ids
stringlengths 6
10
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stringlengths 11
1.02k
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stringlengths 108
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C1F686 | MKYLWVALGGALGALARYTVGVWIYERLGTRFPYGTFAINVTGCFLIGLALTVLDAHMDLSPAWRLAIPTGFIGAYTTFSTFEYETLRAAQHGQMGTAVLYFGSSLALGILAVWLGMVVGNRIVA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13514
Sequence Length: 125
Subcellular Location: Cell inner membrane
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B7J9Q0 | MFATFGFIALFAVLGAWARYGQTLLVQAAFGRGFPWATLSINVLGCFLMGFLFFETLERISVSPELRTGMLTGGLGAYTTFSTFSLETLVLFENGEAVKGLLYMFTSLFLCVGAAFAGAWISHST | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13553
Sequence Length: 125
Subcellular Location: Cell inner membrane
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A4STL2 | MQTWLFVAAGGAIGACLRFGISELMALLLGRHFPYGTLVVNVVGSFIMGIAFALISHGHVVEHPMKPLLMVGILGALTTFSSFALDTVVLAQQGAYLKAVLNMGLNLSLCLAMVLLGMQLVASRV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13188
Sequence Length: 125
Subcellular Location: Cell inner membrane
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Q21Y62 | MRLMISVLAICIGASLGALARWRLGLWLNPGAVLPLGTLAANLIGGYLIGICVAVFQALPNLDPVWRLALITGFLGGLTTFSSFSAEVVGMLGQQRYALGFGTAGLHLFGSLLLTLAGIKTATFLIAFNT | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13564
Sequence Length: 130
Subcellular Location: Cell inner membrane
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Q4FV70 | MQWLAIGLGAAFGACLRGWLARFNPLHHWIPLGTLGANVLGGLLIGLALVWFERMGSGLSPNIRLFVITGFLGGLTTFSTFSAEVFTFIHHGRLLAALGLVGLHVGMTLLATALGFYCFKLVL | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13169
Sequence Length: 123
Subcellular Location: Cell inner membrane
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A9WPV3 | MIVIFVGLAGVLGALMRFGLDSFFAQRGRFAHGQAHHFPLATLSVNVLGSFIIGLAGGFASHAELSPDWHSAISIGIAGGLTTFSSFAVATVSLWQLGNKFSAMVNIGLNLVLGLGAAWLGLSLAA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12969
Sequence Length: 126
Subcellular Location: Cell membrane
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Q98N26 | MFNLLLVVVGGGIGAGIRHLTNMGALRLVGPNYPWGTMAINIVGSFAMGLFIAILARRGGSNEVRLFVATGIFGGFTTFSAFSLDFATLWERGATLPAFGYALASVIGAIIALFLGLWLARSLP | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13022
Sequence Length: 124
Subcellular Location: Cell inner membrane
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Q92QE1 | MNHILLVGAGGALGSVLRYLVGLWMLQRAGPAFPWGTLFVNVTGSFLIGFLAEFIMHKMGASPEMRVFLITGVLGGYTTFSAFSLDAIALLEHGQTMSGLAYIVASVGLSMLAVFAGLALMRAMV | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13200
Sequence Length: 125
Subcellular Location: Cell inner membrane
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Q7UHW8 | MTFVSDLFAIALGGSIGAVLRYLITLTVVSAPLSGWLTLHGSVGTTLANLLGCCALGGLFQFSQALVASDWVATGWAASLAHPRTLLAVRIGVLGSLTTFSTLIGETAVFASQGRILASSMLLGINVIAGWCLFWAAAAVVRNWTS | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15085
Sequence Length: 146
Subcellular Location: Cell inner membrane
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B6IQX6 | MKMILAVAAGGGLGAVARYLTGVGLGHWLGTAYPWATMTVNVTGSFAMGVLAGLGAHVWQPAPELRAFLMVGVLGGFTTFSSFSLDVALLVERGAIGAAAAYVAASFLLSVGGLFAGLALIRTAVA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12629
Sequence Length: 126
Subcellular Location: Cell inner membrane
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P61394 | MAYLLVFVGGGLGAMFRHFINTLSGRLLGTAFPYHTFFINVTGSIVMGLIAGYLAFKGGSSQHFRLFLMTGILGGYTTFSAFSLDAALLYERGAVGLAVVYVLGSVVLAIAGLFGGMALIRAMT | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13057
Sequence Length: 124
Subcellular Location: Cell inner membrane
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Q4WAZ3 | MLGRHECTISESVSALDPTAQEPEYTLVPSTSRDLVRDMTLNMEDAQAHLKEHGWVKIPAVLSKAEAEDALSRLWEAKAASEARGECTFQPILDPNPANVRVFYLPELDAYWRDMLVNPTALDLAKSLLGDQLLVSNFSANIARPGAESMALHSDQSIVLPAPWLDVWAVNVIWCLTRMTKENGATLYIPGSNKWTTWEDVPDNAPDLLVPFEADAGDIVVIDGRLWHTSGSNVTEDEDRAILFAYYSAPHMRPLTNWSAKLPKELQETLSPQLKELLALSHIGYVVKGDLTYMAQKYPSEKGTTAVSA | Function: Dioxygenase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) . Within the pathway, the dioxygenase af480 acts as a 5-dehydro-6-demethoxyfumagillol dioxygenase that hydroylates 5-keto-demethoxyfumagillol at position C-6 . The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (Probable).
Catalytic Activity: 2-oxoglutarate + 5-dehydro-6-demethoxyfumagillol + O2 = 5-dehydro-6-demethoxy-6-hydroxyfumagillol + CO2 + succinate
Sequence Mass (Da): 34231
Sequence Length: 309
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.14.11.82
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Q4WAZ6 | MAYELSTLQLSCVAFVAFMAVLVFRTRTRNLKQNVPPGPRPLPIIGNFFDLPPKGQPEYLHWFKHKDAYGPVSSINVMGTTLVIFHDKDAAHAVMGKKAQKTSARPQLNFAQLCGFENFLITHQYNDKYRLHRKMVHQEIGTKGLSAGFRPIQEQESIRFILQTFNRPDDILQHLKTLAAAIVLKITYGYSIERKGQDPLVELIEHAMENLSQAFVPLAWAVDSVPAIKYLPDWFPGMSYRKTARKWRAINEAAAELPYDFVKRQMAHKAHQPSYVSNLLEKHMIKSEDNKINVSAADEEAIKWTAVSLYAAGSDSTVAIIHSVICGLVMFPEVVTRAQEEIDRVVGSDRLPNFDDRTNLPYVDGIIKEAWRWNPVGPMGLTHKSEEDLVCGEYLIPKGSYLLPSLWWFLNDPKEYPEPRVFKPERYMEPFNHPDPSEIAFGYGRRSCAGRYFADASVYITVVQLLAVFNVRKARDDQGNEIPVTLQAIPGMVNRPAPFQFKVEPRSQHHIDLLRRIESEQIPEVSHASLLKPSTV | Function: Multifunctional cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) . Within the pathway, the multifunctional cytochrome P450 monooxygenase af510 acts as a 2,4,6-trichlorophenol monooxygenase that first performs the C-H hydroxylation at the bridgehead C5 position to yield 5R-hydroxyl-beta-trans-bergamotene . Subsequently, a four electron oxidation initiated at C-9 coupled to cleavage of the cyclobutane C5-C8 bond of the bicyclo[3.1.1] core yields the epoxyketone intermediate 5-keto-cordycol . An additional epoxidation reaction also catalyzed by af510 then furnishes the characteristic bisepoxide ketone 5-keto-demethoxyfumagillol . The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (Probable).
Catalytic Activity: (+)-exo-beta-bergamotene + 3 O2 + 2 reduced [NADPH--hemoprotein reductase] = 5-dehydro-6-demethoxyfumagillol + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60965
Sequence Length: 536
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.14.14.184
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Q4WAZ4 | MLGLPNELSGSQVPGATEYEPGWRRVFKVEDLPGLGDYHIDNQTAVPTSIVCVIALAAAMDISNGKQANSIELYDVTIGRPIHLGTSPVEIETMIAIEPGKDGADSIQAEFSLNKSAGHDENPVSVANGRLRMTFAGHELELLSSRQAKPCGLRPVSISPFYDSLREVGLGYSGPFRALTSAERRMDYACGVIAPTTGEASRTPALLHPAMLEACFQTLLLAFAAPRDGSLWTIFVPTQIGRLTIFPNSSVGINTPASVTIDTHLHEFTAGHKADLPMIKGDVSVYSSEAGQLRIRLEGLTMSPIAPSTEKQDKRLYLKRTWLPDILSGPVLERGKPVFCYELFGLSLAPKSILAATRLLSHRYAKLKILQVGTSSVHLVHSLCRELGSSMDSYTIACESDSSMEDMRRRLLSDALPIKYVVLDIGKSLTEGDEPAAGEPTDLGSFDLIILLKASADDSPILKRTRGLIKPGGFLLMTVAATEAIPWEARDMTRKAIHDTLQSVGFSGVDLLQRDPEGDSSFVILSQAVDHQIRFLRAPFDSTPPFPTRGTLLVIGGASHRAKRPIETIQNSLRRVWAGEIVLIRSLTDLQTRGLDHVEAVLSLTELDQSVLENLSRDTFDGLHRLLHQSKIVLWVTYSAGNLNPHQSGAIGLVRAVQAETPDKVLQLLDVDQIDGNDGLVAESFLRLIGGVKMKDGSSNSLWTVEPELSVQGGRLLIPRVLFDKKRNDRLNCLRRQLKATDSFEKQSALARPIDPCSLFSPNKTYVLAGLSGQMGQSITRWIVQSGGRHIVITSRNPDKDDLWTKELEQRGAHIEIMAADVTKKQEMINVRNQILSAMPPIGGVANGAMLQSNCFFSDLTYEALQDVLKPKVDGSLVLDEVFSSDDLDFFLLFSSISAVVGQPFQANYDAANNFMTGLVLQRRARNLPASVINLGPIIGLGFIQNIDSGGGSEAVIATLRSLDYMLVSERELHHILAEAILIGKSDETPEIITGLETVSDNPAPFWHKSLLFSHII | Function: Stereoselective keto-reductase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2) . Within the pathway, the keto-reductase af490 acts as a 5-dehydrofumagillol 5-reductase that stereoselectively reduces 5-keto-fumagillol to 5R-hydroxy-seco-sesquiterpene . The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (Probable).
Catalytic Activity: fumagillol + NADP(+) = 5-dehydrofumagillol + H(+) + NADPH
Sequence Mass (Da): 110955
Sequence Length: 1017
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.1.1.437
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P04953 | MKSLQKGFTLIELMIVVAIIGILAAIAIPQYQNYIARSQVSRVMSETGQMRTAIETCLLDGKEGKDCFIGWTTSNLLAAAGGSTTNNATAADPGQGGLNITYALESTAENKIEATFGQNAAATLHGKKLTWTRSPEATWSCSTDVDEKFKPTGCKK | Function: Major component of the type IV fimbriae that plays an essential role in twitching motility, natural transformation, and protease secretion.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16637
Sequence Length: 156
Subcellular Location: Fimbrium
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Q9VZW5 | MSGTAVARLLLRLELPSPGVMPPPPTDYDYGGPISDDEFLASAMATEGPTVRYDLFPQNNSQPTLQIVLNHTEVQTDLQYPHYEDLGLDPDPNWTRICEDVYNPLLENNRIEFWVCGVLINIVGVLGILGNIISMIILSRPQMRSSINYLLTGLARCDTVLIITSILLFGIPSIYPYTGHFFGYYNYVYPFISPAVFPIGMIAQTASIYMTFTVTLERYVAVCHPLKARALCTYGRAKIYFIVCVCFSLAYNMPRFWEVLTVTYPEPGKDVILHCVRPSRLRRSETYINIYIHWCYLIVNYIIPFLTLAILNCLIYRQVKRANRERQRLSRSEKREIGLATMLLCVVIVFFMLNFLPLVLNISEAFYSTIDHKITKISNLLITINSSVNFLIYIIFGEKFKRIFLLIFFKRRLSRDQPDLIHYESSISNNGDGTLNHRSSGRFSRHGTQRSTTTTYLVATGGPGGGGCGGGGGNNSLNNVRLTQVSGSPGLVKIKRNRAPSPGPVVYFPAREMQRSASTTNSTTNNNTSIGYDWTLPDSKKLGHVSSGF | Function: A receptor for the FMRFamide peptides . Reacts with high affinity to FMRFamide and intrinsic FMRFamide-related peptides . By stimulating intracellular calcium signaling through the inositol 1,4,5-trisphosphate receptor, Itpr, in dopaminergic neurons, may be involved in the maintenance of neuronal excitability and in the regulation of flight bout duration .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61755
Sequence Length: 549
Subcellular Location: Cell membrane
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A3DCX5 | MRIVFMGTPEFAIPSLEMLVRERYEVAAVVTQPDKPKGRGKKTAMPPVKEFAIKNNIEVLQPSKVKTPEFVSTIRELRPDLLVTAAYGKILPQEVLDIPPYGCVNVHGSLLPKYRGAAPINWAIINGEKVTGITTMYTDAGMDTGDMLLKAEIEISDDMTAGELHDKLACLGAEVLRETLKKIEDSTLQRIPQPHEQATYAPMLDKTVGCINWSKSARDVHNLVRGTNPWPVAFTYYKGQKMKVWVTSVLDEENHNFTPGTILKVGKDGLVVACGVGKVVIKEVQFDSSRRMTVEEYICGHKVGEGEVLGQ | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 34408
Sequence Length: 311
EC: 2.1.2.9
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A1TW87 | MKIIFAGTPEFARVALERLLAAGAEVPLVLTQPDRPAGRGMKLQASPVKQCALAHGIAVAQPRGLRLDGRYAEDAAAARAALEAAGADAMVVAAYGLILPQWVLDLPRLGCLNIHASLLPRWRGAAPIHRAIEAGDAETGVTIMQMDAGLDTGAMLLIEKTAIAPRETTATLHDRLADLGGRLIVEAMELAACGGLAATPQPAEGVTYAHKIEKAESAIDWKLPAAAIDRRVRAFDPFPGASTQCSAETIKVWGCEPLQVPPPEGAQPGEILQVDDAGVDVACGGPDGAAGVLRLTVLQRAGGKRLPVGDFLRGHPLAPGMVLGGGAGA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 33978
Sequence Length: 329
EC: 2.1.2.9
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Q6F6P9 | MKIIFAGTPDFAATALDALIKTPHDIVAVYTQPDRKAGRGQKLTPSPVKQLALEHNLPVLQPLHFKSSTEEGLAAQAELAAFNADVMVVAAYGLILPQIVLDTPKYGCLNIHGSLLPRWRGAAPIQRAIAAGDAETGVTIMKMAAGLDTGDMMFKTYCPIEASDTSASLYEKLAAQGAEAICTVLECEQQLQKFLAEREVQDENQTVYAHKLVKAEAQIDWTQDAIQIDRNIRAFNPWPVAFIPLDDKNNLRVWESTVSKLIAPDAEAGKIIAMDKHGIHVACGTGVVCLTALQWPGGKALNPVQIIQTQKLNIGQVLA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 34511
Sequence Length: 319
EC: 2.1.2.9
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B7I2C3 | MKIIFAGTPEFAATALAALLKTSHEIIAVYTQPDRKAGRGQKLTPSPVKQLALEHNIPVYQPLHFKASTEEGLAAQQELAALGADVMVVAAYGLILPQAVLDTPKYGCLNIHGSLLPRWRGAAPIQRAIATGDDETGITIMQMAAGLDTGDMMYKTYCPIASEDTSATLHDKLAAQGATAICAVLESEETLQKYLAEREVQDESLTVYAHKLVKSEARIDWSMNAVQVDRNIRAFNPWPVAFIQLDENNALRVWNSIISSQSKVNAQAGEIIAIDKQGVHVACGENTFICLTSVQWPGGKALNAQQIAQTQKLHVGQILP | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 34637
Sequence Length: 320
EC: 2.1.2.9
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C1F542 | MKLVFCGTPAFAVPTLEALLQAGHDVALVVTQPDRPSGRGMQVLAPPVKQTALAAGLPVVQPEKIKNNLEFRAQLEAIAPDAIIVVAYGRIIPKWMLDLPRYGNLNLHASLLPKYRGAAPIQWAVAMGETVTGATTMRIDEGLDTGDMLLQDEMEIPPAMTAEELFPLLAEMGAPLMVETLAGLEQGTVTPQKQDEAQATLAPILTREDGRVDFARSAAEIYNRWRGFQPWPGAWTMLGGKKLTLHRMLLAEREDRAEPGMVRVHAGRLFFACGDGGWLEIAELQLEGKKRMPVTDFLRGNTLAPETRLGA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 33935
Sequence Length: 311
EC: 2.1.2.9
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B7J3C1 | MTEKQRIVFAGTPEFARITLAELRQGPEAVVGVFTQPDRPAGRGRTLQASPVKQEALAAGIPVFQPESCKTGEALELLRSLAPDLLIVVAYGQILPQAILALPTRGAINVHASLLPAWRGAAPIARAIAAGDKESGVAIMQMEAGLDSGPVLWEERLPIAADDTAASLHDRLARLGGKALRHVLDDLWAERLKPVPQDPALVTYAHKLKKEEALLDWRLPAATLERLVRAFNPSPVAHTLFRDKGLRVWQARVLGAGGDQAPGSISAVEKDGVVVTCGEDRLQLLAVQPAGKGVLSGSDFARGYRPQVGEVLG | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 33364
Sequence Length: 313
EC: 2.1.2.9
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Q8K974 | MKKLTIIFAGTAYFSMRYLDALTKSEHKVIAVITQPDRPSGRGQKIIFSPVKILSIKRNIPIFQPSELKNEKIQREIFNLNADMMIVVSYGKLIPKEILTMFPKGCINVHTSLLPRWRGATPIQSAILFGDKETGISIIKMNEKMDAGTIINSVKCNILPNDTTETLTFKLIEIGIQVLLKTLYYINKNIVVEKEQNEKHATFSKKISKKDALLNWNTEAYLLERLIRAFNPWPVCYFIVNQIAIRVWQAKIIPTVMKSACVGEIVAFNKNGIQINTAHQILNLQKIQFPGKKIINVEKIISSKKHWFHIGKII | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 35831
Sequence Length: 314
EC: 2.1.2.9
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P59557 | MILNTLNSLKIVFAGTDKFSKDHLKILVTNTTHKILGVITKPDQPLGRGKQITSSLTKKLAKKLKIPVFQPTALNTSTFYNQIYNLNADIIIVVSYGKIIPQLILNIFPLGGINVHTSLLPRWRGPSPIQSALLNGDKLTGITIIKMNNNIDTGDIIYSSSCIINKSDTSVTLQNKLKILSCQGLIQVLKNFKSSYFPIRQSNLATYSNKINKEDAKLIWLKSAIQLERSIRAYNPWPICYFKINNQLSIKVWSANVIIHFNQHKYQIGEIILINKHGMQIKTSKNILNITTVQLPGKKIMHANNLCNSKNKWCIPGTKLTNT | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 36304
Sequence Length: 323
EC: 2.1.2.9
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P44787 | MKSLNIIFAGTPDFAAQHLQAILNSQHNVIAVYTQPDKPAGRGKKLQASPVKQLAEQNNIPVYQPKSLRKEEAQSELKALNADVMVVVAYGLILPKAVLDAPRLGCLNVHGSILPRWRGAAPIQRSIWAGDVQTGVTIMQMDEGLDTGDMLHKVYCDILPTETSTSLYNKLAELAPSALIDVLDNLENGKFIAEKQDGSQSNYAEKLSKEEAQLNWSLSAMQLERNIRAFNPWPIAYFSTEDKDGNAHTLKVYQAKVLPHQDKPAGTILSADKNGIQIATVDGVLNLLQLQSAGKKPMSAQDLLNGRAEWFTIGKVLA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 34789
Sequence Length: 318
EC: 2.1.2.9
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Q9K9Y6 | MKIVFMGTPDFSVPVLRRLIEDGYTIAAVVTQPDRPVGRKRVLTPPPVKVEAEKHQIPVLQPEKIRDEAELERLFSFEPDLIVTAAFGQILPNALLEYPKHGCINVHASLLPKYRGGAPIHQAIIDGEKETGITIMYMAEKLDAGDILTQVTVPIADDDHVGSLHNKLSEAGAALLAKTIPPLIKGELQSIPQDDQLATFAPNITREKEEIDWRKEGERIYNQIRGLHPWPVAYTLWNGKPMKIWWAEKVSSPKKEAPGTVIALEENGFLVATGDETALKVTDLQPAGKKRMLARDFLRGAGSQLSVGSVLGGQDGS | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 34823
Sequence Length: 317
EC: 2.1.2.9
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B8CWS7 | MNIVFMGSPDFAVPGLEKLYNEPGITIKAVVTQPDRKKGRGHKLRPTPVKQMAHKLGLKVLQTDNINREEFITNLRDLSPEAIVVVAFGQKLGKKVLELPSYGCINLHASLLPRYRGASPIHRAIINGDKVTGVTTMYMDEGWDTGDIIYKKEVKINREDTAGTLHDKLASIGGDLLVKTLNDIEKGVAPREKQSEDKASYAYKIDRKIGELDWSRSSEDIFNLVRGVNPWPGAYTTWKGKLLKIWWVEPLKLTVTENDKKMEAGEVITASQEDGIIVKTGDDAVKIIELQLAGRKKITADKFVLGYNIKEGDKLG | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 35194
Sequence Length: 316
EC: 2.1.2.9
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C4K6Y1 | MSESLKIIFAGTPDFSACHLQHLLSHRQKILGVFTQPDRPAGRGKKLAFSPVKILATQHHIPVYQPHSLGLKEEQQSILDLDADVMVVVAYGLLLPQAVLNMPRLGCINVHPSLLPRWRGAAPIQRAIWAGDQETGVTIMQMDSGLDTGNMLYKTVYPIQPDDTGASLQAKLAALGSQDLLLTLKKMAEGKMHGETQDEQKTTYAHKLTKKEARLDWLLPAAHLERCVRAFNPWPVSYFIINEQIIKVWEAQAMPDSQQVSHLQPGTVLKADKNGIQILTSEGVLNMTKFQLPGKKIISAWDFLNSRNEWFQIGKQLLS | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 35594
Sequence Length: 319
EC: 2.1.2.9
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B0TGS9 | MRLVFMGTPDFAVPTLEAIVAAGHEVALVVTRPDRPRGRGQKPQPSPVKEAALRLGLPVDHPACLDNEFVQKLKDLGVEAGVVVAFGRILPPRLLDAFPQRWINVHASLLPKYRGAAPIHRAVIDGEKETGITTMLMSEGLDEGDMLLKRSLAIGPDDTTGQVHDALAELGARLLVETLAAMEAGRLQPQPQDGSQASYAPMLARADEQVDWSAPAEAVHNRVRGMNPWPGAFTMDEGKILKILRGRLRHEGLPLPDPTGSAAHPGEILQIVGDEVAVATGAGVYWLSEVRPAGGKTMTAGAYARGRRIGPGFRFG | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 33843
Sequence Length: 316
EC: 2.1.2.9
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P56461 | MRIVFMGTPGFAEVILRALVGDKDIEVVGLFTQMDKPFGRKKELKAPETKTYILENHLNIPIFQPQSLKEPEVQILKDLKPNFIVVVAYGKILPKEVLTIAPCINLHASLLPKYRGASPIHEMILNDNKIYGISTMLMDVELDSGDILESASFLREDYLDLDALSLKLAHMGAALLLSTLKNFSSITRKSQDHMQASFCKKITKSDGLVGFKDAKSLFLKSLAFKSWPEIFLENGLKLLEVELVENEKSHKEGEILEIDEKGVLVGCLKGSVRIARLQAVGKKPLKAKDYLNGKRLKIGGILA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 33730
Sequence Length: 303
EC: 2.1.2.9
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A9B2Z9 | MRILYLGTPEIAVAPLELLHASGHEIVGVVTQPDRPAGRKNVLTAPPVKLAAERLGIPVFQPETLKDPAAVARLRAFEPEVGVVAAYGEILRKQVLAIPALGYLNIHPSILPLYRGPAPVTGAILAGDDLVGVSIIKLTAKMDAGPILGQMVMPLANDARAGEWTAQLMRQGGELLAQVLPAYAAGQIQAQIQDDSQASYTQMISKNDGLINWNLPALVIERMTRAYDPWPGTAVKLNDQPFKILRAKAHTSWSGTIQPGTLFEQQGQILVATGSGALELLEVQPAGKRPMAANDWRRGAKDIEQL | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 32837
Sequence Length: 306
EC: 2.1.2.9
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Q96DP5 | MRVLVRRCWGPPLAHGARRGRPSPQWRALARLGWEDCRDSRVREKPPWRVLFFGTDQFAREALRALHAARENKEEELIDKLEVVTMPSPSPKGLPVKQYAVQSQLPVYEWPDVGSGEYDVGVVASFGRLLNEALILKFPYGILNVHPSCLPRWRGPAPVIHTVLHGDTVTGVTIMQIRPKRFDVGPILKQETVPVPPKSTAKELEAVLSRLGANMLISVLKNLPESLSNGRQQPMEGATYAPKISAGTSCIKWEEQTSEQIFRLYRAIGNIIPLQTLWMANTIKLLDLVEVNSSVLADPKLTGQALIPGSVIYHKQSQILLVYCKDGWIGVRSVMLKKSLTATDFYNGYLHPWYQKNSQAQPSQCRFQTLRLPTKKKQKKTVAMQQCIE | Function: Methionyl-tRNA formyltransferase that formylates methionyl-tRNA in mitochondria and is crucial for translation initiation.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 43832
Sequence Length: 389
Domain: Composed of an N- and a C-terminal domain. The N-terminal domain carries the tetrahydrofolate (THF)-binding site and the C-terminal domain is presumably involved in positioning the Met-tRNA substrate for the formylation reaction.
Subcellular Location: Mitochondrion
EC: 2.1.2.9
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Q31J85 | MTQPLRIIFAGTPDFSVPPLKTLIDSEHEVVAVYTQPDRPAGRGRKLTASPVKQTALEHDIPVYQPVSLKTPEAQAELEALQADVMIVVAYGLILPKAVLDMPKYGCLNIHASILPRWRGAAPIQRAIQMGDAETGVTIMQMDVGLDTGDMLTILKTPIKPEDTAQTLHDRLSALGCDAMMTTLSNLQTDQLSPVKQDERQVTYAEKLNKAEAELDWQASAQTLARQVQAFNPWPVAFTQYQGQPLRIWQAEVGHASTQKSPGLVISVSKTGMEVATGKGSLLIKQVQPSGKKAMPAYDFAQARQLTGQTLG | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 33962
Sequence Length: 312
EC: 2.1.2.9
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Q1AVZ9 | MRVAFAGTPEFAATVLRGLLGSGHEVGLVISQPDAPRGRGRRTASPPVALLAREAGLPLLQPASISEAAGEISRHDALVVAAYGQILRPDTLYAARHGAYNVHASLLPAYRGAAPVERAIMDGERETGVTVIRMDEGLDTGPVALQRRVPIPPDMTGGELADLLARVGAEALVEVLDRLESGTLNLTRQDSSRASYAPRITRQDQEIDWSRDARRVHDQVRALSPHIGARTRHPEVEGPLKIWRTRVHREAGRELAPGELRAGDGRLFVGCESGVVEILELQLPGGRRLGAAEFLRGHSLTGALRR | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 32985
Sequence Length: 306
EC: 2.1.2.9
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Q5LNI8 | MRVVFMGTPDFSVPVLEALVAAGHEIAAVYCQPPRPAGRGKKDRPTPVHARALDLGLEVRHPVSLKGAEAQADFAALGADVAVVVAYGLILPQAVLDAPRHGCLNIHASLLPRWRGAAPIHRAIMAGDEATGICIMQMEAGLDTGPVLLRSRTPIRAEETTGALHDRLSAMGADLIVEALARLPELTPEPQPEDGVTYAAKIDKAEARVDWTRPAVAIDRQIRGLSPFPGAWTEIAGERVKLLASRLDEGQGTPGEVLDDALTIACGTGAISLIRLQRAGKAAQDADIFLRGWPVPKGTRL | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 31935
Sequence Length: 301
EC: 2.1.2.9
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B8I255 | MKIIFMGTPEFAVPSLEMLINEGYNVIAVVTQPDKPKGRGKKLAAPPVKEFALEHGIKVLQPAKIKTPEFVEQIRELGPDLLITAAYGKIISKDMLDVPPLGCINVHGSLLPAYRGAAPIHWSIINGEKVTGITTMFTDVGLDTGDMLLKRELEISSDMTAGELHDEMAILGAEVLKDTLIHLKNGTLVRSPQDDALSSYAPIITKEVGLIDWNKTVQQVHNLVRGTNPWPGAFTFINESKMRVWKTCIVDFGNSQEHCPGEIVSVDDKGILVKCCDGYIMIKELQFDSSKRMKVRDYIRGNKIDTGEKLGK | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 34438
Sequence Length: 312
EC: 2.1.2.9
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A4FBJ4 | MRLVFAGTPEPAVPSLRALIESANHEVAAVVTRPDAPAGRGRKLMRSPVGALADEHGIEVLTPAKASDPEFLARLRELEPECCPVVAYGALLRQTALDIPEHGWVNLHFSLLPAWRGAAPVQAAIKHGDQITGASTFRLVPELDAGPVYGVVTEEVRDTDTSGVLLERLSVSGAKLLVATLDGIADGTLRAEEQPADGVSYAPKVEVEDARVDFTAPARAVDRLVRSVTPDPGAWASFRDERLKLGPVSIVDEDLGLAPGEIRVERRRVLAGTGSAPVALGEVQAQGKKRMAATDWARGSRIEQGERLK | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Mass (Da): 32953
Sequence Length: 309
EC: 2.1.2.9
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Q9H479 | MEQLLRAELRTATLRAFGGPGAGCISEGRAYDTDAGPVFVKVNRRTQARQMFEGEVASLEALRSTGLVRVPRPMKVIDLPGGGAAFVMEHLKMKSLSSQASKLGEQMADLHLYNQKLREKLKEEENTVGRRGEGAEPQYVDKFGFHTVTCCGFIPQVNEWQDDWPTFFARHRLQAQLDLIEKDYADREARELWSRLQVKIPDLFCGLEIVPALLHGDLWSGNVAEDDVGPIIYDPASFYGHSEFELAIALMFGGFPRSFFTAYHRKIPKAPGFDQRLLLYQLFNYLNHWNHFGREYRSPSLGTMRRLLK | Function: Fructosamine-3-kinase involved in protein deglycation by mediating phosphorylation of fructoselysine residues on glycated proteins, to generate fructoselysine-3 phosphate . Fructoselysine-3 phosphate adducts are unstable and decompose under physiological conditions . Involved in intracellular deglycation in erythrocytes . Involved in the response to oxidative stress by mediating deglycation of NFE2L2/NRF2, glycation impairing NFE2L2/NRF2 function (By similarity). Also able to phosphorylate psicosamines and ribulosamines .
Catalytic Activity: ATP + N(6)-(D-fructosyl)-L-lysyl-[protein] = ADP + H(+) + N(6)-(3-O-phospho-D-fructosyl)-L-lysyl-[protein]
Sequence Mass (Da): 35171
Sequence Length: 309
EC: 2.7.1.171
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Q9ER35 | MEQLLRAQLHTTTLRAFGSSGGGCISEGYAYYTDSGPVFVKVNRRTQARQMFEGEMASLEALRNTGLVRVPKPMKVIDLPGGGAVFVMEHLKMKSLSSQASKLGEQMADLHLYNQKLREKSKTRQNTVGCGAEGAEPQGVTKFGFHTVTCCGFIPQVNEWQEDWPTFFTRHRLQAQLDLIEKDYADRETQELWSRLQVKIPDLFAGIEIVPALLHGDLWSGNVAEDDQGPVIYDPASFYGHSEFELAIASMFGGFPRSFFTAYHRKIPKAPGFDKRLLLYQLFNYLNHWNHFGREYRSPSLGVMRKLLR | Function: Fructosamine-3-kinase involved in protein deglycation by mediating phosphorylation of fructoselysine residues on glycated proteins, to generate fructoselysine-3 phosphate . Fructoselysine-3 phosphate adducts are unstable and decompose under physiological conditions (By similarity). Involved in intracellular deglycation in erythrocytes and pancreatic islets . Involved in the response to oxidative stress by mediating deglycation of NFE2L2/NRF2, glycation impairing NFE2L2/NRF2 function . Also able to phosphorylate psicosamines and ribulosamines (By similarity).
Catalytic Activity: ATP + N(6)-(D-fructosyl)-L-lysyl-[protein] = ADP + H(+) + N(6)-(3-O-phospho-D-fructosyl)-L-lysyl-[protein]
Sequence Mass (Da): 35032
Sequence Length: 309
EC: 2.7.1.171
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P14738 | MKNNLRYGIRKHKLGAASVFLGTMIVVGMGQDKEAAASEQKTTTVEENGNSATDNKTSETQTTATNVNHIEETQSYNATVTEQPSNATQVTTEEAPKAVQAPQTAQPANIETVKEEVVKEEAKPQVKETTQSQDNSGDQRQVDLTPKKATQNQVAETQVEVAQPRTASESKPRVTRSADVAEAKEASNAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTITSTLNEEQTSKELDVKYKDGIGNYYANLNGSIETFNKANNRFSHVAFIKPNNGKTTSVTVTGTLMKGSNQNGNQPKVRIFEYLGNNEDIAKSVYANTTDTSKFKEVTSNMSGNLNLQNNGSYSLNIENLDKTYVVHYDGEYLNGTDEVDFRTQMVGHPEQLYKYYYDRGYTLTWDNGLVLYSNKANGNEKNGPIIQNNKFEYKEDTIKETLTGQYDKNLVTTVEEEYDSSTLDIDYHTAIDGGGGYVDGYIETIEETDSSAIDIDYHTAVDSEAGHVGGYTESSEESNPIDFEESTHENSKHHADVVEYEEDTNPGGGQVTTESNLVEFDEESTKGIVTGAVSDHTTVEDTKEYTTESNLIELVDELPEEHGQAQGPVEEITKNNHHISHSGLGTENGHGNYDVIEEIEENSHVDIKSELGYEGGQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGNQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPSYQFGGHNSVDFEEDTLPKVSGQNEGQQTIEEDTTPPIVPPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPAEPGKPVPPAKEEPKKPSKPVEQGKVVTPVIEINEKVKAVAPTKKPQSKKSELPETGGEESTNKGMLFGGLFSILGLALLRRNKKNHKA | Function: Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and inefficient way through actin rearrangements in host cells. This invasion process is mediated by integrin alpha-5/beta-1. Promotes bacterial attachment to both soluble and immobilized forms of fibrinogen (Fg) by means of a unique binding site localized within the 17 C-terminal residues of the gamma-chain of human Fg. Both plasma proteins (Fn and Fg) function as a bridge between bacterium and host cell. Promotes attachment to immobilized elastin peptides in a dose-dependent and saturable manner. Promotes attachment to both full-length and segments of immobilized human tropoelastin at multiple sites in a dose and pH-dependent manner. Promotes adherence to and aggregation of activated platelets independently of other S.aureus surface molecules. Is a critical mediator implicated in the induction of experimental endocarditis in rats with catheter-induced aortic vegetations, promoting both colonization and persistence of the bacterium into the host.
Location Topology: Peptidoglycan-anchor
Sequence Mass (Da): 111780
Sequence Length: 1018
Subcellular Location: Secreted
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Q96RU3 | MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRHQMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSNSRGEGKPDLKFGGKSKGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSPKQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGATPEDFSNLPPEQRRKKLQQKVDELNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLAEVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVCLDKNAKDS | Function: May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71307
Sequence Length: 617
Domain: The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation.
Subcellular Location: Cytoplasm
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Q8R511 | MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTACKAFLSTLNELNDYAGQHEVISENMTSQITVDLVRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQMRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVVEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSSSKEGKPELKFGGKSRGKLWPFIKKNKLMTLLTSPHQPPPPPPASASPSAVPNGPQSPKQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGVTPEDFSNFPPEQRRKKLQQKVDDLNKEIQKETDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVTQNIEKLRLEAHKFEAWLAEVEGRLPARSEQARRQSGLYDGQTHQTVTNCAQDRESPDGSYTEEQSQESEHKVLATDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLSVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVYLDKNAKGS | Function: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL (By similarity). May act as a link between RND2 signaling and regulation of the actin cytoskeleton. Isoform 1 and isoform 2 promote RND2-induced neurite branching in neuronal cells.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71293
Sequence Length: 616
Domain: The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation (By similarity).
Subcellular Location: Cytoplasm
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Q8UHU0 | MAVVIDGKAKAASVTEAVRKSAEALEAEKGVKPGLAVVIVGNDPASHAYVNSKSKMAKQCGFNSIQHTLPEETTQAALLKLVGELNTDASIHGILVQLPLPKHFNSDEIIQSILPEKDVDGLSVLNAGKLATGDLATGLISCTPAGAMLLVRGIHGDDLSGLNAVVIGRSNLFGKPMGQLLLNANATVTMAHSRTKDLVTVCKTADILVAAVGRAAMVKGDWVKPGATVIDVGINRIAAPEKGEGKSKLVGDVAFDEASAVAAAITPVPGGVGPMTIAMLMANTVIAAHRALGKTAPKF | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30627
Sequence Length: 299
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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B2UM17 | MQIIDGKQVASQVLEEVERDIARLREQGITPGLAVVLVGEDPASQVYVNSKVKKCAELGMNSRKIVLPSDASQEELLRIVRELNVDPSVHGILVQSPPPPHIDEAAVVLEIDPAKDVDGFHPENVAKLVLEDETGFVPCTPLGCMRLLKAAGIETAGANAVVIGRSMIVGKPMAHLLMSKQANATVTVAHSRTKNLPELCRSADIIVAAIGRPAFVTADFVKDGAVVVDVGINRVEDASAKRGYRIVGDVAYDEVAPKCRAITPVPGGVGPMTIAMLMANTVKACRQQTGA | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30847
Sequence Length: 291
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q0VQ92 | MTAQILDGKTLAQQFEQEMRLRVDVLKAKANGHTPILATILVGADPASATYVKMKGNACQRVGMESVAIELSEETTTAQLLAKIDELNNNQDVHGILLQHPVPAQIDERACFDAISLEKDVDGVTCLGFGRMSMGEAAYGCATPKGIMRLLEHYQVELEGKHAVVVGRSAILGKPMAMMMLEANATVTICHSRTQNLPELVKQADIVVGAVGKPEFIKADWIKDGAVVVDAGFHPERCGDIELAPLVDRVAAYTPVPGGVGPMTINTLIFQTLQSGEKAFG | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30120
Sequence Length: 281
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q894G6 | MAVAIDGKRVSEELRKELKNFIDERVEKGLKVPCVSSILIGNDKGSLFYIKNQRRICKEIGIEFKNIVLEENIEEDKIIEVIEDLNKDENVHGIILQMPLPKTLDEEKIVNKICPSKDIDGLTDINAGRFYKGEKCFIPCTAQGIIEIIKSTKESISGKKAVVLGRSVIVGKPVAQLLVNEDATVTICHSKTKDIKSLCKEADIIVSAMGIPKFVKEDFIKDGAIVIDVGFSVLDGKMVGDIDYDNVFKKAGFITPVPGGVGSVTPTMLIKNLCEVFK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30625
Sequence Length: 278
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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B5Y9D1 | MALIMKGKPVADAIYEELQPMTSLNLTLGIIKYKGSDAGGYLSGLSKAAQRLNVQLRVNEVEQFQELTQSVVVMGKDSQVHGILLLKPFPKEWNFRQASDLIPPEKDVDALHPVNLGKLAQGRGNLVPATPQAVLSILDFYNVLPLEGASALVIGRSEAVGLPAFLQLMQRNATVTVAHSRTKDLPSLSRQADLVVVAVGKPNFLTKDHVKEGAVVIDVGTNVLEDGKVVGDVDRENVEPLVRAITPVPGGVGSVTTACLFKNLFLCYQEQTR | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 29456
Sequence Length: 273
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q8FRU9 | MTAIKLDGNLYRDEIFADLAQRVAALKEKGIVPGLATVLVGDDPASHSYVKMKHRDCEQIGVNSIRRDLPADISQEELFAVIDELNADDSCTGYIVQLPLPKHLDENAVLERIDPAKDADGLHPVNLGKLVLNEPAPLPCTPNGSISLLRRFGIELNGAKVVVIGRGVTVGRPIGLMLTRRSENSTVTLCHTGTKDLAAETRAADVIVAAAGQPHMLTADMVKPGAAVLDVGVSRKDGKLLGDVHPDVWEVAGAVSPNPGGVGPLTRAFLVHNVVERAEKLAGL | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30134
Sequence Length: 284
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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A9KGQ5 | MIARILDGRTCAEKVKARVKENIRLLQEKGLPSPGLAVILVGNDPASATYVAHKERACQAVGIRSTVYRMPNTITESELASKIDECNRDSNTHGILLQLPLPAHIDPANLLERIRPDKDVDGFHPYNLGRLVQRRPALRPCTPYGVMTLLTETHENLEGKHAVIVGASNIVGRPMALELLLAKCTVTVCHRFTRDLAEHVKSAELLIVAIGKPGIIQSEWIKPGAIVIDVGFSRLSPNKIAGDIDFETAKERASWITPVPGGVGPMTVATLLENTLQAAQTFL | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30820
Sequence Length: 283
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q7NAE4 | MFIKLDGTKLSQKLKEDLAKKVNNQKIKILIIISDPSEASRIYVRNKINYCDSLGIQTEVYDLSKIDDTNQFIVEMNQKISLSNPNGVLVQLPIKERLDTNKIIENIPIRLDVDAFLYHRFDQDQKEKVIPCVLNAVLELFKEYQLSFLDKKILLIGNGITSNQPIVNYLNEHQIKFDLITKENSQLLEEKTKVADLVISAVGKAKFLANYQFKRGVIFIDIGIDKYFDPEQSKYLICGDFDYDKLKEIASYGTPTPGGIGPLTIYSLVKNLINLSEIQKVNK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 32338
Sequence Length: 283
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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P47259 | MSFDGKLKAQSILETYKNFDWSKCKLVIIQANDDDSSDSFIKQKLIACNTVGAKSELIKLSNQITQAELIEKIISLNHDVNVTGIILQLPVYPHLDKNSLLEAINPLKDVDGLTTNHLAEIKPCIVEAIITLKELFNLEFNNQKIVVVGLGITGGKPIYEFLKTSGYKVQACDKDTPNTFELIKSADIVFTAIGKSHFFQAKNFKKGVILFDIGVSRNKQNKLCGDINPEGIEKKARWWTKTPGGVGPFTVLAIIKNLWILHEKNKRCLQSSI | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30457
Sequence Length: 273
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q6MSL3 | MVILDGKLVSKQIKQTLKKQIDTYLNKNYKKPKLAVILIGNDPASELYVSNKIKACNLVGIESVLLRFGQNITSEMLSDQINQLNNDNSVDAILLQLPLPKHLDEQEFLQAIDPLKDVDGFHYINQGKMLEGYDTIYPCTPIGIINLLKAYNIDVRSKDITIIGTSNIVGKPLAIMLSNMGATISMCNKNTKSLKKYTKRSDIVISTTGKQALIKKDMIKKNAIVIDVGIIKDPITNKIVGDVDFENVKELCSYITPVPGGVGPMTVSMLLENTFKLYKLHIKENYEN | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 32102
Sequence Length: 288
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q98QV3 | MMKKLLSNELVQIKRAELKEKFSKLDQKVKFAIVLIGDNASSKIYVKKKIEFAQDIGVEAKLFHFEENVDFNLLKDAFKKIDKEYDGIILQLPVLHFDVNELLLMIDKNKDLDGLNPENEKAFYENRECIIPATARAIWTFLKFHKISVENKKVFVVGQSRLVGKPISQFLKNNNAIVRVFDKSTGLKGTEEADILIVATGVAQLIKAENIKENSILIDVGFSKINNKIYGDLDIESIKEKALKYTPPIGAIGPVTVLSLFENLYEIILKKK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 30885
Sequence Length: 272
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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A0QSY5 | MGAISLDGKTTRDEIFVDLKERVAALTAAGRTPGLGTVLVGDDPGSQAYVRGKHADCAKVGINSIRRDLPADITTEQLNETIDELNANPDCTGYIVQLPLPKHLDENAALERIDPAKDADGLHPTNLGRLVLGKQAALPCTPRGIVHLLRRFDVPIAGAHVVVIGRGVTVGRPMGLLLTRRSENATVTLCHTGTRDLPALTRQADIIIAAVGVPHMVTADMVKPGAAVVDVGVSRVDGKLTGDVAPDVWEVAGHVSPNPGGVGPLTRAFLLTNVVEAEESKLA | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 29693
Sequence Length: 283
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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Q4A6B1 | MKILSGREKAEQDLKQLKKELDELNLNRPIKLAIIQVGDKMESNRYVEQKLKKAKEIGIEAKCFKFDENITQKRLLLAMDEINENWDGILIQLPLPKHLPKEVILDAVPYEKDIDGLSHRNEFILYNEKNSDDKFFVPAAARAVLELIEHHEINYKKKKVAVVGRSHLVGKPVAHILKRRGASVSTFDENTPIKLVASADIVIVAIGVPKYIKAENIKQGAIIIDVGTNYDQNDPSVIFGDVDHESVKTKASAITPVPGGVGPLTVVCLLKNLVEIYK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da): 31128
Sequence Length: 278
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
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K0I977 | MGRDEEAAAQAEAWNHGFGFIKTSVIKTAIELEIPDILHNQGGPLSLSALSSAVGVPPDRLHRIMRFLAHHGVSKKTASPPGESDYYYAETAVSRSLTKDNLGPFVLLQGAQRGPSACITAQGLKSRERPGVEELGSDPLYEDPIFTEKVFRDAMTCHARVTTSAVIENYGEGFRGVGSLVDVGGSYGMTLGMLVEAFPWIRGICYDLPPVVAKAKPLHGVEFVAGSMFESVPKADVIMLMFVLHNWSDNECIDILKRCKEAIPAETGRLMIIDAIIDEDGEGDEFAGARLGLDVTMMAVTYEGKERTHREWAYILTEAGFRKYVVNNIKALESLIEAYP | Function: Flavonoid 7-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects . Catalyzes S-adenosylmethionine-dependent regioselective 7-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including apigenin (API) and luteolin (LUT), and, with a lower efficiency, scutellarein (SCU), naringenin (NAR), chrysoeriol (CHRYS), diosmetin (DIOS), acacetin (ACA) and scutellarein-7-methyl ether (SCU7Me) .
Catalytic Activity: (2S)-naringenin + S-adenosyl-L-methionine = (2S)-sakuranetin + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37182
Sequence Length: 340
Pathway: Flavonoid metabolism.
EC: 2.1.1.-
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K0I7Q2 | MAVDKEVQLHAQAWEHALSYINSTALSAAVELEIPDILEDHGGLMSLSELSAASGCPREPLYRLMRFLIFHGIFTKSDDCYAQSPLSRLFTRENLGPYMLMQATPVTRSPAGLSGEALKTGTSLYLKSIRGEDSWSDPAYGYHMKAFTNAMIAHARLTAAAIVSNYPAAFDGLRSVVDVGGRHGTAIGRLVEAFPWVRGIAFDLPEIVADAPPRKGVDFVGGDMFESVPKADAVMLMWILHDWSDDKCIEILKKCKEAIPASTGKVMIVDAIINEDGEGDEFSGARLSLDMIMLAVMAQGKERTYKEWVHLLNEAGFSKHTVKNIKSIESVIEAYP | Function: Flavonoid 4'-O-methyltransferase involved in the biosynthesis of polymethoxylated flavonoids natural products such as nevadensin and salvigenin, aroma compounds which contribute to the flavor of sweet basil, and exhibit pharmacological activities such as anti-allergic, anti-oxidant, antibacterial, anti-proliferative, and anti-inflammatory effects . Catalyzes S-adenosylmethionine-dependent regioselective 4'-O-methylation of flavonoids; active on various hydroxylated flavonoid substrates, including scutellarein-7-methyl ether (SCU7Me) and cirsimaritin (CIRM), and, with a lower efficiency, hispidulin, ladanein (LAD), cirsioliol (CIRL) and genkwanin (GENK) .
Catalytic Activity: S-adenosyl-L-methionine + scutellarein 7-methyl ether = H(+) + ladanein + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36840
Sequence Length: 336
Pathway: Flavonoid metabolism.
EC: 2.1.1.-
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Q5Z9N5 | MPPTLLLLLLLLPPSLASPDRDIYALAKLKAALVPSPSATAPPPLADWDPAATSPAHCTFSGVTCDGRSRVVAINLTALPLHSGYLPPEIALLDSLANLTIAACCLPGHVPLELPTLPSLRHLNLSNNNLSGHFPVPDSGGGASPYFPSLELIDAYNNNLSGLLPPFSASHARLRYLHLGGNYFTGAIPDSYGDLAALEYLGLNGNTLSGHVPVSLSRLTRLREMYIGYYNQYDGGVPPEFGDLGALLRLDMSSCNLTGPVPPELGRLQRLDTLFLQWNRLSGEIPPQLGDLSSLASLDLSVNDLAGEIPPSLANLSNLKLLNLFRNHLRGSIPDFVAGFAQLEVLQLWDNNLTGNIPAGLGKNGRLKTLDLATNHLTGPIPADLCAGRRLEMLVLMENGLFGPIPDSLGDCKTLTRVRLAKNFLTGPVPAGLFNLPQANMVELTDNLLTGELPDVIGGDKIGMLLLGNNGIGGRIPPAIGNLPALQTLSLESNNFSGALPPEIGNLKNLSRLNVSGNALTGAIPDELIRCASLAAVDLSRNGFSGEIPESITSLKILCTLNVSRNRLTGELPPEMSNMTSLTTLDVSYNSLSGPVPMQGQFLVFNESSFVGNPGLCGGPVADACPPSMAGGGGGAGSQLRLRWDSKKMLVALVAAFAAVAVAFLGARKGCSAWRSAARRRSGAWKMTAFQKLEFSAEDVVECVKEDNIIGKGGAGIVYHGVTRGAELAIKRLVGRGGGEHDRGFSAEVTTLGRIRHRNIVRLLGFVSNRETNLLLYEYMPNGSLGEMLHGGKGGHLGWEARARVAAEAACGLCYLHHDCAPRIIHRDVKSNNILLDSAFEAHVADFGLAKFLGGATSECMSAIAGSYGYIAPEYAYTLRVDEKSDVYSFGVVLLELITGRRPVGGFGDGVDIVHWVRKVTAELPDNSDTAAVLAVADRRLTPEPVALMVNLYKVAMACVEEASTARPTMREVVHMLSNPNSAQPNSGDLLVTF | Function: Receptor-like kinase protein that regulates the size of the floral meristem.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 105512
Sequence Length: 994
Subcellular Location: Membrane
EC: 2.7.11.1
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B5RHS5 | MALYCGDNFGVYSQPGLPPPAAAAAAAAAAPGAPPASRAPYALADYAAPPAAAANPYLWLNGPGVGVGVGVGVGGPPAAAAAAAAAYLGAPPPPPPPPGGAAGPFLQPPPAAGTFGCAQRAFAQPAPAAPASPAGPAAPGELGWLSMASREDLMKMVRPPYSYSALIAMAIQSAPERKLTLSHIYQFVADSFPFYQRSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGKGNYWTLDPNCEKMFDNGNFRRKRKRRSEASSASTSTVAAGTTKSEEGLSSGLGSGVGGKPEGDSPSALLRPPQSPEPPEGTKSTASSPGGSLLSSAPCLNTFFSSLSTLSVSSSGGAQRAGPGSRHLGIQGTPLSSSGAFPASCISSEAPPDTLQLSNGASSGSGQRSSYYSPFPASTSGGQSSPFGSPFYNFSMVNSLIYPREGSEV | Function: Transcription factor required for pharyngeal arch development, and which is involved in hair, ear, jaw and dental development . May act as a pioneer transcription factor during pharyngeal arch development (By similarity). Required for the development of the epithelium of hair and whisker placodes and that of teeth . Required for hair follicle stem cell specification (By similarity). Acts downstream of TBX1 for the formation of the thymus and parathyroid glands from the third pharyngeal pouch (By similarity).
PTM: Phosphorylation promotes the transcription factor activity. Dephosphorylation by protein phosphatase 2A (PP2A) reduces its activity.
Sequence Mass (Da): 44053
Sequence Length: 436
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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D3Z120 | MALYCGDNFVYSQPAAAPGAPPTSRAPYGLSDYAAPPAAAANPYLWLNGPGVGGPASAASYLGAPPPPPGAAPGPFLQPPAAPGTFAGAQRGFAQPSASAPASPAGSAAPGELGWLSMASREDLMKMVRPPYSYSALIAMAIQSAPERKLTLSHIYQFVADNFPFYQRSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGKGNYWTLDPNCEKMFDNGNFRRKRRRRAEASSNLTVPSGTSKSEGQSSRLRVSGKLEGDSPSSILRPSQSPEPPEGTKSTASSPGASTLTSTPCLNTFLSTFNTLNVNSSSSMGNQRTLPGSRRHLGGTQLPSSTFPNTSVPDSSPDSMQLSTVGGSNQLSSYYNPFSGGSSGDQSSPFSSPFYNFSMVNSLIYPRDGSDI | Function: Transcription factor required for pharyngeal arch development, which is involved in hair, ear, jaw and dental development . May act as a pioneer transcription factor during pharyngeal arch development . Required for epithelial cell differentiation within the epidermis . Acts at multiple stages of otic placode induction: necessary for preplacodal ectoderm to execute an inner ear program . Required for hair follicle stem cell specification . Acts downstream of TBX1 for the formation of the thymus and parathyroid glands from the third pharyngeal pouch .
PTM: Phosphorylation promotes the transcription factor activity . Dephosphorylation by protein phosphatase 2A (PP2A) reduces its activity .
Sequence Mass (Da): 42015
Sequence Length: 399
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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P42128 | MAEVGEDSGARALLALRSAPCSPVLCAAAAAAAFPATTSPPPPAQPPPGPPALPAEPGPGPVPSTVATATTTAPALVAAAAASVRQSPGPALARLEGREFEFLMRQPSVTIGRNSSQGSVDLSMGLSSFISRRHLQLSFQEPHFYLRCLGKNGVFVDGAFQRRGAPALQLPQQCTFRFPSTAIKIQFTSLYHKEEAPASPLRPLYPQISPLKIHIPEPDLRSLVSPIPSPTGTISVPNSCPASPRGAGSSSYRFVQNVTSDLQLAAEFAAKAASEQQADASGGDSPKDESKPPYSYAQLIVQAISSAQDRQLTLSGIYAHITKHYPYYRTADKGWQNSIRHNLSLNRYFIKVPRSQEEPGKGSFWRIDPASEAKLVEQAFRKRRQRGVSCFRTPFGPLSSRSAPASPTHPGLMSPRSSGLQTPECLSREGSPIPHDPDLGSKLASVPEYRYSQSAPGSPVSAQPVIMAVPPRPSNLVAKPVAYMPASIVTSQQPSGHAIHVVQQAPTVTMVRVVTTSANSANGYILASQGSTGTSHDTAGTAVLDLGNEARGLEEKPTIAFATIPAASRVIQTVASQMAPGVPGHTVTILQPATPVTIGQHHLPVRAVTQNGKHAVPTNSLTGNAYALSSPLQLLAAQASSSTPVVITRVCEVGPEEPAAAVSVAANAAPTPAASTTTSASSSGEPEVKRSRVEEPGGTATTQPTAMAATGPQGPGTGE | Function: Transcriptional regulator involved in different processes such as glucose metabolism, aerobic glycolysis, muscle cell differentiation and autophagy . Recognizes and binds the forkhead DNA sequence motif (5'-GTAAACA-3') and can both act as a transcription activator or repressor, depending on the context . Together with FOXK2, acts as a key regulator of metabolic reprogramming towards aerobic glycolysis, a process in which glucose is converted to lactate in the presence of oxygen . Acts by promoting expression of enzymes for glycolysis (such as hexokinase-2 (HK2), phosphofructokinase, pyruvate kinase (PKLR) and lactate dehydrogenase), while suppressing further oxidation of pyruvate in the mitochondria by up-regulating pyruvate dehydrogenase kinases PDK1 and PDK4 . Probably plays a role in gluconeogenesis during overnight fasting, when lactate from white adipose tissue and muscle is the main substrate . Involved in mTORC1-mediated metabolic reprogramming: in response to mTORC1 signaling, translocates into the nucleus and regulates the expression of genes associated with glycolysis and downstream anabolic pathways, such as HIF1A, thereby regulating glucose metabolism . Together with FOXK2, acts as a negative regulator of autophagy in skeletal muscle: in response to starvation, enters the nucleus, binds the promoters of autophagy genes and represses their expression, preventing proteolysis of skeletal muscle proteins . Acts as a transcriptional regulator of the myogenic progenitor cell population in skeletal muscle . Binds to the upstream enhancer region (CCAC box) of myoglobin (MB) gene, regulating the myogenic progenitor cell population . Promotes muscle progenitor cell proliferation by repressing the transcriptional activity of FOXO4, thereby inhibiting myogenic differentiation . Involved in remodeling processes of adult muscles that occur in response to physiological stimuli . Required to correct temporal orchestration of molecular and cellular events necessary for muscle repair . Represses myogenic differentiation by inhibiting MEFC activity . Positively regulates Wnt/beta-catenin signaling by translocating DVL into the nucleus (By similarity). Reduces virus replication, probably by binding the interferon stimulated response element (ISRE) to promote antiviral gene expression (By similarity).
PTM: Phosphorylation by GSK3 (GSK3A or GSK3B) promotes interaction with YWHAE/14-3-3-epsilon and retention in the cytoplasm . In response to mTORC1 signaling, phosphorylation by GSK3 is prevented, leading to translocation to the nucleus .
Sequence Mass (Da): 74920
Sequence Length: 719
Subcellular Location: Nucleus
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Q01167 | MAAAAAALSGAGTPPAGGGAGGGGAGGGGSPPGGWAVARLEGREFEYLMKKRSVTIGRNSSQGSVDVSMGHSSFISRRHLEIFTPPGGGGHGGAAPELPPAQPRPDAGGDFYLRCLGKNGVFVDGVFQRRGAPPLQLPRVCTFRFPSTNIKITFTALSSEKREKQEASESPVKAVQPHISPLTINIPDTMAHLISPLPSPTGTISAANSCPSSPRGAGSSGYKVGRVMPSDLNLMADNSQPENEKEASGGDSPKDDSKPPYSYAQLIVQAITMAPDKQLTLNGIYTHITKNYPYYRTADKGWQNSIRHNLSLNRYFIKVPRSQEEPGKGSFWRIDPASESKLIEQAFRKRRPRGVPCFRTPLGPLSSRSAPASPNHAGVLSAHSSGAQTPESLSREGSPAPLEPEPGAAQPKLAVIQEARFAQSAPGSPLSSQPVLITVQRQLPQAIKPVTYTVATPVTTSTSQPPVVQTVHVVHQIPAVSVTSVAGLAPANTYTVSGQAVVTPAAVLAPPKAEAQENGDHREVKVKVEPIPAIGHATLGTASRIIQTAQTTPVQTVTIVQQAPLGQHQLPIKTVTQNGTHVASVPTAVHGQVNNAAASPLHMLATHASASASLPTKRHNGDQPEQPELKRIKTEDGEGIVIALSVDTPPAAVREKGVQN | Function: Transcriptional regulator involved in different processes such as glucose metabolism, aerobic glycolysis and autophagy (By similarity). Recognizes and binds the forkhead DNA sequence motif (5'-GTAAACA-3') and can both act as a transcription activator or repressor, depending on the context . Together with FOXK1, acts as a key regulator of metabolic reprogramming towards aerobic glycolysis, a process in which glucose is converted to lactate in the presence of oxygen (By similarity). Acts by promoting expression of enzymes for glycolysis (such as hexokinase-2 (HK2), phosphofructokinase, pyruvate kinase (PKLR) and lactate dehydrogenase), while suppressing further oxidation of pyruvate in the mitochondria by up-regulating pyruvate dehydrogenase kinases PDK1 and PDK4 (By similarity). Probably plays a role in gluconeogenesis during overnight fasting, when lactate from white adipose tissue and muscle is the main substrate (By similarity). Together with FOXK1, acts as a negative regulator of autophagy in skeletal muscle: in response to starvation, enters the nucleus, binds the promoters of autophagy genes and represses their expression, preventing proteolysis of skeletal muscle proteins (By similarity). In addition to the 5'-GTAAACA-3' DNA motif, also binds the 5'-TGANTCA-3' palindromic DNA motif, and co-associates with JUN/AP-1 to activate transcription . Also able to bind to a minimal DNA heteroduplex containing a G/T-mismatch with 5'-TRT[G/T]NB-3' sequence . Binds to NFAT-like motifs (purine-rich) in the IL2 promoter . Positively regulates WNT/beta-catenin signaling by translocating DVL proteins into the nucleus . Also binds to HIV-1 long terminal repeat. May be involved in both positive and negative regulation of important viral and cellular promoter elements .
PTM: Hyperphosphorylated during mitosis by CDK1 and, to a lower extent, CDK2 . Phosphorylation at Ser-373 and Ser-428 affects stability by promoting degradation .
Sequence Mass (Da): 69062
Sequence Length: 660
Domain: The C-terminal part of the DNA-binding domain may contribute to DNA recognition specificity.
Subcellular Location: Nucleus
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B1Y3P5 | MPELPEVEVTRLGLVDRIGGATVRALQLGKPLRWPIGVAPQQLAGQRIGELARRGKYIWMPLQDGSTPAGGLLWHLGMSGSLRFEAQLPPPGPHDHVELVTDRGSLRLTDPRRFGAVVWSPSLQAGCAARLLGGLGVEPLEDGFTASVLHQGLRGRRVAIKQALLAGDIVVGVGNIYCSEALFVAGIDPRLAAQRLSLARCERLVQAIRQVLRQALMAGGSTLRDFRDAHGMGGAFQLQAQVYDRADQPCRRCGALVRRIVQGQRATYFCPVCQRR | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 29959
Sequence Length: 276
EC: 3.2.2.23
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Q1WUN7 | MPELPEVETVRRGLEKLVLNKKIKDIRVLYSKTIVNEESEFIEKLTNKTIKKIDRRGKYLLFRFSSDLTMISHLRMEGKYFVEPSTKEVEKHTHVVFDFTDGTSLRYNDVRKFGRMQLVKTGMEIQTAGLAKLGPEPKEKTFIVEDFSKNLKRRKKAIKNALLDQTIVAGLGNIYADEVLWMSKIHPETPANKLTEEEVKVLRDNIIKELALATEAGGTTIRSYTDAFRHSGGFQFSLHAYQRTGDPCERCGTPIQRIVVGQRGTHFCPKCQVVKS | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 31579
Sequence Length: 276
EC: 3.2.2.23
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Q8Y6W7 | MPEMPEVENVRATLQELVPGKKIDQVIVRVPKMIVSTPPDEFVHMLVGQEIEGVRRRGKFLLFDLTNCTILSHLRMEGKFRLMDENEEVSKHTHIIFHFEDHTELRFLDVRKFGTMEVTNKYGEGETRSIKKLGPEPLTQAFTLTDFATGVKKTSRAIKTALLDQKLVAGVGNIYADEICFEAKVRPERAANSLSDKEIKRIFKATKSIMTEAVALGGSTVRTYVNSQGKLGQYQNKLKVYGKTDEPCVVCGTPIEKIKLNGRGTHFCPNCQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 30772
Sequence Length: 273
EC: 3.2.2.23
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C6BUX8 | MPELPEVEVISRGLAESLEGKTIESVKILNHSSVKMPWYLFSSRVAGEKITRIHRRAKLLIMDLGDDLHITFHLKMTGRVLAHEGPTTPEPHTRIVFGLTDGGSIEFHDTRKFGEVRALNNEELQEWDFYKNLGPEPLEVTAEELAERITGRKAQIKGLLLNQSVVAGCGNIYADESLFRSGIHPKAKASDLSNESLVKLFTELQAVLKQAIQENGSSIRDYVDAGGDAGGFQNSFKVYGKKGEPCPDCGKIFEGATVAGRTSTFCSNCQKMKD | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 30222
Sequence Length: 274
EC: 3.2.2.23
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Q6KHS0 | MPELPEVKTVILHLKKLILDKTISKIEIFIPKMIKEISSEEFKKYLENETIFNIENEGKFIVFFLSNNKIMLSHLRMEGGYNFYSKKRQKEIHDRLIFHFTDGSSLHYHDSRMFGTFHFRNSENYLKIKPLSLVAPVPWKIDLDEFFKLLKRKKTAIKKILLDQQIIAGLGNIYVDETLFASKVHPEFKANQLSLEQVKLILKNATRILQESTKLGGSSIRSYTSLNEKEGSFQNFLQVHTKFNKPCPNCGELIQKIKLGGRGTYFCKKCQQLN | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 31937
Sequence Length: 274
EC: 3.2.2.23
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Q1H3I3 | MPELPEVEVTRRGLEPLIGATVTQAVIRQPAMRWPIPSHLPQVLHGARLLELRRRGKYIIARFESGCLILHLGMSGRLCLLESDTFPEKHDHFDLHFADGRVMRMRDPRRFGAVLWAGDQPDEHSLLKVLGQEPLDEAFNGEFLQQAIRTRSSPIKTVIMDSHLVVGVGNIYASESLFRAGIHPETPARALTLAQCRRLVEEVKLTLQDALQAGGSSLRDFFGADGNPGYFQQTYFVYGRTGQPCRVCQTPIAVLRLGQRSTFYCPACQQGQPPSNAMP | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 31168
Sequence Length: 279
EC: 3.2.2.23
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B1ZGU8 | MPELPEVETVRRGLAPAMVGARFARVTLRRPNLRFPFPERFAERLEGTTVRELARRAKYLTAHLDSGESLILHLGMSGRFDVRMPDGSNLSPGDFYLEGALGTPKHDHVVMAFANGATVTYNDARRFGFMDLVATRDLETCRHFAAMGVEPLSDALDGAVLARLFARKITPLKAALLDQRLIAGLGNIYVCEALHRSGLHPALPAGALAKPDGAPTPKAKKLVKEIKAVLTEAVAAGGSTLRDYARPDGERGAFQHGFRVYDRVGHACPTKGCTGRIGRIVQGGRSTFFCETCQVR | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 32192
Sequence Length: 296
EC: 3.2.2.23
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Q9X3X1 | MPELPEVETTIRGLSEVLMGEKIIDVKVRRASLRRPIPSDIQERLIGSTIISLSRRAKYGIIVNDRDDALIFHLGMSGRWKINPENFEKHDHFVLQTKNNFIVSLYDPRRFGSLDLVKKNQLLEWSYFRNIGPEPLTGNFNPEYLQKKLFSSSAPIKKILLDQKVVAGIGNIYACEALHQAKIHPQRPSKNLNFDEITSLVFSIKNILQKAIAEGGSTLKDYARPNGELGYFSTKFKVYGKEGEQCECGHTIERYTLGGRSTFLCSSCQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity).
Catalytic Activity: Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
Sequence Mass (Da): 30664
Sequence Length: 270
EC: 3.2.2.23
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P53739 | MAGHHHEHEQERDHEQEHEHDSLQRPTTGSERTRSISFSKLLTRSWKRNASSSNNMSVSSVNLYSDPENSRESDHNNSGSEGQSSRFSKLKSMFQSGNSSKNASAHNSSQSSLEGDSASSSSKLRYVKPMTSVANASPASPPLSPTIPETDVLQTPKMVHIDQHEHEREHSNCGSPIMLSSSSFSPTVARTGTGRRRSPSTPIMPSQNSNNSSSTSAIRPNNYRHHSGSQGFSSNNPFRERAGTVRSSNPYFAYQGLPTHAMSSHDLDEGFQPYANGSGIHFLSTPTSKTNSLTNTKNLSNLSLNEIKENEEVQEFNNEDFFFHDIPKDLSLKDTLNGSPSRGSSKSPTITQTFPSIIVGFDNEYEEDNNNDKHDEKEEQQTTTDNKTRNLSPTKQNGKATHPRIKIPLRRAASEPNGLQLASATSPTSSSARKTSGSSNINDKIPGQSVPPPNSFFPQEPSPKISDFPEPRRSRRLRTKSFSNKFQDIMVGPQSFEKIRLLGQGDVGKVFLVREKKTNRVYALKVLSKDEMIKRNKIKRVLTEQEILATSNHPFIVTLYHSFQSEDYLYLCMEYCMGGEFFRALQTRKTKCICEDDARFYASEVTAALEYLHLLGFIYRDLKPENILLHQSGHIMLSDFDLSIQAKDSKVPVVKGSAQSTLVDTKICSDGFRTNSFVGTEEYIAPEVIRGNGHTAAVDWWTLGILIYEMLFGFTPFKGDNTNETFTNILKNEVSFPNNNEISRTCKDLIKKLLTKNESKRLGCKMGAADVKKHPFFKKVQWSLLRNQEPPLIPVLSEDGYDFAKLSSNKKRQTSQDSHKHLDEQEKNMFEERVEYDDEVSEDDPFHDFNSMSLMEQDNNSMIYGNTNSYGKIAYTPNSNRSRSNSHRTFFKR | Function: Flippase activator that phosphorylates DNF1 and DNF2 and which is involved in the generation of phospholipid asymmetry in membranes by the inward translocation of phospholipids and in the retrieval pathway from early endosomes to the trans-Golgi network (TGN). Phosphorylates also the N-terminal half of YPK1. Involved in pheromone-response.
PTM: The N-terminal non-catalytic domain is phosphorylated by YPK1.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 100546
Sequence Length: 893
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q6MLJ0 | MKVQSLLRIETQLLLGRLLTRSGDQAWDFVVPFALLVIFPGKLQVAAFYYLIVKIGTFLLTPSSGKWIDTHPRIQVVKWGVWLQFFAILAGMVFFGMLDGLVRAGGRESWLLSVLFIALALSGVMASLGSQITDISVGNDLAPSLVAPEKLTHFNSWLRRIDLATEVGAPILAGALFAFHPEQLPLAGLFLIGLWNLVSFVPEYFLLRNVIQRSGLKIKVLTEAQSWKDTFHINLRGSFSDPIFWLILSYALLWLSVLSPHGVLLAAYLKDEMRLPETEIGLFRGLGAVFGLISTVSFPYLVRRLGLISSSRWHLGFQGVTLGIAVTAFAMGSTASVYVFLGCILLSRVGLYGFSNGEFELRQRLIPEGRRGELNSLSSLTTTSATLILFSAGSLLPQTEDFKYLVYVSLAAVLLANVVFIKWSSRQGVVTSGAAEPVES | Cofactor: The cofactor facilitates a conformational change critical to the transport cycle. The binding of Ca2+ from extracellular fluid activates the transporter by triggering a conformational change that enables the transition from the open outward to open inward states.
Function: Iron transpoter that exports Fe(2+) from the cell. Also binds to Co(2+) and Ni(2+). May act as a multivalent divalent metal transporter . The transporter is composed of 12 transmembrane (TM) helices organized into N-terminal (TM1-6) and C-terminal (TM7-12) domains. The substrate-binding site is formed at the interface of the two domains and is alternately accessible from either side of the membrane. The transport cycle is viewed as a series of ligand-induced conformational changes that include open outward and open inward states .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48363
Sequence Length: 440
Subcellular Location: Cell membrane
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Q8PU58 | MIGDTMSGIIDSYIPVAIFLAVGLIMPPMTMFMVKQLSPRSKAASKYTTYESGSVPTGTARIQFNVEYYLYAIAFVLFDIEVLFLYPWATVYKGHGITSIAVVEMFVFIFILLFGYVYLWKKEALTWVK | Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. It also catalyzes the oxidation of F(420)H(2) with quinones such as 2,3-dimethyl-1,4-naphthoquinone, 2-methyl-1,4-naphthoquinone and tetramethyl-p-benzoquinone.
Catalytic Activity: H2 + methanophenazine = dihydromethanophenazine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14667
Sequence Length: 129
Subcellular Location: Cell membrane
EC: 1.12.98.3
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F1SVH7 | MGEVKETKTNNSKENPEEEVPGVITTTTSAIHNFLKKTKAQDIINWGRKNSLWFMTQPMGCCGVEMIATGCAHYDTDRFGIIPRNSPRHADVMIISGYVTKKYLPALKRLWDQMPAPKWVIAMGDCAISGGPFYESYSTVQNIDEIFPIDVYIPGCPPRPEALIQGFVELQEKIKARKDRGTEY | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. It also catalyzes the oxidation of F(420)H(2) with quinones such as 2,3-dimethyl-1,4-naphthoquinone, 2-methyl-1,4-naphthoquinone and tetramethyl-p-benzoquinone.
Catalytic Activity: H2 + methanophenazine = dihydromethanophenazine
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20732
Sequence Length: 184
Subcellular Location: Cell inner membrane
EC: 1.12.98.3
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F1SVL1 | MDARTIIESLTGKFPEAISEAGIESPIRIRAYVDKDKAKEVCEYLKGSLQFDHLCSVSGVDYPQRDELEAVYHIASYDHPVVLMLKARLPRDSPEIESVVSVYWNANWYERETYELYGIFFKNHPELKPLVLPDDMLGEWPLRKDYEGFPNRTARNLV | Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. It also catalyzes the oxidation of F(420)H(2) with quinones such as 2,3-dimethyl-1,4-naphthoquinone, 2-methyl-1,4-naphthoquinone and tetramethyl-p-benzoquinone.
Catalytic Activity: H2 + methanophenazine = dihydromethanophenazine
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18326
Sequence Length: 158
Subcellular Location: Cell membrane
EC: 1.12.98.3
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F1SVE4 | MEEMLESNEMIVHLGPQHPMQPGPFRLNLKLKGETIMDAEVEMGYIHKGIEKILENRTYLQGITIVDRICYLVALTNEECYVGCVEKLLDIEPPERAQYIRVILEELSRLQSHLLGLGEYGEFIGFVSMFMYTIKEREDILTLIDMVTGARVTHSYLRFGGVRDDLPEGFKEKTIPVLNKLKKVIRDYEEMFYSDTIYRERTIGIGVLTADEAKSLGVSGPVLRATGVPFDIRKNEPYLVYRDLDFKVCTETAGDCFARVQVRLNEMRESIYIIEQCLDMIPNGPIFPEGTPYGKRTPVMRVPAGEVFHRVEDPRGEMGMYMVSDGSDRPYRVKVRGPYYPTLQALPPLIIGTTVADMVSISGSMDGCTSEVDR | Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. It also catalyzes the oxidation of F(420)H(2) with quinones such as 2,3-dimethyl-1,4-naphthoquinone, 2-methyl-1,4-naphthoquinone and tetramethyl-p-benzoquinone.
Catalytic Activity: H2 + methanophenazine = dihydromethanophenazine
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42492
Sequence Length: 374
Subcellular Location: Cell inner membrane
EC: 1.12.98.3
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Q8PZ67 | MPPKIAEVIQHDVCAACGACEAVCPIGAVTVKKAAEIRDPNDLSLYEKGAAFQVCEGCLTCSRICPVVDGFIENELLNVRKFFGAKSKDNAGSQDGGVTSGILKALFNKGEIDCAVGITRNENWEPEVVLLTSAEDVERTRGTKYTSDPVVAALREAFEKYDRIAVVGVPCQAHAARLIRENVNEKIVLIIGLLCMESFHHDVMLDKIIPEIMKVNVRDIVKMEFTKGKFWVYTKDGEVHSVPIKDIAKYARNPCHHCCDYTSVFADISVGSVGAPDGWNSVFIRTEIGEKYFDMVRDEMEIMEDPKPGLELVGKLIEMKRKGNAEHFQEVCKEFSFETGIRSETV | Cofactor: Binds 2 [4Fe-4S] cluster.
Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. It also catalyzes the oxidation of F(420)H(2) with quinones such as 2,3-dimethyl-1,4-naphthoquinone, 2-methyl-1,4-naphthoquinone and tetramethyl-p-benzoquinone. Might have a dual function, acting as an electron input module when connected to the membrane integral Fpo complex, or as a soluble single subunit, being involved in the reoxydation of reduced ferredoxin in the cytoplasm .
Catalytic Activity: H2 + methanophenazine = dihydromethanophenazine
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38359
Sequence Length: 346
Subcellular Location: Membrane
EC: 1.12.98.3
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Q8PU59 | MTFMAIEIPEFIVPFVPWIRGTVGLVLVGAIFLGGMAAVWIERKLSADIQLRYGPSRVGKFGLLQLVADAIKLFTKEDVRPGNADRFLYDNAPVFMLTSLFLMLVAIPVGAVFIDGNLYPLAVTEMDISILFIEAVSAINIFGIFMAAYGSNNKYSLLGAFRNFARMIGYEVPLGIAIVSVAVMTGSLNIIDITSAQGSFVWNIFLQPIGFVVFFIALMADLGRLPFDQNESEEELVAGWVTEYTGMRFGLVFFAEYMHMILGSFLVALLFLGGWNVPAFVANNAVLGLIAPTGILLLKTVLVLMTIIGMRWAVPRFRIDQVVDMSWKKLLPLSLLNLAWAVGLGLYLGA | Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. It also catalyzes the oxidation of F(420)H(2) with quinones such as 2,3-dimethyl-1,4-naphthoquinone, 2-methyl-1,4-naphthoquinone and tetramethyl-p-benzoquinone.
Catalytic Activity: H2 + methanophenazine = dihydromethanophenazine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38443
Sequence Length: 350
Subcellular Location: Cell membrane
EC: 1.12.98.3
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Q8PU60 | MGCPEVQDRPGSGYELEETPAPVPVEPCLGSRPWTLSGGLSMVLKNIKYALKNIPKERVTRLCPEVESPLSERFRGLQTLDKSKCIGCGICANTCPNSAIKIVKAPIAPGSEKKRWFPQIDIGHCLFCGLCIDQCPKGALSSGKEYCKGMVKWAHKDLLMTPEKLAREVDIQEGDER | Cofactor: Binds 2 [4Fe-4S] cluster.
Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. It also catalyzes the oxidation of F(420)H(2) with quinones such as 2,3-dimethyl-1,4-naphthoquinone, 2-methyl-1,4-naphthoquinone and tetramethyl-p-benzoquinone.
Catalytic Activity: H2 + methanophenazine = dihydromethanophenazine
Sequence Mass (Da): 19459
Sequence Length: 177
EC: 1.12.98.3
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Q8PU61 | MIDPGTVGAALETAVFGLLALVTVFFAIFVVIAKDVVRAGLALIMCMFGVAGLYILLNAQFLGVIQVLVYIGAIGVLILFAVMLTKREIGGGPVQINRPLAFLVCLLFVAVVVTGAFGTSWNTVSELPENPADPSNIEGIGMLIFTHFVAPFEVLSIVLLASLIGAIYMAKGEGNR | Function: Component of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. It also catalyzes the oxidation of F(420)H(2) with quinones such as 2,3-dimethyl-1,4-naphthoquinone, 2-methyl-1,4-naphthoquinone and tetramethyl-p-benzoquinone.
Catalytic Activity: H2 + methanophenazine = dihydromethanophenazine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18513
Sequence Length: 176
Subcellular Location: Cell membrane
EC: 1.12.98.3
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P17596 | MGRMLTIRVFKYDPQSAVSKPHFQEYKIEEAPSMTIFIVLNMIRETYDPDLNFDFVCRAGICGSCGMMINGRPSLACRTLTKDFEDGVITLLPLPAFKLIKDLSVDTGNWFNGMSQRVESWIHAQKEHDISKLEERIEPEVAQEVFELDRCIECGCCIAACGTKIMREDFVGAAGLNRVVRFMIDPHDERTDEDYYELIGDDDGVFGCMTLLACHDVCPKNLPLQSKIAYLRRKMVSVN | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor.
Catalytic Activity: a menaquinone + succinate = a menaquinol + fumarate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27165
Sequence Length: 239
Subcellular Location: Cell inner membrane
EC: 1.3.5.1
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Q5E2B5 | MSNRKPYVREMTRTWWKDHPFYRFYMVREATVLPLIFFTICLLVGLGSLVKGPLAWASWLDFMANPIVVALNIVALAGSLFHAQTFFSMMPQVMPIRLGGKTLDKKVVVLAQWAAVAAITLLVLVIV | Function: Anchors the catalytic components of the fumarate reductase complex to the cell membrane, binds quinones.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14339
Sequence Length: 127
Subcellular Location: Cell inner membrane
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Q8ZIX8 | MNQVPKRSDEPIFWGLFGAGGMWGAIIAPVIILLVAILLPLGAFPGDALSYERILAFCQSFIGRVFLLLMIILPLWCGLHRIHHAMHDLKIHVPAGKWVFYGLAAILSVVTFIGVLTL | Function: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used in anaerobic growth, and succinate dehydrogenase is used in aerobic growth. Anchors the catalytic components of the fumarate reductase complex to the cell inner membrane, binds quinones.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 12990
Sequence Length: 118
Subcellular Location: Cell inner membrane
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P32614 | MSLSPVVVIGTGLAGLAAANELVNKYNIPVTILEKASSIGGNSIKASSGINGACTETQRHFHIEDSPRLFEDDTIKSAKGKGVQELMAKLANDSPLAIEWLKNEFDLKLDLLAQLGGHSVARTHRSSGKLPPGFEIVSALSNNLKKLAETKPELVKINLDSKVVDIHEKDGSISAVVYEDKNGEKHMVSANDVVFCSGGFGFSKEMLKEYAPELVNLPTTNGQQTTGDGQRLLQKLGADLIDMDQIQVHPTGFIDPNDRSSSWKFLAAESLRGLGGILLNPITGRRFVNELTTRDVVTAAIQKVCPQEDNRALLVMGEKMYTDLKNNLDFYMFKKLVQKLTLSQVVSEYNLPITVAQLCEELQTYSSFTTKADPLGRTVILNEFGSDVTPETVVFIGEVTPVVHFTMGGARINVKAQVIGKNDERLLKGLYAAGEVSGGVHGANRLGGSSLLECVVFGRTAAESIANDRK | Cofactor: Binds 1 FAD per monomer.
Function: Irreversibly catalyzes the reduction of fumarate to succinate. Together with the second isozyme of soluble fumarate reductase (OSM1), essential for anaerobic growth. Involved in maintaining redox balance. Reduction of fumarate is the main source of succinate during fermentation, and under anaerobic conditions, the formation of succinate is strictly required for the reoxidation of FADH(2).
PTM: The N-terminus is blocked.
Catalytic Activity: NAD(+) + succinate = fumarate + H(+) + NADH
Sequence Mass (Da): 50844
Sequence Length: 470
Subcellular Location: Cytoplasm
EC: 1.3.1.6
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Q6QGJ4 | MITAMYAVGPNGEFGLRGKLPWGSFKEELDAFYSQLDVLNPDNIIIGAGTYLALPYAVRERMIGASDLFIRADRPLPDDITHDIYTPISMIGDTLPTFLKDQQTVVLGGANLLLEMYQHGHIESAFVSTIFSEQKLEADTHLDSMILDYNYESTRLVYAVGANSDNSLRFVQELVTY | Function: Provides the tetrahydrofolates necessary for the synthesis of nucleotides and amino acids. Bacteriophage T5 induces high levels of dihydrofolate reductase in the host cell, probably for the viral replication.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Mass (Da): 19776
Sequence Length: 177
EC: 1.5.1.3
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B5XRB0 | MTSNERILQPFTLPNGTELKNRLLMAPMTTCTGYFDGTVTSELVEYYRARAGSIGTIIVECCFIDDYGLAFPGAIGIDNDEKIAGLAKIAEAIKAQGSKAILQIYHGGRMVDPQLIGGRQPVAPSAIAAPREGAAMPRALSGEEVEGMIAKFGDGVRRAILAGFDGVEIHGANTYLIQQFYSPNSNQRDDEWGGSRDNRARFPLAVLDITHKMARQYADDAFIIGYRFSPEEMEVPGIRFDDTMYLLEKLAARGVDYLHFSVGATLRPSIVDTSDPTPLIEKYCAMRSETLAQVPVMGVGGVVNVADAELGLDHGYDLIAVGRACIAYPDWAARIAAGEELELFIDSTQREALHIPEPLWRFSLVEAMIRDMSMGDAKFKPGMFVETVQDDANELVINVSLENDHIADIELAASPVQTVEFTTSFEEIRERILTANTPHVDAISGATSQSEAVKKAVAKAMLKSSKALAAEEGGNDAAPKSYDVVVVGSGGAGLAAAIQAHDEGASVLIVEKMPTIGGNTIKASAGMNAAETRFQRVKGIQDSKELFYQETLKGGHNKNNPQLLRRFVENAPQAIEWLADRGIMLNDITTTGGMSIDRTHRPRDGSAVGGYLISGLVRNITKRGIDVLLDTSVEEILMSGDEVSGVRLVNDEKEVIEVQTKSIVVATGGFSANSAMVVKYRPDLDGFVTTNHKGATGSGIALLERIGAGTVDMGEIQIHPTVEQQTSYLISESIRGGGAILVNQQGNRFFNEMETRDKVSAAIIALPEHYAYIVFDEHVRAKNKAADEYIAKGFVTSASSPRELAEKLGMDYHAFLATLECYNGAVEKQHDEQFGRTTALRAPINEGPFHAIRIAPGVHHTMGGVTINTDGEVLNVDQQPIRGAYAAGEVVGGIHGGNRIGGNAVADIIIFGTLAGHQAAKRARG | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the anaerobic reduction of fumarate to succinate . Uses NADH as the inherent electron donor in this process . Is involved in anaerobic fumarate respiration in K.pneumoniae .
PTM: Is flavinylated on Thr-447 by ApbE2, encoded in a neighboring gene . Flavinylation is essential for catalytic activity .
Catalytic Activity: NAD(+) + succinate = fumarate + H(+) + NADH
Sequence Mass (Da): 99523
Sequence Length: 925
Domain: Consists of three domains. The first domain of FRD (Oxidored_FMN, PF00724) carries a non-covalently bound FMN and is used for NADH oxidation. The second, FMN_bind domain (PF04205) contains a covalently bound FMN, that acts as an electron carrier between the two other domains of FRD. The C-terminal FAD_binding_2 domain contains a non-covalently bound FAD and forms a site for fumarate reduction.
Subcellular Location: Cytoplasm
EC: 1.3.1.6
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Q5A446 | MKIQQLIVFLFAVVLIDARTPKRYSELDIVMSTCTTFIGKYGTVCTSTGKRSTNWNCYCKTDAGFGTISDCLVRGFNNNTNIISKFTESCNMTESKFHAKYDKIQAEFKTNGTEYAKMTTKSSSGSKTSASASKSSKSTGSSNASKSSTNAHGSNSSTSSTSSSSSKSGKGNSGTSTTETITTPLLIDYKKFTPYKDAYQMSNNNFNLSINYGSGLLGYWAGILAIAIFANMIKKMFPSLTNYLSGSISNLFRKHLFLPATFRKKKAQEFSIGVYGFFDGLIPTRLETIIVVIFVVLTGLFSALHIHHVKDNPQYATKNAELGHLIADRTGILGTFLIPLLILFGGRNNFLQWLTGWDFATFIMYHRWISRVDVLLIIVHAITFSVSDKATGKYNTRMKRDFMIWGTVSTICGGFILFQAMLFFRRKCYEVFFLIHIVLVVFFVVGGYYHLESQGYGDFMWAAIAVWAFDRVVRLGRIFFFGARKATVSIKGDDTLKIEVPKPKYWKSVAGGHAFIHFLKPTLFLQSHPFTFTTTESNDKIVLYAKIKNGITSNIAKYLSPLPGNTATIRVLVEGPYGEPSSAGRNCKNVVFVAGGNGIPGIYSECVDLAKKSKNQSIKLIWIIRHWKSLSWFTEELEYLKKTNVQSTIYVTQPQDCSGLECFEHDVSFEKKSDEKDSVESSQYSLISNIKQGLSHVEFIEGRPDISTQVEQEVKQADGAIGFVTCGHPAMVDELRFAVTQNLNVSKHRVEYHEQLQTWA | Function: Ferric reductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane. Also participates in Cu(2+) reduction and Cu(+) uptake (By similarity). Involved in maintenance of cell wall integrity (CWI), mitochondrial function, and interaction between the pathogen and the host.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84888
Sequence Length: 760
Subcellular Location: Cell membrane
EC: 1.16.1.9
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P32791 | MVRTRVLFCLFISFFATVQSSATLISTSCISQAALYQFGCSSKSKSCYCKNINWLGSVTACAYENSKSNKTLDSALMKLASQCSSIKVYTLEDMKNIYLNASNYLRAPEKSDKKTVVSQPLMANETAYHYYYEENYGIHLNLMRSQWCAWGLVFFWVAVLTAATILNILKRVFGKNIMANSVKKSLIYPSVYKDYNERTFYLWKRLPFNFTTRGKGLVVLIFVILTILSLSFGHNIKLPHPYDRPRWRRSMAFVSRRADLMAIALFPVVYLFGIRNNPFIPITGLSFSTFNFYHKWSAYVCFMLAVVHSIVMTASGVKRGVFQSLVRKFYFRWGIVATILMSIIIFQSEKVFRNRGYEIFLLIHKAMNIMFIIAMYYHCHTLGWMGWIWSMAGILCFDRFCRIVRIIMNGGLKTATLSTTDDSNVIKISVKKPKFFKYQVGAFAYMYFLSPKSAWFYSFQSHPFTVLSERHRDPNNPDQLTMYVKANKGITRVLLSKVLSAPNHTVDCKIFLEGPYGVTVPHIAKLKRNLVGVAAGLGVAAIYPHFVECLRLPSTDQLQHKFYWIVNDLSHLKWFENELQWLKEKSCEVSVIYTGSSVEDTNSDESTKGFDDKEESEITVECLNKRPDLKELVRSEIKLSELENNNITFYSCGPATFNDDFRNAVVQGIDSSLKIDVELEEESFTW | Function: Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane. Also participates in Cu(2+) reduction and Cu(+) uptake.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 78854
Sequence Length: 686
Subcellular Location: Cell membrane
EC: 1.16.1.9
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P0DTV5 | DLLGTLGNLPLPFI | Function: Peptide with unknown biological function that may act on skin macrophages to produce a cytokine-mediated stimulation of the adaptive immune system in response to invasion by microorganisms . It does not show antimicrobial and hemolytic activities but stimulates production of the pro-inflammatory cytokines TNF-alpha and IL-1beta by mouse peritoneal macrophages and does not potentiate the stimulation produced by lipopolysaccharide (LPS) . The peptide increases IL-12 production in both unstimulated and LPS-stimulated cells, but it does not stimulate IL-6 production in a significant manner . Stimulates insulin release from pancreatic beta-cells in a dose-dependent manner . This insulinotropic activity is relatively weak compared to that of GLP-1 . Acts without effects on membrane depolarization or changes in calcium current . Insulin release is predominantly mediated by the K(ATP) channel-independent pathway . Like GLP-1, but in a less potent manner, this peptide stimulates beta-cell proliferation . In a comparable potency to that provided by GLP-1, also provides protection of cells against cytokine-induced apoptosis .
PTM: Ile-14 amidation is not necessary for insulin release stimulation, since the synthetic non-amidated peptide shows the same activity as the amidated peptide.
Sequence Mass (Da): 1483
Sequence Length: 14
Subcellular Location: Secreted
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P36033 | MHWTSILSAILLFCLSGARASPAKTVIRNKVPLLVTNACTRIFQKVTWEYTSKSKRSSPVCSYEPAFQSMLYCIYETLDEKGYSNKTLEKTFSTIKKNCASYSDALQNMTNSEFYDVLNNGTRHMTPYVKGSANLTYPVEMDTQLRKAYYHALHGFYANLDVGNIYGGIICAYFVAIMAFAGVLHCMNYTPFKTVLLKQKLVGYVRGYLTLPTIGSKHASDFSYFRIFTGYLPTRLEGIIILGYLVLHTVFLAYGYEYDPENIIFKSRRVQVARYVADRSGVLAFAHFPLIVLFAGRNNFLEYISGVKYTSFIMFHKWLGRMMFLDAMIHGSAYTSYTVANKTWATSKNRLYWQFGVAALCLAGTMVFFSFAVFRKYFYEAFLFLHIVLGAMFFYACWEHVVSLSGIEWIYTAIAIWIVDRIIRIIKASYFGFPKASLQLIGDDLIRLTVKKPARPWRAKPGQYVFVSFLHPLYFWQSHPFTVLDSVSKNGELVIILKEKKGVTRLVKKYVCRNGGKTSMRLAIEGPYGSSSPVNNYNNVLLLTGGTGLPGPIAHAIKLGKTSAAAGKQSVKLVIAVRGFDVLEAYKPELMCLENLNVQLHIYNTMEVPSLTPSDSLDISQQDEKADEKGTVVATTLEKSANPLGFDGVVFHCGRPNVKELLHEAAELSGSLSVVCCGPPIFVDKVRNETAKIVLDKSAKAIEYFEEYQCW | Function: Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane. Also participates in Cu(2+) reduction and Cu(+) uptake.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80072
Sequence Length: 711
Subcellular Location: Cell membrane
EC: 1.16.1.9
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P25437 | MKSRAAVAFAPGKPLEIVEIDVAPPKKGEVLIKVTHTGVCHTDAFTLSGDDPEGVFPVVLGHEGAGVVVEVGEGVTSVKPGDHVIPLYTAECGECEFCRSGKTNLCVAVRETQGKGLMPDGTTRFSYNGQPLYHYMGCSTFSEYTVVAEVSLAKINPEANHEHVCLLGCGVTTGIGAVHNTAKVQPGDSVAVFGLGAIGLAVVQGARQAKAGRIIAIDTNPKKFDLARRFGATDCINPNDYDKPIKDVLLDINKWGIDHTFECIGNVNVMRAALESAHRGWGQSVIIGVAVAGQEISTRPFQLVTGRVWKGSAFGGVKGRSQLPGMVEDAMKGDIDLEPFVTHTMSLDEINDAFDLMHEGKSIRTVIRY | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates.
Catalytic Activity: NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-formylglutathione
Sequence Mass (Da): 39359
Sequence Length: 369
Subcellular Location: Cytoplasm
EC: 1.1.1.284
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P44557 | MEIKQINSTIKSRAAVAFAPNQPLQIVEIDVEMPRKGEVLIRNTHTGVCHTDAFTLSGSDPEGVFPVVLGHEGAGVVVAVGEGVLSVKPGDHVIPLYTAECGECEFCRSGKTNLCVSVRDTQGKGLMPDCTTRFSYQGQPIYHYMGCSTFSEYSVVAEVSLAKINPEANHEQVCLLGCGVTTGIGAVHNTAKVQEGDSVAVFGLGAIGLAVVQGARQAKAGRIIAIDTNPAKFELAKQFGATDCLNPNDYDKPIKDVLLDINKWGIDHTFECIGNVNVMRQALESAHRGWGQSIIIGVAGAGQEISTRPFQLVTGRVWKGSAFGGVKGRSELPQMVEDSMKGDIQLEPFVTHTMPLDKINEAFELMHEGKSIRTVIHY | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-formylglutathione
Sequence Mass (Da): 40651
Sequence Length: 378
Subcellular Location: Cytoplasm
EC: 1.1.1.284
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P73138 | MKSRAAVAFEVGKPLQIVEIDVAPPQQGEVLVKITHTGVCHTDAFTLSGDDPEGLFPVVLGHEGAGIVVEVGEGVTSVQLGDHVIPLYTAECGKCLFCRSGKTNLCVAVRATQGKGVMPDGTSRFSYNGQSLYHYMGCSTFSEYTVVAEVSLAKINPEANHEHVCLLGCGVTTGIGAVHNTAKVQPGDSVAVFGLGGIGLAVVQGARQAKAGRIIAIDTNPAKFELAKQMGATDCINPKDHDQPIQQVIVEMTGWGVDHSFECIGNVEVMRSALECAHRGWGQSVIIGVAGAGQEISTRPFQLVTGRKWMGTAFGGVKGRSQLPGMVEQSMRGEIQLAPFVTHTMELKDINQAFDLMHDGKSIRSVIHY | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-formylglutathione
Sequence Mass (Da): 39211
Sequence Length: 369
Subcellular Location: Cytoplasm
EC: 1.1.1.284
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A2A2Y4 | MFASCHCVPRGRRTMKMIHFRSSSVKSLSQEMRCTIRLLDDSEISCHIQRETKGQFLIDHICNYYSLLEKDYFGIRYVDPEKQRHWLEPNKSIFKQMKTHPPYTMCFRVKFYPHEPLKIKEELTRYLLYLQIKRDIFHGRLLCSFSDAAYLGACIVQAELGDYDPDEHPENYISEFEIFPKQSQKLERKIVEIHKNELRGQSPPVAEFNLLLKAHTLETYGVDPHPCKDSTGTTTFLGFTAAGFVVFQGNKRIHLIKWPDVCKLKFEGKTFYVIGTQKEKKAMLAFHTSTPAACKHLWKCGVENQAFYKYAKSSQIKTVSSSKIFFKGSRFRYSGKVAKEVVEASSKIQREPPEVHRANITQSRSSHSLNKQLIINMEPLQPLLPSPSEQEEELPLGEGVPLPKEENISAPLISSSPVKAAREYEDPPSEEEDKIKEEPLTISELVYNPSASLLPTPVDDDEIDMLFDCPSRLELEREDTDSFEDLEADENAFLIAEEEELKEARRALSWSYDILTGHIRVNPLVKSFSRLLVVGLGLLLFVFPLLLLLLESGIDLSFLCEIRQTPEFEQFHYEYYCPLKEWVAGKVHLILYMLGCS | Function: Putative tumor suppressor gene that may be implicated in the origin and progression of lung cancer.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 68772
Sequence Length: 597
Subcellular Location: Membrane
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Q7Z6J6 | MLSRLMSGSSRSLEREYSCTVRLLDDSEYTCTIQRDAKGQYLFDLLCHHLNLLEKDYFGIRFVDPDKQRHWLEFTKSVVKQLRSQPPFTMCFRVKFYPADPAALKEEITRYLVFLQIKRDLYHGRLLCKTSDAALLAAYILQAEIGDYDSGKHPEGYSSKFQFFPKHSEKLERKIAEIHKTELSGQTPATSELNFLRKAQTLETYGVDPHPCKDVSGNAAFLAFTPFGFVVLQGNKRVHFIKWNEVTKLKFEGKTFYLYVSQKEEKKIILTYFAPTPEACKHLWKCGIENQAFYKLEKSSQVRTVSSSNLFFKGSRFRYSGRVAKEVMESSAKIKREPPEIHRAGMVPSRSCPSITHGPRLSSVPRTRRRAVHISIMEGLESLRDSAHSTPVRSTSHGDTFLPHVRSSRTDSNERVAVIADEAYSPADSVLPTPVAEHSLELMLLSRQINGATCSIEEEKESEASTPTATEVEALGGELRALCQGHSGPEEEQVNKFVLSVLRLLLVTMGLLFVLLLLLIILTESDLDIAFFRDIRQTPEFEQFHYQYFCPLRRWFACKIRSVVSLLIDT | Function: May be involved in regulation of cell migration . May regulate cell-matrix interactions via its interaction with ITGB5 and modifying ITGB5 cytoplasmic tail interactions such as with FERMT2 and TLN1. May regulate ROCK1 kinase activity possibly involved in regulation of actin stress fiber formation .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 65065
Sequence Length: 570
Subcellular Location: Membrane
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Q16658 | MTANGTAEAVQIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPGPDCRFLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTADHRFLRHDGRLVARPEPATGYTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTATGGVQSTASSKNASCYFDIEWRDRRITLRASNGKFVTSKKNGQLAASVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVAIKVGGRYLKGDHAGVLKASAETVDPASLWEY | Function: Actin-binding protein that contains 2 major actin binding sites . Organizes filamentous actin into parallel bundles . Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers . Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration . Mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to NGF .
PTM: Phosphorylation at Ser-39 inhibits actin-binding . Phosphorylation is required for the reorganization of the actin cytoskeleton in response to NGF .
Sequence Mass (Da): 54530
Sequence Length: 493
Domain: Composed of four fascin beta-trefoil domains.
Subcellular Location: Cytoplasm
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Q61553 | MTANGTAEAVQIQFGLISCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLGRYLAADKDGNVTCEREVPDGDCRFLVVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQSVSPAEKWSVHIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTSDHRFLRHDGRLVARPEPATGFTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNVSTRQGMDLSANQDEETDQETFQLEIDRDTRKCAFRTHTGKYWTLTATGGVQSTASTKNASCYFDIEWCDRRITLRASNGKFVTAKKNGQLAASVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYDVFQLEFNDGAYNIKDSTGKYWTVGSDSSVTSSSDTPVDFFLEFCDYNKVALKVGGRYLKGDHAGVLKACAETIDPASLWEY | Function: Actin-binding protein that contains 2 major actin binding sites (By similarity). Organizes filamentous actin into parallel bundles . Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers (By similarity). Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration . Mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to NGF (By similarity).
PTM: Phosphorylation at Ser-39 inhibits actin-binding. Phosphorylation is required for the reorganization of the actin cytoskeleton in response to NGF.
Sequence Mass (Da): 54508
Sequence Length: 493
Domain: Composed of four fascin beta-trefoil domains.
Subcellular Location: Cytoplasm
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Q1LY10 | MDDQKESLRKIITTLALKNEEIQNFICSLKQSLENLEANSNRVQEDLESEFSSLHSVLDDLKEGMVTRIKQERASRTYELQSQLGACTKALESSEELLEFANQTLCSSENDSFTQAAKDIKDSVTMAPAFRLSLKAKASDSMNHMMVDFTHERNLLQSITFLPVPATPEIHVADCQVFDNTVTVVWTLPEPDSKIDHYILEHRKTNHEGPPRAREDYPWMVVEGIKETEYTLTGVRFDTRYMTFRVKACNKAVAGEFSEPVTLETHAFVFKLDASSSHQNLKVEDLSVEWDSSGGKVAVQDIRKEKNRTNSPMHSPARTAMMSPKRAPSARVGRDRFTAESYTVLGDTMIDAGQHYWEVRFDKESKAFAAGVALRSLGRFDQLGKSNASWCIHLNNWLQQSLTAKHNNKARTLDCSIPDRIGIYCNYEEGTLSFYNSRNKTLLHTFRTKFQQPVIPAFMVWNGSFSVQTGLQVPSIVLSGQKRNSNTSSSNASLT | Function: May be involved in microtubule organization and stabilization.
Sequence Mass (Da): 55876
Sequence Length: 495
Domain: B30.2 box contains a microtubule-binding site.
Subcellular Location: Cytoplasm
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Q9BTV5 | MEEQREALRKIIKTLAVKNEEIQSFIYSLKQMLLNVEANSAKVQEDLEAEFQSLFSLLEELKEGMLMKIKQDRASRTYELQNQLAACTRALESSEELLETANQTLQAMDSEDFPQAAKQIKDGVTMAPAFRLSLKAKVSDNMSHLMVDFAQERQMLQALKFLPVPSAPVIDLAESLVADNCVTLVWRMPDEDSKIDHYVLEYRRTNFEGPPRLKEDQPWMVIEGIRQTEYTLTGLKFDMKYMNFRVKACNKAVAGEFSEPVTLETPAFMFRLDASTSHQNLRVDDLSVEWDAMGGKVQDIKAREKDGKGRTASPINSPARGTPSPKRMPSGRGGRDRFTAESYTVLGDTLIDGGEHYWEVRYEPDSKAFGVGVAYRSLGRFEQLGKTAASWCLHVNNWLQVSFTAKHANKVKVLDAPVPDCLGVHCDFHQGLLSFYNARTKQVLHTFKTRFTQPLLPAFTVWCGSFQVTTGLQVPSAVRCLQKRGSATSSSNTSLT | Function: May be involved in microtubule organization and stabilization.
Sequence Mass (Da): 55820
Sequence Length: 496
Domain: B30.2 box contains a microtubule-binding site.
Subcellular Location: Cytoplasm
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Q1DFW5 | MTLRAMTDVGAELGLSPEDVLPWGTHRAKVSLDALGKRGGRQGRLVLVSAINPTPPGEGKTTMSVALAMGLRKRGRRAVAALREPSLGPVFGVKGGGTGGGQASLEPAADINLHFTGDLHAITSANNLLSALVDNAVFYGQPVALDATRVRWRRALDMNDRFLRNVIVGLGGKAQGVPREDHFDITAASEVMAILALAEGLKDLEARLGRVIIGHTRDGQPVRARDVDAAASMVALLKDALMPNLAQTREGGPALVHAGPFANIAHGCSSVMGTRMGLAYADEVITEAGFGFDLGAEKFLDIKCRGSGLWPRGVVLVVTLRALKHHGGASPARVAEPDREALVRGFAHLEKHLESVAAFGLPAVLCVNRFPQDTESELEELRAFGKARGVETAVCDGFSRGGDGSLELADCVLEMLDGTDAAPPQPRFLYDVAQTPEEKVAAIARTVYGADDVAFTASAKKDLDAIRELGGAGLPVCMAKTHLSLSDDPTKLGRPRGFTLTVREVRLSAGAGFMVALTGEILTMPGLPREPAARRVTVHDDGRVTGLMQGE | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 58072
Sequence Length: 551
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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