPLRSALDPISSPYFSSLNGTLSIAKEVLIGPFQGDHRRSESARILSDLAPSLMQPRFLNAASSSQQSLSKSSHPGAPYPLLRLPTNLPFNKSSRPTASSLAILEAVDNLASLSLGDVSHPQNGQNSPSLIRGFKATIPSSELAKQRRRMVRGGIVDEDLGGKIGLKKLGDRARGLLTEKGEDEEDGELGVGRHAVKKRRKKRESRRFTEGRHLEGKLRLEDLAKQADEIGQDKENLHVRQSLIQSEIAEVGAKIDALEDIRRHLEASLLHLQEEDLELDDELEGVQELMASPAIKAAAGAKSLPLSSSGAG... | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral ... |
Q5AXW3 | MDKHRRDDSPSGLSDIVERDGLLGTGITSRHIEAFGRKVTSTAGHLMGPSGDPSTSTHYQNAMVDIHRELRRPSTQRKVFALAQTTPTDLVRSKLSTSEIQSRAISSLPDELLLNIPDDTSSYSLFEGFQATQNDHEYRKAHRRGRSKGKKLLKDKDGEQADPPSTLTELKKERDLLSRRMELMGVRKNMCSSEIVDIDNKIANFHRMRQIVLDRLAGLEMEEAELEHEVNEIDNKLDDMAEEEAAQAAQAAAAAAAATTAGSETHEEPASEDPAMDASFMSESIYQKLPSPRSLKHRSIRKRSMPVLHEHFAPGSEIKE... | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral ... |
A4RJV3 | MASPEDENPFQDDPGQEDEDGSILSPRGLEAFSRKVTTTASHLMGPVVDPSSSGHYQSAMTEVQKHLRRPNLQRSMFSMARTTPSDLVRSKLSTREIQHRALAHVPDDMLANIPEDDNNSYSLFQGFQASFPELTDEGKKHRRRVSRGRKLLDEGPTTPENGTTGLQKLRKERASMSHELEMLGIRKNMASSEIREIDIKIANLHGMRRIILERLAALEQEETLLEHDLMEVEARVEDAQMLADEAESTAQQSSPRDTDDADAEDNDGFMSQSIYEKIPSAASTPSKSRKPRIVRRKSMAVLHEHFEPGTSIRELRAHQD... | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral ... |
A8PTE4 | MGSSSANKKHASTSSAPSNDVRAPHADTNRLLNDMAPQLMTPAMMNAMARISLQSTPIATTRDPFPLQRATLLLAPRFSMENPARSLARISSSLLQFSGLSKHSKSGREQQRTPITSMDVGVLEESQRILATADADLDASLDTSLLDDDNDTSDVAAAADAPVSLFRGYKATVPQVSTSKTRRRQLQASENIRRSKHEPHLLSLQELEVQDRDMLAERRNLEIRRALYHAEIVHVDAKIAALEATKASLQQKLLHVREEELELDDERQGVSELLELQRHRRAMPGGRGLDAGTVLPIGAGSSRWRKTPVFLPSEHDDLPH... | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral ... |
Q7S8R5 | MANSDQNRDVFPDDVSIDDDTSVISTRGLEAFGRKVTTTASHLIGPITDPTSHPHYQTAMTEIHKQLQKPTLQRGVFAIARTTPTDLVRSKLSSKEIQSRALAYVPDELLRNIPASSNSYSLFQGFQASFPDFTDDGKKHKRRVSRGRKMLDESPVQPGSPHAVQRLKKDKASMMHQLEMLGVRKNMASSEIREIDNKIANLHGMRKIILDRLANLEKEEAVLEHDIMDVESRLDEAQELADEAESLAMATPNKSEEDLSRTEEGFMSQSIYEKLPAANTPPGKKKPRNHRKKTLPILHEHFEPGTMIRSMRAHQDNITA... | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral ... |
Q0U2T3 | MASSFARDGSPSRGRSTSPRPRIPEESLEASLMDGLPDTRQLQAFGRKVTATAGSLIGTEGVGQHYQNALGELHRELRRPMLQRSVFSFAQTTPREIVRSRISVPEIQQRALAYVPDDMLANIPEDNNEFSLFQGFQATLPDEPETIKKKGKTHNARGQRLIGGELEDDEYSKLPPSMQRLQKQKHSMSHQLEMMGVRKHMCVAEIHEIDNKIANLNTMRKMVLDRLAGLEIQEEELAQDLLGVDNEIEDLQEELDDAAALAPPKEDSRPTTSGSEAVSETFMSESIYQKISPKSKNRGKKPIRRPSMRVLHEHLESGSK... | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral ... |
Q9P7I3 | MTDNNSKSKDSSQKIPNDSLTPTISKGLRKDVFYWTKAIAYTTWNFFDSSPVTPQRNPISLFVRGLSHPFLRHRLSKSQFNEWFLSHNGVDPVQAQTLPDPLLFDIPDHQETSYSLLEGYSVTAHDHSDTSPLPITSSNQKEGKKNVSSIDVSMVSDSSEFKPDSLQHEKLVKKCNQLRLQKLINSSELAQIDLELSKLYSRRRQVLERLSKIEEQNLKYTSKLASVEKLMLDSDAQDLYSSYSHDLIPSQIEAGKNGANPDVFDDTHDKYTDNLSARAISPRAPRPSTASEVVSDYFEQNSAFSKAPENTESSVNQNYI... | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral ... |
Q4P8R5 | MSYSPLLGADRRAGEPSSGLASSTSIRDTLSGALNSTKAYLQPFTPASPYLGSNGVNGHNEPSRLLSDVAPQLMTTRMMAAVTNSNTALGLTPDGQRRARLLLTPGFSITSPARSLVRIGGSLIQSGIGRGPMNGITSNELFVLEESDRILATAARDLDLEANADAQLGARSAIEASKSKAAEPSVSLLRGFQATIPSSTEGRQRRRRVRALASGFEDGPEGPTKLGLKAMGDKARGLMVEGVDAEPVSAFQAREQRHARRNQASRILSRAKEGSRSSAIQLEELERQLREIEREQGDVGVRRSLIDSEMAAVDDKIKVL... | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral ... |
A7THX0 | MDDNEQFSQLRNVISTTASALLGIENLDKSILSSNSRYKKILSETIKNLGGDDSLVKLRKNFSNLKRQEESHDAYERYSGDDYFRNQLTDSRTTFRVLTYLSDEILKASLDDEKSNHDQGLLEFTNEEESGTKNTSSLFQGFEASLPILNERLENNDKNKYIKNSEGNDHNNNNDNNDDKNDKLFEFTNNYISSVSIDTEKISRSYSMKYLKTLSEDVLRKLNFTLIQEDVTKEEVEDLSIKLERLKERHQSACKRLETVEQDELFLENALSLIKDRMKFIQEYDLELESNDPEIEDINQNEKSYNEAKESNDLNTSQQN... | Function: Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division... |
Q6CB13 | MSDVTHFSKVVAATASTLVSGDLSQSHVMRDISRPAFQKRIFSFSKRPSELVRITSSSKDVLLPDEMLVDIPSNENQFSLFQGFQATLPEHSVGSQLLLGDGSKVGEKSAREQLVEGKKSLSHKLDLLEVRKALAANEITEIDARVAHLQSMRQIVFDRVASLEQQEFQLESEVLRIDAELEQMEEEKEEVIQRHDYETRTPEELEDDVVDLKSVSEKLQSASQKTLPRRNLSRRKTQPTLQQYYEPGNKIRQIKAHSDSVTCLDFDIPFGTMVSAGMDLGLKVWDLSRGDLVTDLKGHNASVTCLQVDNNVLATGSADA... | Function: Involved in mitochondrial fission. Acts as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity).
Location Topology: Peripheral ... |
P47025 | MSVNDQITHIGKTLSTTASAFLNYQKSNSNTQDVLTNNGPYKNLLSNTVNNASSTSYFYKRTEHGRFVKNASNTFEDIYSKTRRGDVFRNKFTDNKTCFRMLTYISDDLLNEIPTKEGLKSDADGKLLTEGGENENLRKNASKKETSLFQGFKSYLPIAELAIENTERLNYDTNGTSGTVGAKDVMSKTNERDEIHTELPNFQDSFLIPPGVETKKISSSYSPSALKSFSQTLVNSLEFLNIQKNSTLSEIRDIEVEVENLRQKKEKLLGKIANIEQNQLLLEDNLKQIDDRLDFLEEYGLEVIEANSDENAEDDGMSER... | Function: Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein, binding to FIS1 on the mitochondrial outer membrane and recruiting the dynamin-like GTPase DNM1 to form mitochondrial fission complexes. Formation of these complexes is required to promote constricti... |
O06989 | MVLLKKGFAILAASFLAIGLAACSSSKNPASSDGKKVLTVSVEETYKEYIESIKTKFEKENDVTVKIVEKQMFEQLEALPLDGPAGNAPDVMLAAYDRIGGLGQQGHLLDIKPSNTKSFGDKEMQQVTVDGKVYGMPLVIETLILYYNKDLLKTAPKTFKDLEKLTEDPRFAFASEKGKSTGFLAKWTDFYMSYGLLAGYGGYVFGKNGTDSGDIGLNNKGAVEAVKYAEKWFETYWPKGMQDNSSADDFIQQMFLEGKAAAIIGGPWSAANYKEAKLNYGAAPIPTLPNGEEYAPFAGGKGWVASKYTKEPELAEKWLE... | Function: Part of the ABC transporter complex involved in maltodextrin import. Binds maltodextrin. Can also bind maltose with low affinity, but is not involved in its uptake.
Location Topology: Lipid-anchor
Sequence Mass (Da): 45601
Sequence Length: 417
Subcellular Location: Cell membrane
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P51608 | MVAGMLGLREEKSEDQDLQGLKDKPLKFKKVKKDKKEEKEGKHEPVQPSAHHSAEPAEAGKAETSEGSGSAPAVPEASASPKQRRSIIRDRGPMYDDPTLPEGWTRKLKQRKSGRSAGKYDVYLINPQGKAFRSKVELIAYFEKVGDTSLDPNDFDFTVTGRGSPSRREQKPPKKPKSPKAPGTGRGRGRPKGSGTTRPKAATSEGVQVKRVLEKSPGKLLVKMPFQTSPGGKAEGGGATTSTQVMVIKRPGRKRKAEADPQAIPKKRGRKPGSVVAAAAAEAKKKAVKESSIRSVQETVLPIKKRKTRETVSIEVKEVV... | Function: Chromosomal protein that binds to methylated DNA. It can bind specifically to a single methyl-CpG pair. It is not influenced by sequences flanking the methyl-CpGs. Mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3A. Binds both 5-methylcytosine (5mC) and ... |
Q2KIA0 | MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPNFEMPVSIPVSSHNSLVYSNPVSSLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNMQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYG... | Function: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an essential role in h... |
Q8CFN5 | MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVETLRKKGLNGCDSPDPDADDSVGHSPESEDKYRKINEDIDLMISRQRLCAVPPPSFEMPVTIPVSSHNSLVYSNPVSTLGNPNLLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNIQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSEDVDLLLNQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYG... | Function: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18 . May also be involved in neu... |
Q14814 | MGRKKIQIQRITDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNHSNKLFQYASTDMDKVLLKYTEYNEPHESRTNADIIETLRKKGFNGCDSPEPDGEDSLEQSPLLEDKYRRASEELDGLFRRYGSTVPAPNFAMPVTVPVSNQSSLQFSNPSGSLVTPSLVTSSLTDPRLLSPQQPALQRNSVSPGLPQRPASAGAMLGGDLNSANGACPSPVGNGYVSARASPGLLPVANGNSLNKVIPAKSPPPPTHSTQLGAPSRKPDLRVITSQAGKGLMHHLTEDHLDLNNAQRLGVSQSTHSLTTPVVSVATPSLL... | Function: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific, growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays div... |
P86889 | MGSAMVLSMSLLGFLPYAVFGPAIGVLVDRHDRKKIMIGADLIIAAAGSVLTIVAFYMELPVWMVMIVLFIRSIGTAFHTPALNAVTPLLVPEEQLTKCAGYSQSLQSISYIVSPAVAALLYSVWELNAIIAIDVLGAVIASITVLIVRIPKLGDRVQSLDPNFIREMQEGMAVLRQNKGLFALLLVGTLYMFVYMPINALFPLISMDYFNGTPVHISITEISFASGMLIGGLLLGLFGNYQKRILLITASIFMMGISLTISGLLPQSGFFIFVVCSAIMGLSVPFYSGVQTALFQEKIKPEYLGRVFSLTGSIMSLAMP... | Function: Confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides but not to 16-membered macrolides, lincosamides or analogs of streptogramin B. May function as an efflux pump to regulate intracellular macrolide levels (By similarity).
Location Topology: Multi-pass membrane pro... |
Q5XBB2 | MEKYNNWKLKFYTIWAGQAVSLITSAILQMAIIFYLTEKTGSAMVLSMASLLGFLPYAVFGPAIGVLVDRHDRKKIMIGADLIIAAAGSVLTIVAFYMELPVWMVMIVLFIRSIGTAFHTPALNAVTPLLVPEEQLTKCAGYSQSLQSISYIVSPAVAALLYSVWELNAIIAIDVLGAVIASITVAIVRIPKLGDRVQSLDPNFIREMQEGMAVLRQNKGLFALLLVGTLYMFVYMPINALFPLISMDYFNGTPVHISITEISFASGMLIGGLLLGLFGNYQKRILLITASIFMMGISLTISGLLPQSGFFIFVVCCAIM... | Function: Confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides but not to 16-membered macrolides, lincosamides or analogs of streptogramin B. May function as an efflux pump to regulate intracellular macrolide levels (By similarity).
Location Topology: Multi-pass membrane pro... |
Q8KBE8 | MNSKQITTLWCAVIVEELIRQEAGFFCISPGSRSTPLTLAVASNPKARFRMFPDERSAGFYALGYARATGMPAVLVCTSGTAVANYFPAVVEASADAQPMLVLSADRPFELLECGANQAIRQQNIFGSYTRWSFELPEPGIATPLASLLSTVDHAVRKSLSLPAGPVHLNLPFREPLEPEAPDPGHPWAAPLETWQASGEPWSRFARPLHEPSAESIVTLRELLAQAERPLFVAGSMSNAADGEAVAALAESLGVPLFADLTSGIRLSSDCTPWQLAFQNEAFVERFQPDVVIHFGGHVIGKQPAMALRKQPPLHYVVVR... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
A0M345 | MKYSKIPVARSVVALCVAKDIKHVVISPGSRNAPLTIGFTHHDEITPYSIVDERCAAFFALGLAQELKKPVALVCTSGSALLNYYPAIAEAYYSDIPLVIISADRPIERIDIGDGQTIRQKNVFENHILYSANLYSELVLENQSQDPKLQQKQFEAQKHNEREVNLALNKAIEEKGPVHINVPFYEPLYDTVENINVNPLQIFPEIKERHYSEKQLQNYANEWNRAERKMVIVGVAQPNAVEQKFLEGLATDPSVIVLTETTSNLHQEQFFTRIDTLIGPIEKDENREELFNRLQPDILLTFGGMIVSKKIKSFLRNYSP... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
B0RCZ5 | MAAADALPTSSASASASADGPRTGNPSTDRAIAMLLALVREGVTDVVLCPGSRSQALALVAAELERVDGVRLHVRIDERAAGFLALGLGVESGRPAPVITTSGTAVANLHPAVLEGWHSGVPMLLLTGDRPAELRGIASNQTTRQPGMFGDRVACIDVPAPEETDDDLARDALLARDAYRRARDERTPVHVNVAFRDPLSVAVPDLTEAVAEVRAAAPATPAPAGPATADVLDLPHGPRTLVVAGHAAGEAAEELARAGGWPLAAEISSGSHFGPNLVVSFRELLAREGFGDRVERVIVFGHPTLTREVPLLVGREDVEA... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q8FSB6 | MSVTPAQELAREVIEALSPHITDVVLCPGSRNSPLSLEVLSREDLRVHVRIDERSAAFLALGLARVQRRPVPVIMTSGTAVSNCLPAVTEAAHAHIPLLVVSADRPAHLIGTGSSQTIDQTDIFGALAPTVTVAAPEHVGRISQALGNGASQSPRHINVALDMPLVAPDLPELHGQRGPVDWEQRWVDHGVVDVDLSRNTLVIAGDEAWEIEELAEVPTIAEPTAPVAYHPVHPLAAEFLLKDQVSAEGYVVTTRPDHIIVVGHPTLHRGVLKLMTDPTIELTVLSRTDVITDPGRHADRVGSRVKVTGEQQKQWLKICD... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q4JT09 | MRAGLVLVDQLIRSGVREAVLCPGSRNSPLNLAFVEAERVGRVRLHVRTDERSAAFLALGLAKVSRRPVPVVMTSGTAVANCLPAMVEATLSGVPLVVLSANRPLSMLGSGANQTIDQAEIFGTHSVCTLNTGELALEGAAAGAAGELRDLVRKLINAATDPIDGGGAHLDVPLREPLVPPTLDELSLWAGEIAAAEDAATTEGAHDSHAPSQPTRGPRKLPYGQVEVDLSRRTLVIAGSVSDVAWARSIMDELADVPTVAEPVAPAPDFPVHSAAVDMFSTQVVSDGEHSAVTIPEQIVVIGRPTLHRGVTKLLANKDI... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q6A9B0 | MNPSTAVARRLVNALVEAGVEHVVYCPGSRDAPIGYALADAETAGWLRVYVRLDERSAGFVALGLGRAGCPAALVTTSGTAVANIHPAVLEADAAGVPLIVLSADRPAEMWHTGANQTTVQTGIFGSAPRLSTDVPAGFPADERLDALVLRAVTAATGALSADPGPVHLNVSFRDSLVPDGPWQPQALVPRRVSSFPTAPTPLVMPARTVVVAGDGAGSLARELAQQGGWPLLAEPTSGSRVGDNALTDYQTVLGSELVDDVEAVLVLGHPTLSRPVSRLLARPDVTVVTDRSRWTDVAGVARVVTGPVELAEIDTDPAW... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q11U88 | MQAIYDIPEILFQHGVTDVVLSPGSRCAPLSIAFSRHKKLQIKVVPDERSAAFIALGMSLQTQKPTVLICTSGSALYNYAPAIVEAYYQRVPLIVLSADRPPEWIDQNDGQTIRQQEIYGKHSKAFFQLSAEHELPDTQWETYRKVNEAVSISEAYPKGPVHINIPFREPFYPKGEIMFSGSPTVIKREQPLHTLSDEQWKSIQHKLDSYKKILFVGGQHLYDESLRLKIGNIKAPFIGEVVSNLHGVRNVIHTHDTLLTSIPLTDLEELKPDLVISFGGALLSKWLKQFIRSNESIDHWYVGPDVTTPDVFQHLCQIIP... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q47DK0 | MTDIGTLNFTWSQAIIGGFVAAGITDAVISPGSRSTPLALAMLRQAGLRCHIAIDERSAAFFGLGLAKSSHCPVLLLATSGTAPANWLPAVIEASQSGIPLILISADRPPELQDCGANQTVSQPGLFGSHTRASYTLGTPEPGFNPGYLHRVARQACEQASWPHPGPVHINQPFREPMLPSEPVLSGEMPEKISISHPDLQPDLNALGDLARRISGRPGIIVCGEMPSRDGQNEALVALATRLRSPIFAEPLSGLRFGPHDRSHLCVRYNDWLGKTDLVSQYRPEWVIRFGAYPVTRNLQKLVSEITETHALVDPWPRWI... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
B8FTY8 | MTNYIAALVDELYQLGVREAVISPGSRSTPLSVLFCEYGFQVYVGIDERSAGFFALGIAKEKERPVVLVCSSGSAVAHYFPAIVEAKHSHVPLIVLTADRPPELRQVGAPQTIDQIKFYHDYAKYFEELALPEEREGMYRYVRGVMRKAYVSSLDQGYGVAHINIPLREPLSPDLDGVDFTAGRLDYPFAWKTGEKGLTMDSSVFQDKKGIIICGGDPYADYHREVLELAERLKAPLLADPLANFRNDDHPLIMDCYDAFLKSDAVKVELKPEFIIHFGQTPVSKRLQNFTAMHQDVLYFQVNDYFQYRDPSLSISRYLV... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q6ARP3 | MRAKQHISDLAHHCIAHGMRHLVISPGSRNAPLIRAFAASSQIECLSIVDERSAAFVALGLATELQAPVGVLCTSGTALLNYGPAIAEAYYLRAPLIVLSADRPARLVGQQDSQTICQDNLFANIVKGSYSLPEEPETVAELELSARVIAQAFSTALSPCFGPVHINIPLDEPLYGGELMAESLIALSPLQLAEPKGMSPALWQEVESAWRGAKRRMIVCGQGVADAELQALLARFAPDKTVTIIAENTANIVGPWLVDRPDAVLLACDEASRSLLAPDCLISFGGHLVAKHIKLLLREFKPAFHFRLDPAQMGIDTYQC... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q8CPQ5 | MNHSEALTEQVFSFASELYAYGVREVVISPGSRSTPLALAFEAHPNIKTWIHPDERSAAFFALGLIKGSEKPVAILCTSGTAAANYTPAIAESQISRLPLVVLTSDRPHELRSVGAPQAINQVNMFSNYVNFQFDLPIADGSEHTIDTINYQMQIASQYLYGPHRGPIHFNLPFREPLTPDLDRVDLLTSVTKTLPHYQKSISVDDIKDILQEKNGLIIVGDMQHQAVDQILTYSTIYDLPILADPLSQLRKEKHPNVITTYDLLYRAGLNLEVDYVIRVGKPVISKKLNQWLKKTDAYQIIVQNNDQIDVFPTPPHISY... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q49WG6 | MNNHTDALTKQVFTIVSELYAYGIREVVISPGSRSTPLAIAIEAHPKLKSWIHPDERSAAFFAMGLMKGSEKPVAILCTSGSAAANYTPAISESSLSHLPLVVLTSDRPHELRGIGAPQAINQTNMFANYVQYQFDFPIAEKNDNEDIMANTIKFQLQKASQFLYGPHRGPIHLNLPFREPLTPNTEKVEWLTSDTKILPHYQKTTSLNEISAMMKKRKGLIIVGDMQHQDVDQILTFSTIHDMPILADPLSQLRREHHPNVVTTYDLLLRSGLELEADFVIRVGKPVISKKLNQWLKVTEAFQILVQNNDRPDAFPITP... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q2LXE3 | MPLSDNLNLLWSSLIVAELVKNGLDTFFISPGNRNAPLISALIHEERSVKKICVDERAAGYRALGHAKAAGRPGVLVCTSGTAPANYYPAVIEAFRDEIPLVILSADRPPELIGSDANQTIVQPDLYGRYCRDSLLIPCPSADYPLEALLARIDSLIARPVGPVHINCAFRDPLVPGIPDSRPIPDELLATAGRLYAREGAYTTYPSPGTLHTGLEDVEAILNRTARGLIVIGRLDGPRDAPALEELAKKLGWPVFCDIASSMKGRIPSDRQIFSLDHPEALRLVSAYAPETILQFGSGLVSKHYFASLLPHSEATVIQI... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q31NA4 | MGQAAAITMPIDPRNLNTLWSSVLAESFVRLGLQTVVICPGSRSAPLAIAFAEHPEIDAIPILDERSAGFFALGRAKASHRPVALICSSGTAGANFYPAVIEAKESGVPLLVITADRPPELRQCHAGQAIDQLRLFGSYALWEAELALPVLDLGLLRYLRQTAQQAWQQALRGGPVHLNQPLREPLAPIADPATQTWLAQQWPGENFFAELLTAVPTPQIQQPLPPLPSQGLITVGPIAPEDPAAFVQAIAQLSAHLGWPVLSDAVTPLRQFADHCPRLISSYDLILRQPHWRASLQPEAVLQIGELPTSKELRLWLTEQ... | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carb... |
Q9XAP8 | MTRASLNKQPHEVASMFDHVAERYDLTNAVLSLGQDRAWRKAVARAVDARPAQKVLDLAAGTATSSLPFARTGAYVVPCDFSQGMLQVGKERHSWLPFTAGDATRLPFKDDVFDAVTISFGLRNVQDTDAALREMYRVTRPGGRVVICEFSHPTWAPFRTVYTEYLMRALPPVARAVSSNPDAYVYLAESIRAWPDQPALAGRLGRAGWSRVAWRNLTGGVVTLHRGFKAS | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25537
Sequence Length: 231
Pathway: Quinol/quinone metabolism; menaquinon... |
B1W525 | MTRASLEKQPHEVASMFDGVAANYDLTNDVISLGQARLWRRAVAAAVDARPAQKILDLAAGTATSSQPFVKAGAYVVPCDFSLGMLKVGKERHPWMPFTAGDGMRLPFKDETFDTVTISFGLRNIQDTEVALRELYRVTKPGGRVVICEFSQPTWTPFRTVYTEYLMRAIPPAARAVSSNPDAYVYLAESIRDWPDQPALAALLQKAGWSKVAWRNLTGGVVALHRATRA | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25343
Sequence Length: 230
Pathway: Quinol/quinone metabolism; menaquinon... |
Q67LE6 | MAPGYQPPSPEEKEQYVRELFDKIAENYDAMNQVMSAGQWEKWHREFVAQTHFRPGDHILDVACGTGDLTLLDAAQVAPDGKVIGVDISEGMLEVGRRRVAASPYKDLITLQLGNAMDLPFPDNTFDGVTMGWAMRNVASIPRTLSEIYRVLKPGGRFICLEASKPFSRFIRFGFFVYWKTFLPLIDWFVVKAGRQAKVRPYTYLSRSLDNYPFPDQLEELFREAGFVETDYQLLMLGTVAIHVGTKRREG | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28582
Sequence Length: 251
Pathway: Quinol/quinone metabolism; menaquinon... |
Q31P90 | MSVLAPDAVEGLFDQIAPIYDNLNDQLSFGLHRLWKRMAVKWSAAKPGDRVLDLCCGSGDLAFLLAKVVGSKGQVIGFDRSQALLSVAGDRARQLASALVIDWQRGDALDLPFPDDHFDAATLGYGLRNVPDIPTVLRQLQRVLKPGARAAILDMHRPYSPLLRQFQQVYLDRWVVPAAAAQNCAAEYEYIDASLEAFPQGQQQVALAIAAGFQRAKHYELAAGLMGVLVVEA | Function: Methyltransferase required for the conversion of 2-phytyl-1,4-beta-naphthoquinol to phylloquinol.
Catalytic Activity: demethylphylloquinol + S-adenosyl-L-methionine = H(+) + phylloquinol + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25441
Sequence Length: 233
Pathway: Cofactor biosynthesis; phylloquinone bi... |
Q12866 | MGPAPLPLLLGLFLPALWRRAITEAREEAKPYPLFPGPFPGSLQTDHTPLLSLPHASGYQPALMFSPTQPGRPHTGNVAIPQVTSVESKPLPPLAFKHTVGHIILSEHKGVKFNCSISVPNIYQDTTISWWKDGKELLGAHHAITQFYPDDEVTAIIASFSITSVQRSDNGSYICKMKINNEEIVSDPIYIEVQGLPHFTKQPESMNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNEQPEKSPSVLTVPGLTEMAVFSCEAHNDKGLTVSKGVQINIKAIPSPPTEVSIRNSTAHSILISWVPGFDGYSPFRNCSIQ... | Function: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis).... |
Q60805 | MVLAPLLLGLLLLPALWSGGTAEKWEETELDQLFSGPLPGRLPVNHRPFSAPHSSRDQLPPPQTGRSHPAHTAAPQVTSTASKLLPPVAFNHTIGHIVLSEHKNVKFNCSINIPNTYQETAGISWWKDGKELLGAHHSITQFYPDEEGVSIIALFSIASVQRSDNGSYFCKMKVNNREIVSDPIYVEVQGLPYFIKQPESVNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNEKPERSPSVLTVPGLTETAVFSCEAHNDKGLTVSKGVHINIKVIPSPPTEVHILNSTAHSILVSWVPGFDGYSPLQNCSIQVKEAD... | Function: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis).... |
P57097 | MVLAPLLLGLLLLSALWNGGTAEKEEEIKPDQPFSGPLPGSLPADHRPFFAPHSSGDQLSPSQTGRSHPAHTATPQMTSAASNLLPPVAFKNTIGRIVLSEHKSVKFNCSINIPNVYQETAGISWWKDGKELLGAHHSITQFYPDEEGVSIIALFSITSVQRSDNGSYICKMKVNDREVVSDPIYVEVQGLPYFTKQPESVNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNENPERSPSVLTVAGLTETAVFSCEAHNDKGLTVSKGVQINIKVIPSPPTEVHILNSTAHSILVSWVPGFDGYSPLQNCSIQVKEAD... | Function: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis).... |
P94700 | MSEPQKSEPQKSEPQNGRGALFAGGLAAILASACCLGPLVLIALGFSGAWIGNLTVLEPYRPIFIGAALVALFFAWRRIYRPAQACKPGEVCAIPQVRATYKLIFWIVAALVLVSLGFPYVMPFFY | Function: Involved in mercury resistance. Probably transfers a mercuric ion from the periplasmic Hg(2+)-binding protein MerP to the cytoplasmic mercuric reductase MerA.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13664
Sequence Length: 126
Subcellular Location: Cell inner membrane
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P04140 | MSEPKTGRGALFTGGLAAILASACCLGPLVLIALGFSGAWIGNLAVLEPYRPIFIGVALVALFFAWRRIYRQAAACKPGEVCAIPQVRATYKLIFWIVAALVLVALGFPYVMPFFY | Function: Involved in mercury resistance . Probably transfers a mercuric ion from the periplasmic Hg(2+)-binding protein MerP to the cytoplasmic mercuric reductase MerA (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12498
Sequence Length: 116
Subcellular Location: Cell inner membrane
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Q12650 | MANAPHGGVLKDLLARDAPRQAELAAEAESLPAVTLTERQLCDLELIMNGGFSPLEGFMNQADYDRVCEDNRLADGNVFSMPITLDASQEVIDEKKLQAASRITLRDFRDDRNLAILTIDDIYRPDKTKEAKLVFGGDPEHPAIVYLNNTVKEFYIGGKIEAVNKLNHYDYVALRYTPAELRVHFDKLGWSRVVAFQTRNPMHRAHRELTVRAARSRQANVLIHPVVGLTKPGDIDHFTRVRAYQALLPRYPNGMAVLGLLGLAMRMGGPREAIWHAIIRKNHGATHFIVGRDHAGPGSNSKGEDFYGPYDAQHAVEKYK... | Function: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Catalytic Activity: ATP + H(+) + sulfate = ad... |
Q0V6P9 | MANPPHGGVLKDLIARDAPRRQELYAEAEKLPAIVLSDRQLCDLELILNGGFSPLEGFMNEKDYTGVVAENRLADGNLFSIPITLDVSKETIDEVGVKAGARIALRDSRDDRNLAIITVDDIYKPDKVKEANEVFGDNDEAHPAVKYLHHTAKEFYVGGKVEAIDRLEHYDYVGLRYTPAELRLHFDKLGWQKVVAFQTRNPMHRAHRELTVRAARARQANVLIHPVVGLTKPGDIDHFTRVRVYQALMPRYPNGMAVLALLPLAMRMGGPREAIWHAIIRKNHGATHFIVGRDHAGPGKNSKGVDFYGPYDAQDAVEKY... | Function: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Catalytic Activity: ATP + H(+) + sulfate = ad... |
P78937 | MTKALLKDLNARDAPLREQLEQEATSLPKIVLSERQFCDVELILNGGFSPLDGFMNQKDYLNVVENLRLSTGEVFPIPITLDLNESQADSLKAGDRVALLDPRDGQTVIAILTVEDKYTPDKANEAEKVFGANDRAHPAVDYLFGRAGNVYVGGKLQAVTPIRHFDFVEYRYSPAQLRSDFQRNNWNRVVAFQTRNPMHRAHRELTVRAAKQHGARVLIHPVVGMTKPGDIDHFTRVRVYEAILQRYPKGSAKLSLLPLAMRMAGPREALWHAIIRKNYGASHFIIGRDHAGPGKNSQGEDFYGPYDAQYLVEQYAQEIG... | Function: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Catalytic Activity: ATP + H(+) + sulfate = ad... |
Q4P460 | MANAPHGGVLKDLLVRDAPIAAQLRQEADTLPEIVLTERQLCDLELIINGGFSPLQGFMNQTDYNGCLDNMRLADGNLFPMPITLDVDEQQIEALKIQQGARIALRDPRDDNAIAIITVTDVYAVDKVREATAVFGSDDLAHPAITYLHKSVKNFYVGGDVQAVSKPAYYDYVALRYTPAELRQHFAKISWRKVVAFQTRNPMHRAHRELTVRAARQRQANVLIHPVVGMTKPGDVDHYTRVRVYQSLMPRYPNGMATLALLPLAMRMGGPREALWHAIIRKNFGVTHFIVGRDHAGPGKDSSGKDFYGPYDAQTLVTKY... | Function: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Catalytic Activity: ATP + H(+) + sulfate = ad... |
P08536 | MPAPHGGILQDLIARDALKKNELLSEAQSSDILVWNLTPRQLCDIELILNGGFSPLTGFLNENDYSSVVTDSRLADGTLWTIPITLDVDEAFANQIKPDTRIALFQDDEIPIAILTVQDVYKPNKTIEAEKVFRGDPEHPAISYLFNVAGDYYVGGSLEAIQLPQHYDYPGLRKTPAQLRLEFQSRQWDRVVAFQTRNPMHRAHRELTVRAAREANAKVLIHPVVGLTKPGDIDHHTRVRVYQEIIKRYPNGIAFLSLLPLAMRMSGDREAVWHAIIRKNYGASHFIVGRDHAGPGKNSKGVDFYGPYDAQELVESYKHE... | Function: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Catalytic Activity: ATP + H(+) + sulfate = ad... |
P32389 | MKQEQSHEGDSYSTEFINLFGKDTATHPSSNNGANNNGMGSTNSLDQFVATASSSSSLVTSSENRRPLIGDVTNRGNTNLYDHAVTPEILLEQLAYVDNFIPSLDNEFSNVDWNVNTTHNNANNNGADTFSSINANPFDLDEQLAIELSAFADDSFIFPDEDKPSNNNNNSNNGNDDHSNHDVLHEDPSTNNRQRNPHFLTQRRNTFLTSQYDQSKSRFSSKNKRNGNNGETNNFGDNMQNNHPFEPNFMGSPSQFPADATNMTSIDHGGFTNVDITSTENNTTGDNGVDALSNLLHRTTHTPNRSSPLSNVTSAQNSSS... | Function: Positive trans-acting factor capable of stimulating the transcription of the MET genes from the methionine biosynthetic pathway. MET4, MET28 and CBF1 are required for full induction of MET25 and MET16 gene transcription. MET4 controls as well the derepression of MET6. Required for the transcription of genes n... |
P38675 | MPPFELGDPIPSETAHAVSVSLPTWSANVGYEEGQDWVVKRMATGYPRFFIHRTIQAFAADIVATHVSTKAKRTSDITAMLFPTPTIASRCVDFIRSRAPADVCSNIEVVNLVLDMSDPEARALEPLCPSISAVIMPQDGFPFAKQYWQHSGDGVSSRRAEFCHGLFKDGLLRPDTELRNAAVSAAKPCRGPKRYQRQASLDAGGNQQTIMHGHIHRATGETAMIQETSRFLEERFGRNLDLSFVHPAKSAIKRRIAGALRSADHDLGGSPSLSEKQMSSNTRGIANLREEDIYLFPCGMNAIFHAHRALYSIRTPPGST... | Function: Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia (By similarity).
Catalytic Activity: L-cysteine + O-succinyl-L-homoserine = H(+) +... |
O74314 | MSANISYLVNPPTEVGSSIPADTEHAISVTLPTWKSNVGYEEGDPNVTTKMKSGYPRFFISAHVKDCISIIKKFPEIEILKLKDYDMFLYPSLSVAKQSAAFLESKGPIDSAEVIIYDATKGLRKHLDSIDRNRKYTEEIHIPQVYSVLFPSKYFGIAKQFWQHTGDGISSRRAAAFLHSYKKIQSISEFLVAQRSISHLKSKSRSRYASHPDLQALNTWMTNEGNQANDEMEDVSLYLEERYGRNLDLSLATAAKLVLRRRIAGTLKDEVDLQKALPKEGSQYLREVKGLSHDDVFLFPTGMSAIYNTHRILRLVLDDS... | Function: Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia (By similarity).
Catalytic Activity: L-cysteine + O-succinyl-L-homoserine = H(+) +... |
P47164 | MISRTIGESIPPNTKHAVSVCLPTWEATVGYEEGESSIINSLTTGYPRFFIHKSIKKLCEILSAKYSMEDEACLCFPSYKVANRCREFIKVKTGLSTKVRILQLCTPKPMNQEEKLWRRECKITVVFVDQEIFPVMKQYWQHSGEIVSSRMAEYILHELQVKDNLKKMETVDNGKKFMTEDENRVNEEYIETRFGRNLNFLAADKAKYLIRKRIATKVVEKIDSEGLSDLFSFEHYNESNGPFNVGSGEALDDDQLNSDIPAETITSMGESGSNSTFENTATDDLKFHVNPNTDVYLFPSGMASIFTAHRLLLNFDAKRL... | Function: Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia.
Catalytic Activity: L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-cystathioni... |
O14172 | MASKYQSVQPGGSLIIAWRAQGKKVLIVGGGVVAAGRILHVLNADAHVIVVSPKAGLCKEVAWRIQEKQVEWRDRGFLVEDLSDDVNMVLTAIDDPSLSSEIYKLCKSKKIPVNAADIPPECDFYFGSEIRNGPLQIMVSTNGKGPKLASLIRKKIESSINPATGMALEKTGLLRQKLRDIVPEPENSRKRMRWMIEICELWSLEELAMLDENLINRLLGYFPKKTPSYREITTPAYSKIDNYIWFGAIIISGAVLLKHVSKAR | Function: Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme (By similarity).
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Mass (Da): 2944... |
P15807 | MVKSLQLAHQLKDKKILLIGGGEVGLTRLYKLIPTGCKLTLVSPDLHKSIIPKFGKFIQNEDQPDYREDAKRFINPNWDPTKNEIYEYIRSDFKDEYLDLEDENDAWYIIMTCIPDHPESARIYHLCKERFGKQQLVNVADKPDLCDFYFGANLEIGDRLQILISTNGLSPRFGALVRDEIRNLFTQMGDLALEDAVVKLGELRRGIRLLAPDDKDVKYRMDWARRCTDLFGIQHCHNIDVKRLLDLFKVMFQEQNCSLQFPPRERLLSEYCSS | Function: Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme.
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Mass (Da): 31918
Sequence Lengt... |
E3HDJ8 | MCCIAGAPSLSGRERAEKEGIRFKENKGELKIGIINLMPFKEEVEYQFYAVLGRFDISVEVEFLYPENHVFKNTDGSYIKDNYYPLGELNNRNYDAIIMTGAPVELLDFQKVNYWDEIKNLIKSNKLPALYICWGAQAALYVKYGIEKFTLNEKLLGIFRHRTNKNPFVSGEFWAPHSRNTQNSSKDIKNAGLRILAESDEAGVYMASDRDYREFYISGHGEYQRERLKYEYSRDQNLFPKNYFPEDDPKKEPPMKWDSHRKEFYYKWLSHIREKKFSNISDKR | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 33537
Sequence Length: 284
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoser... |
P06721 | MADKKLDTQLVNAGRSKKYTLGAVNSVIQRASSLVFDSVEAKKHATRNRANGELFYGRRGTLTHFSLQQAMCELEGGAGCVLFPCGAAAVANSILAFIEQGDHVLMTNTAYEPSQDFCSKILSKLGVTTSWFDPLIGADIVKHLQPNTKIVFLESPGSITMEVHDVPAIVAAVRSVVPDAIIMIDNTWAAGVLFKALDFGIDVSIQAATKYLVGHSDAMIGTAVCNARCWEQLRENAYLMGQMVDADTAYITSRGLRTLGVRLRQHHESSLKVAEWLAEHPQVARVNHPALPGSKGHEFWKRDFTGSSGLFSFVLKKKLN... | Function: Primarily catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis . Also exhibits cysteine desulfhydrase activity, producing sulfide from cysteine . In addition, under certain growth conditions, exhibits significant alanine racemase coactivity .
Catalytic A... |
P85217 | HDVYGGDYRITGDDGHS | Catalytic Activity: H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate
Sequence Mass (Da): 1864
Sequence Length: 17
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.4.1.13
|
Q52811 | MKDKDSLLQNAGINTRLTHIGNDPFDYHGFINPPVVHASTVLFPNARAMETRTQKYTYGTRGTPTTDALCEAIDALEGSAGTILVPSGLAAVTIPFLGFVAAGDHALVVDSVYGPTRHFCDTMLKRLGVEVEYYHPEIGAGIETLFRSNTKLVHTEAPGSNTFEMQDIPAISAVAHRHGAVVMMDNTWATPVYFRPLDHGVDISIHASTKYPSGHSDILLGTVSANAEHWERLKEANGVLGICGAPDDAYQILRGLRTMGLRLERHYESALDIAKWLEGRDDVARVLHPALPSFPSHHLWKRDFKGASGIFSFVLAADGP... | Function: Catalyzes the cleavage of cystathionine to homocysteine, pyruvate and ammonia during methionine biosynthesis.
Catalytic Activity: H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate
Sequence Mass (Da): 43004
Sequence Length: 396
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo ... |
Q4L332 | MSLSKETEVIFDEHRGVDYDSANPPLYDSSTFHQKVLGGNAKFDYARSGNPNRQLLEEKLAKLEGGQYAFAYASGIAAISAVLLTLKANDHVILPDDVYGGTFRLTEQILNRFDIQFTTVNATQPKEIERAIQPNTKLIYVETPSNPCFKITDIRAVAAIAKRHHLLLAVDNTFMTPLGQSPLALGADIVVHSATKFLGGHSDIIAGAAITNRKDVADALYLLQNGTGTALSAHDSWTLAKHLKTLPVRFKQSTSNAEKLVAFLKEREEIAEVYYPGNSSLHLSQANSGGAVIGFRLKDETKTQDFVDALTLPLVSVSLG... | Function: Catalyzes the transformation of cystathionine into homocysteine . Can also catalyze, at low levels, the conversion of cystathionine into methionine and the conversion of methionine into methanethiol .
Catalytic Activity: H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate
Sequence Mass (Da): 42697
Se... |
P43623 | MIDRTELSKFGITTQLSVIGRNPDEQSGFVNPPLYKGSTIILKKLSDLEQRKGRFYGTAGSPTIDNLENAWTHLTGGAGTVLSASGLGSISLALLALSKAGDHILMTDSVYVPTRMLCDGLLAKFGVETDYYDPSIGKDIEKLVKPNTTVIFLESPGSGTMEVQDIPALVSVAKKHGIKTILDNTWATPLFFDAHAHGIDISVEAGTKYLGGHSDLLIGLASANEECWPLLRSTYDAMAMLPGAEDCQLALRGMRTLHLRLKEVERKALDLAAWLGNRDEVEKVLHPAFEDCPGHEYWVRDYKGSSGLFSIVLKNGFTRA... | Catalytic Activity: H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate
Sequence Mass (Da): 36971
Sequence Length: 340
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
EC: 4.4.1.13
|
O50008 | MASHIVGYPRMGPKRELKFALESFWDGKSTAEDLQKVSADLRSSIWKQMSAAGTKFIPSNTFAHYDQVLDTTAMLGAVPPRYGYTGGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVNFSYASHKAVNEYKEAKALGVDTVPVLVGPVSYLLLSKAAKGVDKSFELLSLLPKILPIYKEVITELKAAGATWIQLDEPVLVMDLEGQKLQAFTGAYAELESTLSGLNVLVETYFADIPAEAYKTLTSLKGVTAFGFDLVRGTKTLDLVKAGFPEGKYLFAGVVDGRNIWANDFAASLSTLQALEGIVGKD... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da... |
Q9SRV5 | MASHIVGYPRMGPKRELKFALESFWDGKSSADDLQKVSADLRSDIWKQMSAAGIKYIPSNTFSHYDQVLDTTAMLGAVPSRYGFTSGEIGLDVYFSMARGNASVPAMEMTKWFDTNYHYIVPELGPEVKFSYASHKAVNEYKEAKALGVETVPVLVGPVSYLLLSKLAKGVDKSFDLLSLLPKILPVYKEVIAELKAAGASWIQLDEPLFVMDLEGHKLQAFSGAYAELESTLSGLNVLVETYFADIPAEAYKTLTSLKGVTAFGFDLVRGTKTIDLIKSGFPQGKYLFAGVVDGRNIWANDLAASLITLQSLEGVVGKD... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da... |
Q8XS05 | MTTIHTLGYPRIGAQRELKFALESFWKGASTEADLRDTGRALRERHWNAQRDAGLDFVTVGDFAWYDQVLQTAALLGALPTRYGFDPAQLTLAQSFVLARGNADHAAMEMTKWFDTNYHYLVPELTPDLRFGPGTGWLFDEVREAQAAGHRVKVALLGPVTFLHLAKARGGLADKLSLLPQLLPAYAAVLKRLAAEGVEWVQIDEPALVLDLPQAWSDAYGPAYATLAAAGGPRLLLATYFEAASHHAALIRSLPVAGVHLDLVRAPQQLEAFAPWPADKVLSAGVVDGRNIWRTDLEQALARVAPLAQTLGERLWLAPS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): ... |
Q0S6X7 | MTFSFTATVLGSPRIGPNRELKKAVESYWAGRLDAEGLDALARDLRRRTWTSLRDAGLDSVPVNTFSYYDHVLDTAAMLGALPDRVAGIESDLDRYFAAARGNDTVAPLEMTRWFDTNYHYLVPEISPTTTFALDPSKVLRELEEARALDIPARPVVVGPVTFLLLSKAVGSDAPLLDRLDELVPLYADLLGRLAGAGADWVQIDEPALVADRNPKEIAAAKRAYDRLSGLELRPAILVASYFGSLGDALPAIASTGVEGIAIDLVAGSDTLATVPDLTRKHVVAGVVDGRNIWRTDLDAALASLGTLLGSTGSLAVSTS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
Catalytic Activity: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate
Sequence Mass (Da): ... |
Q8EA52 | MTEWNGEYISPYAEHGKKNEQVKKITVSIPLKVLKVLTDERTRRQVNNLRHATNSELLCEAFLHAYTGQPLPDDADLSKECPDSIPAEAKRLMDEMGIEWEDME | Function: This regulatory protein, when combined with SAM (S-adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis.
Sequence Mass (Da): 11959
Sequence Length: 104
Domain: Does not bind DNA by a helix-turn-helix motif.
Subcellular Location: Cytoplasm
|
Q72I53 | MRALRLVTSESVTEGHPDKLADRISDAILDALIAQDKKARVAAETLVTTGLVFVAGEITTEGYVDIPNLVRKTVREVGYTRAKYGFDADTCAVLTAIDEQSPDIAGGVNLSYEWRVLKSTDPLDRVGAGDQGLMFGYATDETPELMPLPITLAHRLTMRLAEVRKTGLLPYLRPDGKAQVTVVYEGDKPLYVKTVVVSAQHSPEVEQEQLREDLIREVVRQAIPPEYLKDGETEYLINPSGRFILGGPHADTGLTGRKIIVDTYGGAVPHGGGAFSGKDPTKVDRSASYYARYMAKNIVAAGLARRALVELAYAIGKARP... | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the en... |
Q73JR4 | MKNDINYFTSESVSEGHPDKLCDQISDAVLDACLRDDPESHVACETFASTALVLVGGEITTNTYVDIQEIARSIAEEIGYTNTDFGLDCHSMAVMNMIHSQSPDISQGVDGTGLDEYKGQQGAGDQGMMFGFACKETPELMPAPIMFSHSVLRYAAKLRKEKVIPWLRPDSKTQITVKYEGFKPIKIDTVVLSHQHYPDVQYDELKDTLINRVIKPVLGPTGLLADDTKYFINPTGRFVIGGPFGDTGLTGRKIIVDTYGGMGRHGGGAFSGKDPSKVDRSAAYMARYIAKNVVAADLARRCEVQLAYAIGVPFPVAVRV... | Cofactor: Binds 2 divalent ions per subunit.
Function: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the en... |
Q8NSN2 | MSHTASTPTPEEYSAQQPSTQGTRVEFRGITKVFSNNKSAKTTALDNVTLTVEPGEVIGIIGYSGAGKSTLVRLINGLDSPTSGSLLLNGTDIVGMPESKLRKLRSNIGMIFQQFNLFQSRTAAGNVEYPLEVAKMDKAARKARVQEMLEFVGLGDKGKNYPEQLSGGQKQRVGIARALATNPTLLLADEATSALDPETTHEVLELLRKVNRELGITIVVITHEMEVVRSIADKVAVMESGKVVEYGSVYEVFSNPQTQVAQKFVATALRNTPDQVESEDLLSHEGRLFTIDLTETSGFFAATARAAEQGAFVNIVHGGV... | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39103
Sequence Len... |
Q6A6X6 | MSTDITPSSAPQCPDHIVFEHVTKEFRTRSGTVRALDDVSLAIKRGSISAVIGHSGAGKSTLVRLINGLETPTRGRVLVDGTDVSQLSDKAMRPLRADIGMIFQQFNLFGSRTIYDNVAYPLKLAHWKKADEKKRITELLSFVGLTSKAWDHPDQLSGGQKQRVGIARALATKPSILLADESTSALDPETTADVLSLLKRVNAELGVTVVVITHEMEVVRSIAQQVSVLAAGHLVESGSARQVFAHPQSETTQRFLATIIGQHPNGEEQARLQSENPHARLVDVSSVASHSFGDALARISHTGASFQIVHGGVIEVHDGS... | Function: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39015
Sequence Len... |
P30750 | MIKLSNITKVFHQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVLVDGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEVKRRVTELLSLVGLGDKHDSYPSNLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQERLQAEPFTDCVPMLRLEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQ... | Function: Part of the ABC transporter complex MetNIQ involved in methionine import . Responsible for energy coupling to the transport system . It has also been shown to be involved in formyl-L-methionine transport .
Catalytic Activity: ATP + H2O + L-methionine(out) = ADP + H(+) + L-methionine(in) + phosphate
Location T... |
Q5Z1C4 | MSTDQSPCPSATGAELLPPPDGTLAIVPVGDIRLESGAVIPDVHLGVQRWGELSPGLDNVVLVEHALTGDSHVVGPADDVHQLPGWWNGMVGPGAPMDTDEWCVIATNVLGGCKGSTGPGSTAPDGKPWGSRFPAISIRDQVTAEAALFDRIGIHRLAAVVGGSMGGMRVLEWMVGAPERVAAALVLAVGARATADQIGTQTTQIAAITADPDWQGGDYHDTGRAPTTGMGIARRIAHLTYRTEDELDHRFANHAQDGEDPFDGGRWAVQSYLEHQAEKLCRRFDPATYVLLTEAMNRHDVGRGRGGVAAALAATPVPCV... | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 40409
Sequence Length: 382
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoser... |
Q4FP51 | MNINVNIKNIIIDKPLKLDCGQTINNYSLAYETYGSLNENKDNAILIFHALTGDQFVSGINPITKKEGWWSYAVGSGKAIDTDKYFVICANVIGGCMGSYGPSEINPDTNKKYGTTFPVITINDMVNAQFNLLNFFNIEKLFAVMGGSMGGMQTLQFVNNFPDKAKVAIPIACTASHSAQNIAFNELGRQSIMADANWENGDYSNQNKNPNKGLSVARMAAHITYLSKNGLQEKFGRKLQERDDLKFGFDADFQIESYLRYQGSVFVDRFDANSYLYITRAMDYFDLVKEHHGNLSKAFEKTKTKFLIISFTSDWLYPTS... | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 41643
Sequence Length: 372
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoser... |
K4ICC9 | MPEIFKYQDPFQLENGEVLPELEVSYSTLGKLNKEKSNVIWVCHALTANAQPEDWWRGLIGNEKGIDTEKYFIVCANIIGSCYGSTNPKSINPETGEVYGLNFPLFSIRDVTKSLELLSEALEIEHIQFLIGGSMGGMQAMEWAIEKPDKIKNLILLATNAKHSSWGIALNETQRMAIEADSTFYKKETNSGKKGLEAARAIALLSYRNYNTYRHTQVDQEHTADHFRASTYQKYQGEKLSKRFNAKCYWYLSKAMDSHNVGRNRGDCKKALAKIKAETLVIAVQSDLLFPVEEQRFLAQYIPKGKLEIIDSIYGHDGFL... | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 38209
Sequence Length: 336
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoser... |
Q98G09 | MAALRAGKTNNEADQPSSPVLRFGADKPLKLDAGTLLSPFQIAYQTYGTLNDARSNAILVCHALTGDQHVANTNPVTGKPGWWEVLIGPGRIIDTNRFFVICSNVIGGCLGSTGPASTNPATGKPYGLDLPVITIRDMVRAQQMLIDHFGIEKLFCVLGGSMGGMQVLEWASSYPERVFSALPIATGARHSSQNIAFHEVGRQAVMADPDWHGGKYFENGKRPEKGLAVARMAAHITYLSEAALHRKFGRNLQDREALTFGFDADFQIESYLRHQGMTFVDRFDANSYLYMTRSMDYFDLAADHGGRLADAFAGTKTRFC... | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 42364
Sequence Length: 389
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoser... |
Q2S5A6 | MSQTLTVPTLTLENGTTLRDVPVAYRTWGTLNATGTNAVLVCHALTGDTNVADWWGGLLGPGRALDPTEDFVVCLNVPGSPYGSVAPVTVNPDTGERYGAGFPPFTTRDTVRLHRRALETLGVQRVACAVGGSMGGMHVLEWAFEATDDGAPFVRSLVPIAVGGRHTAWQIGWGAAQRQAIFADPKWRDGTYPPDDPPTNGLATARMMAMVSYRSRPSLDGRFGRDAMPEQDGTPYAVESYLHHHGNKLVDRFDANCYVALTRQMDTHDVARGRGDYAKVLRAIEQPSLVVGIDSDVLYPLSEQEELAEHLPSATLEVLS... | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 38064
Sequence Length: 352
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoser... |
E0UR96 | MSLNLQTYTEHFTNPLYLESGRILEPYDITYETYGTMNEDKSNVVVVCHALTGSHHAAGLYEDETKPGWWDGFIGSGKAIDTDKYFVICSNVIGSCFGSTGPMSLQHPYQEPYRYKFPVVSIKDMVKAQRILFDRLDIHRVHAIVGGSMGGMQALQFAIHYPNFANKIIALATTHATQPWAIAFNKVAQESILNDPDFKQGYYDPDLLKEQGLSGMAVGRMAGHISFLSHESMREKFGRDYKLTDGLYELFGKFQVESYLEYNGYNFTKWFDPLAYLYITKAINIYDLSRGFDSLAEALKRVTSALYLVSFKNDLLFKNF... | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 41872
Sequence Length: 368
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoser... |
Q67NS3 | MNAAPVPILLTQRRYARVATPENPLVLESGQRLTDVTLCYEVFGRLNPAGDNAILVCHALTGDSHVAGRYRPDDPKPGWWDDAVGPGKALDTDRYCVICSNVLGGCQGSTGPSSVNPATGRPYGLDFPLVTVRDMVRAQARLLDLLGVRRLLAVIGGSLGAMQALEWAATYPDRMRGIIPIGGAGRFHPQGIAFNEVQRQAILNDPGFLGGQYYGTPGPVRGLATARMLGMITYRSDESMWTQFGRNPQGEANPLHQGFAVAYQVESYLHYQGRKLVERFDANSYLYLTRAMDLMDLGRGRGSYEEAHARIQARVLAVGI... | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 42255
Sequence Length: 383
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoser... |
Q47L17 | MSHDTTPPLPATGAWREGDPPGDRRWVELSEPLPLETGGELPGVRLAYETWGSLNEDRSNAVLVLHALTGDSHVVGPEGPGHPSPGWWEGIIGPGLALDTDRYFVVAPNVLGGCQGSTGPSSTAPDGRPWGSRFPRITIRDTVRAEFALLREFGIHSWAAVLGGSMGGMRALEWAATYPERVRRLLLLASPAASSAQQIAWAAPQLHAIRSDPYWHGGDYYDRPGPGPVTGMGIARRIAHITYRGATEFDERFGRNPQDGEDPMAGGRFAVESYLDHHAVKLARRFDAGSYVVLTQAMNTHDVGRGRGGVAQALRRVTAR... | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 40833
Sequence Length: 379
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoser... |
Q9RA51 | MSEIALEAWGEHEALLLKPPRSPLSIPPPKPRTAVLFPRREGFYTELGGYLPEVRLRFETYGTLSRRRDNAVLVFHALTGSAHLAGTYDEETFRSLSPLEQAFGREGWWDSLVGPGRILDPALYYVVSANHLGSCYGSTGPLSLDPHTGRPYGRDFPPLTIRDLARAQARLLDHLGVEKAIVIGGSLGGMVALEFALMYPERVKKLVVLAAPARHGPWARAFNHLSRQAILQDPEYQKGNPAPKGMALARGIAMMSYRAPEGFEARWGAEPELGETYLDYQGEKFLRRFHAESYLVLSRAMDTHDVGRGRGGVEEALKRL... | Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Sequence Mass (Da): 42251
Sequence Length: 380
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoser... |
Q69Z36 | MPSSLFADLERNGSGGGGGGGGGGGGGGSGGGETLDDQRALQLALDQLSLLGLDSDEGASLYDSEPRKKSVNMTECVPVPSSEHVAEIVGRQGGSGRDGDRRGFSISPTPSLEPWLPGCKIKALRAKTNTYIKTPVRGEEPVFVVTGRKEDVAMARREIISAAEHFSMIRASRNKNTALNGAVPGPPNLPGQTTIQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEAHIALRTGGIIELTDENDFHANGTDVGFDLHHGSGGSGPGSLWSKPTPSITPTPGRKPFSSYRNDS... | Function: RNA-binding protein. May be involved in post-transcriptional regulatory mechanisms (By similarity).
PTM: Phosphorylation at Ser-494 creates a docking site for 14-3-3, which stabilizes the protein and modulates its ability to bind RNA.
Sequence Mass (Da): 61781
Sequence Length: 601
Domain: Binds RNA through it... |
A1L3F4 | MPSSLFADMERNGSGGGGGETLDDQRALQIALDQLSLLGLDNDESAMYDNEPRKKSINMTECVQVPSSEHVAEIVGRQGCKIKALRAKTNTYIKTPVRGEEPVFVVTGRKEDVALARREIISAAEHFSMIRASRNKNAAALNGGSVPAPPNLPGQTTIQVRVPYRVVGLVVGPKGATIKRIQQQTHTYIVTPSRDKEPVFEVTGMPENVDRAREEIEAHIAVRTGGLIEVADENDFHANGTDVGFDLHGSLWSKSNQSSGSRKALSNYRNDSSSSLGSASTDSYFGGTRMADYSPPSPDLSYTNNNNNNNGNGYVYSTGI... | Function: RNA-binding protein. May be involved in post-transcriptional regulatory mechanisms (By similarity).
Sequence Mass (Da): 54164
Sequence Length: 507
Domain: Binds RNA through its KH domains.
Subcellular Location: Cytoplasm
|
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