ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P08495 | MGLIVQKFGGTSVGSVEKIQNAANRAIAEKQKGHQVVVVVSAMGKSTDELVSLAKAISDQPSKREMDMLLATGEQVTISLLSMALQEKGYDAVSYTGWQAGIRTEAIHGNARITDIDTSVLADQLEKGKIVIVAGFQGMTEDCEITTLGRGGSDTTAVALAAALKADKCDIYTDVPGVFTTDPRYVKSARKLEGISYDEMLELANLGAGVLHPRAVEFAKNYQVPLEVRSSTETEAGTLIEEESSMEQNLIVRGIAFEDQITRVTIYGLTSGLTTLSTIFTTLAKRNINVDIIIQTQAEDKTGISFSVKTEDADQTVAVL... | Function: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine.
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-asparta... |
P94417 | MKVVKFGGSSLASGAQLDKVFHIVTSDPARKAVVVSAPGKHYAEDTKVTDLLIACAEQYLATGSAPELAEAVVERYALIANELQLGQSIIEKIRDDLFTLLEGDKSNPEQYLDAVKASGEDNNAKLIAAYFRYKGVKAEYVNPKDAGLFVTNEPGNAQVLPESYQNLYRLRERDGLIIFPGFFGFSKDGDVITFSRSGSDITGSILANGLQADLYENFTDVDAVYSVNPSFVENPKEISELTYREMRELSYAGFSVFHDEALIPAFRAGIPVQIKNTNNPSAEGTRVVSKRDNTNGPVVGIASDTGFCSIYISKYLMNRE... | Function: Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine.
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-asparta... |
P08660 | MSEIVVSKFGGTSVADFDAMNRSADIVLSDANVRLVVLSASAGITNLLVALAEGLEPGERFEKLDAIRNIQFAILERLRYPNVIREEIERLLENITVLAEAAALATSPALTDELVSHGELMSTLLFVEILRERDVQAQWFDVRKVMRTNDRFGRAEPDIAALAELAALQLLPRLNEGLVITQGFIGSENKGRTTTLGRGGSDYTAALLAEALHASRVDIWTDVPGIYTTDPRVVSAAKRIDEIAFAEAAEMATFGAKVLHPATLLPAVRSDIPVFVGSSKDPRAGGTLVCNKTENPPLFRALALRRNQTLLTLHSLNMLH... | Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Mass (Da): 48532
Sequence Length: 449
Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
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O88845 | MRGAGPSPRHSPRALRPDPGPAMSFFRRKVKGKEQEKTLDVKSTKASVAVHSPQKSTKNHALLEAAGPSHVAINAISANMDSFSSSRTATLKKQPSHMEAAHFGDLGRSCLDYQTQETKSSLSKTLEQVLRDTVVLPYFLQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKRHETPASSVTEALDRRLGDSSSAPLLVTQSEGTDLSSRTQNPQNHLLLSQEGHSARSLHREVARTGSHQIPTDSQDSSSRLAVGSRNSCSSPLRELSEKLMKSIEQDAVNTFTKYISPDAAKPIPITEAM... | Function: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is... |
O43687 | MGQLCCFPFSRDEGKISELESSSSAVLQRYSKDIPSWSSGEKNGGEPDDAELVRLSKRLVENAVLKAVQQYLEETQNKNKPGEGSSVKTEAADQNGNDNENNRK | Function: Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by i... |
O55074 | MGQLCCFPFARDEGKICEKDRREPEDAELVRLSKRLVENAVLKAVQQYLEETQNKKQPGEGNSTKAEEGDRNGDGSDNNRK | Function: Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by i... |
Q5ZJJ5 | MNPFWSMSAASGRKRPEADEKTLSGELRTSPPRASAKKQLPSVPKNAVPVTKPASPAMSSQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLVFDLPVFHPLVDPLSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTTSPLNPEAAVLYEKDIQLFKSKVVDSVKLCSSHLFDQPKIEDPYAIVFSPWNPAIHDEAREKMLTQKKKPEDQHCKSMHVSGLSWVKPGSVQPFSKEEKTMPT | Function: May function to promote vesicle trafficking and/or fusion. May also regulate apoptosis (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33304
Sequence Length: 293
Subcellular Location: Cytoplasm
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Q9H8T0 | MNPFWSMSTSSVRKRSEGEEKTLTGDVKTSPPRTAPKKQLPSIPKNALPITKPTSPAPAAQSTNGTHASYGPFYLEYSLLAEFTLVVKQKLPGVYVQPSYRSALMWFGVIFIRHGLYQDGVFKFTVYIPDNYPDGDCPRLVFDIPVFHPLVDPTSGELDVKRAFAKWRRNHNHIWQVLMYARRVFYKIDTASPLNPEAAVLYEKDIQLFKSKVVDSVKVCTARLFDQPKIEDPYAISFSPWNPSVHDEAREKMLTQKKPEEQHNKSVHVAGLSWVKPGSVQPFSKEEKTVAT | Function: Component of the FTS/Hook/FHIP complex (FHF complex) . The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). Regulates apoptosis by enhancing phosphorylation and activation of AKT1. Increases release of TNFSF6 via the ... |
Q70DU8 | MAAKKVFGSAEASNLVTELRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTSLTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLTKLLEQYLDPSAVRVVEGAVTETSALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIVGKWGCNNGQACVSPDYILTTKEYAPKLIDAMKLELEKFYGKNPIESKDMSRIVNSNHFDRLSKLLDEKEVSDKIVYGG... | Function: Involved in oxidative stress tolerance by detoxifying reactive aldehydes derived from lipid peroxidation. Medium- to long-chain saturated aldehydes are preferred substrates, while the short-chain aldehyde propanal is a weak substrate. Is strictely NAD(+) specific.
Catalytic Activity: an aldehyde + H2O + NAD(+... |
Q8W033 | MTKLLEINHIQTLCFAKGFSPARLNVATSPFRISRRGGGGYCSNACIPYRLKFTCYATLSAVVKEQASDFSGKEAALLVDELRSNFNSGRTKSYEWRISQLQNIARMIDEKEKCITEALYQDLSKPELEAFLAEISNTKSSCMLAIKELKNWMAPETVKTSVTTFPSSAQIVSEPLGVVLVISAWNFPFLLSVEPVIGAIAAGNAVVLKPSEIAPAASSLLAKLFSEYLDNTTIRVIEGGVPETTALLDQKWDKIFFTGGARVARIIMAAAARNLTPVVLELGGKCPALVDSDVNLQVAARRIIAGKWACNSGQACIGVD... | Function: Involved in oxidative stress tolerance by detoxifying reactive aldehydes derived from lipid peroxidation. Medium- to long-chain saturated aldehydes are preferred substrates, while the short-chain aldehyde propanal is a weak substrate. Can use both NAD(+) and NADP(+), but the coenzyme preference is substrate d... |
Q7SY23 | MLRARSAVSQSWKGFKTFSCVAVEVKNEPVLEFKEGSKERAELEEALRNLKGKTEEIPCVIGNEEVWTKDIRFQLSPFNHSHQVAKFCYADKDLLNKAIEASVAARREWDLKPVSDRAQIFFKAADIISGPKRAEVLAKTMIGQGKTVVQAEIDAAPELIDFFRFNAKHAIELEDQQPLDSDGSTNTMLYRGLEGFVAAVAPFNFTAIGGNLAGTPALMGNVVLWKPSDTAMSASYAVYKILRESGLPPNIIQFVPADGPVFGDTVTSSEHLAGINFTGSVPTFKRLWKQVAQNLDIYKNFPRVAGECGGKNFHFVHKSA... | Function: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles (By similarity).
Catalytic Activity: H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-g... |
P30038 | MLLPAPALRRALLSRPWTGAGLRWKHTSSLKVANEPVLAFTQGSPERDALQKALKDLKGRMEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKPIADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVELEGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFHTFPRLAGECGGKNF... | Function: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, g... |
Q8CHT0 | MLPLPSLRRSLLSHAWRGAGLRWKHTSSLKVTNEPILAFSQGSPERDALQKALKDLKGQMEAIPCVVGDEEVWTSDIQYQLSPFNHAHKVAKFCYADKALLNRAIDAALAARKEWDLKPMADRAQVFLKAADMLSGPRRAEVLAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKFAVELEGEQPISVPPSTNHTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNIIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWRQVAQNLDRFRTFPRLAGECGGKNFH... | Function: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, g... |
P0C2X9 | MLPPALLRRSLLSYAWRGSGLRWKHASSLKVANEPILAFTQGSPERDALQKALNDLKDQTEAIPCVVGDEEVWTSDVRYQLSPFNHGHKVAKFCYADKALLNKAIEAAVLARKEWDLKPVADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKFAVELEGEQPISVPPSTNHVVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAMLASYAVYRILREAGLPPNVIQFVPADGPTFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQNLDRFRTFPRLAGECGGKNFH... | Function: Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, g... |
P20292 | MDQETVGNVVLLAIVTLISVVQNGFFAHKVEHESRTQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWSAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSVAGIFNYYLIFFFGSDFENYIKTISTTISPLLLIP | Function: Required for leukotriene biosynthesis by ALOX5 (5-lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes.
Location Topology: Multi-pass membran... |
P30357 | MDQEAVGNVVLLAIVTLISVVQNGFFAHKVEHESRNQNGRSFQRTGTLAFERVYTANQNCVDAYPTFLAVLWTAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFLMSLAGILNYCLILLFGSDFENYIKTISTT | Function: Required for leukotriene biosynthesis by ALOX5 (5-lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity).
Location Topology: Mu... |
P30358 | MDQETVGNIVLLAIVTLISVVQNGFFAHKVEHESKTHNGRSFQRTGPLAFERVYTANQNCVDAYPTFLVMLWSAGLLCSQVPAAFAGLMYLFVRQKYFVGYLGERTQSTPGYIFGKRIILFLFAMSLAGILNYFLIAFFGSDFENYIKTVTTT | Function: Required for leukotriene biosynthesis by ALOX5 (5-lipoxygenase). Anchors ALOX5 to the membrane. Binds arachidonic acid, and could play an essential role in the transfer of arachidonic acid to ALOX5. Binds to MK-886, a compound that blocks the biosynthesis of leukotrienes (By similarity).
Location Topology: Mu... |
Q2KJC9 | MWRVPGLLCVRVARKSKFSGSWNRPAAFMSTLLINQPQYAWLKELGLREENDGVYNGSWGGRGEVITTYCPANNEPIARVRQASMADYEETVEKAREAWSIWADVPAPKRGEVVRQIGDALREKIQVLGSLVSLEMGKILVEGVGEVQEYVDVCDYAVGLSRMIGGPILPSERPGHALIEQWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNACLWKGAPTTSLISVAVTKIIAKVLEDNKLPGAICSLTCGGADIGTAMAKDERVDLLSFTGSTQVGKQVALMVQERFGRSLLELGGNNAIIAFEDADLSLVVPSALF... | Function: Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism.
Catalytic Activity: H2O... |
P10593 | MAETNPELSDLMAQTNKKIVPKFTEIFPVEDVNYPYSAFIASVRKDVIKHCTDHKGIFQPVLPPEKKVPELWFYTELKTRTSSITLAIRMDNLYLVGFRTPGGVWWELARPATPTSSATTPGGSASAAGTRTSSATRVWRPSPWAARDDQGRQRPGEEEEDGDTGGGGGADADADAGGAELAAAAAAADPQADTKSKLVKLVVMVCEGLRFNTLSRTVDAGFNSQHGVTLTVTQGKQVQKWDRISKAAFEWADHPTAVIPDMQKLGIKDKNEAARIVALVKNQTTAAAAAATAASADNDDDEA | Function: A possible regulatory factor for the synthesis of zeins, the major group of storage proteins.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 32428
Sequence Length: 303
Subcellular Location: Cytoplasm
EC: 3.2.2.22
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Q9FYL3 | MSSTISLKPTHLILSSFSTGKVLQFRRSRFSHTPSSSSSRYRTLVAQLGFRPDSFDFIKDHAENLLYTIADAAVSSSETFESVAGTTTKTTQSNDWFSGIANYMETILKVLKDGLSTVHVPYSYGFAIILLTVLVKAATFPLTKKQVESAMAMKSLTPQIKAIQERYAGDQEKIQLETARLYKLAGINPLAGCLPTLATIPVWIGLYRALSNVADEGLLTEGFFWIPSLAGPTTVAARQNGSGISWLFPFIEGHPPLGWPDTLAYLVLPLLLVFSQYLSIQIMQSSQSNDPAMKSSQAVTKLLPLMIGYFALSVPSGLSL... | Function: Required for the insertion of some light harvesting chlorophyll-binding proteins (LHCP) into the chloroplast thylakoid membrane. Plays a role in the accumulation of some cytochrome b6f components in the thylakoid membrane . Required for the assembly and/or stability of the F(1)F(0) ATP synthase in chloroplast... |
Q9YAW1 | MSIEPQKPNTILVGRKPTINYVMAALKLLNEEGAPEVVIKARGRNICNAVDTVEMLKNLFIKNLVIKKVNIYSESLDSEGKKKVSAIEIVVAKG | Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and function... |
Q8TXF9 | MAEEENVVYVGSKPVMNYVLACITQFNEGANEVRIKARGRAISRAVDVAEIVRNRFMPEVEVKDIKIGTEELETEEGDTVNVSTIEIVLEKPV | Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and function... |
P60849 | MSSGTPTPSNVVLIGKKPVMNYVLAALTLLNQGVSEIVIKARGRAISKAVDTVEIVRNRFLPDKIEIKEIRVGSQVVTSQDGRQSRVSTIEIAIRKK | Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. May be involved in DNA compaction. May bind rRNA and mRNA, playing a role in maintaining the structural and functional stability of RNA... |
Q9YAX2 | MACEGAPEVRIGRKPVMNYVLAILTTLMEQGTNQVVVKARGRNINRAVDAVEIVRKRFAKNIEIKDIKIDSQEIEVQTPEGQTRTRRVSSIEICLEKAGESA | Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and function... |
O28323 | MAEHVVYVGNKPVMNYVLATLTQLNEGADEVVIKARGRAISRAVDVAEIVRNRFMPGVKVKEIKIDTEELESEQGRRSNVSTIEIVLAK | Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and function... |
Q97ZF4 | MTEKLNEIVVRKTKNVEDHVLDVIVLFNQGIDEVILKGTGREISKAVDVYNSLKDRLGDGVQLVNVQTGSEVRDRRRISYILLRLKRVY | Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and function... |
P71011 | MFIEQMFPFINESVRVHQLPEGGVLEIDYLRDNVSISDFEYLDLNKTAYELCMRMDGQKTAEQILAEQCAVYDESPEDHKDWYYDMLNMLQNKQVIQLGNRASRHTITTSGSNEFPMPLHATFELTHRCNLKCAHCYLESSPEALGTVSIEQFKKTADMLFDNGVLTCEITGGEIFVHPNANEILDYVCKKFKKVAVLTNGTLMRKESLELLKTYKQKIIVGISLDSVNSEVHDSFRGRKGSFAQTCKTIKLLSDHGIFVRVAMSVFEKNMWEIHDMAQKVRDLGAKAFSYNWVDDFGRGRDIVHPTKDAEQHRKFMEYE... | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine, the other is coordinated via 3 cysteines and maybe direct contact with the SboA precursor.
Function: Catalyzes the formation of 3 thioether bonds during production of the sactipeptide subtilosin... |
Q0W252 | MPEDNVIFVGNKPVMNYVLAAVTQFNEGAKEVTIKARGRAISRAVDTAEVVRHRFLTDVEIDRIQISTEELASEKGEKINVSSIEIFLKRPRAATD | Function: Binds double-stranded DNA tightly but without sequence specificity. It is distributed uniformly and abundantly on the chromosome, suggesting a role in chromatin architecture. However, it does not significantly compact DNA. Binds rRNA and mRNA in vivo. May play a role in maintaining the structural and function... |
P00883 | MPHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKEN... | Function: Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein.
PTM: Asn-361 in form alpha is deaminated to Asp in form beta.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 39343
Se... |
B5DGM7 | MPHAFPFLTPDQKKELSDIALKIVAKGKGILAADESTGSVAKRFQSINTENTEENRRLYRQLLFTADDRAGPCIGGVIFFHETLYQKTDAGKTFPEHVKSRGWVVGIKVDKGVVPLAGTNGETTTQGLDGLYERCAQYKKDGCDFAKWRCVLKITSTTPSRLAIMENCNVLARYASICQMHGIVPIVEPEILPDGDHDLKRTQYVTEKVLAAMYKALSDHHVYLEGTLLKPNMVTAGHSCSHKYTHQEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNVMNQCPLHRPWALTFSYGRALQASALKAWGGKPGN... | Function: Plays a key role in glycolysis and gluconeogenesis.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 39556
Sequence Length: 363
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphat... |
P05062 | MAHRFPALTQEQKKELSEIAQSIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFSVDSSINQSIGGVILFHETLYQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAAN... | Function: Catalyzes the aldol cleavage of fructose 1,6-biphosphate to form two triosephosphates dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate in glycolysis as well as the reverse stereospecific aldol addition reaction in gluconeogenesis. In fructolysis, metabolizes fructose 1-phosphate derived from the ph... |
P79226 | MAHRFPALTPEQKKELSDIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDNSINQSIGGVILFHETLYQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRIADQCPSSLAIQENANTLARYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAEN... | Function: Catalyzes the aldol cleavage of fructose 1,6-biphosphate to form two triosephosphates dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate in glycolysis as well as the reverse stereospecific aldol addition reaction in gluconeogenesis. In fructolysis, metabolizes fructose 1-phosphate derived from the ph... |
P53448 | MTHQYPALTTEQKRELQDIAQRIVAPGKGILAADESTGSMAKRLNPIGVENTEENRRLYRQLLFTADERMDKCIGGVIFFHETLYQKADDGTPFAKMIKDRGIVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRSVLKISETSPSELAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAACYKALSDHHVYLEGTLLKPNMVTAGHSCPTKFSNQEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINNCPLTKPWALTFSYGRALQASALSAWRGVKEN... | Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 39475
Sequence Length: 363
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
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P53449 | LLKPNMVTPGHSCPTKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINTCPLVRPWALTFSYGRALQASALSAWRGQRDNANAATEEFVKRAEVNGLAALGKYEGSGDDSGAAGQSLYVANHAY | Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 14438
Sequence Length: 137
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
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Q9GKW3 | MPHSYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISERTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYTPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCPLPRPWALTFSYGRALQASALNAWRGQRDN... | Catalytic Activity: beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
Sequence Mass (Da): 39422
Sequence Length: 364
Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
EC: 4.1.2.13
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Q9USD4 | MTSKESICWYLANILLVTCIGYYSYKTPFTKVEESFAMQAIHDIQTYRWDLSKYDHLEFPGAVKRSFIPSLFIAVLSYIPSWFVNPLLAARWTIGYLSWESMNSVSCSISKRFGTLSGALFILFSCAQFHLVYYMSRPLSNIFGLIATNHSLSLLLKNNYYGSISILVFAAAIVRSEIALLLMCLILPLLLQRRITLSKLLLVGISSSLAAVGASFLIDSYFWGAWCWPELEAFLFNVVEGKSSDWGTSPFYYYFVRLPWLFLNPTTLLFLLISFVYIKPARLLIYVPLFFIFVYSFLGHKEWRFIIYSIPWFNAASAIG... | Function: Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha... |
P53730 | MRWSVLDTVLLTVISFHLIQAPFTKVEESFNIQAIHDILTYSVFDISQYDHLKFPGVVPRTFVGAVIIAMLSRPYLYLSSLIQTSRPTSIDVQLVVRGIVGLTNGLSFIYLKNCLQDMFDEITEKKKEENEDKDIYIYDSAGTWFLLFLIGSFHLMFYSTRTLPNFVMTLPLTNVALGWVLLGRYNAAIFLSALVAIVFRLEVSALSAGIALFSVIFKKISLFDAIKFGIFGLGLGSAISITVDSYFWQEWCLPEVDGFLFNVVAGYASKWGVEPVTAYFTHYLRMMFMPPTVLLLNYFGYKLAPAKLKIVSLASLFHII... | Function: Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha... |
Q750J3 | MSTTTKSKMEGPKTVVVTCGATVPFPGLVNAVLDRRVLAELAQCGFSRVMVQYGRGFAAEFERQVGAAGAVRAACDAEGLEGCDAHAWRWQGLEIIGFAFHAQMESLIGTSAALVVSHAGTGSILDALRQQKPLIVCVNEALLDNHQEQIARRFEALGHLWAIRADVDELAGALARSTRETLAPLPPAYKQGFAELLQDVAHR | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity).
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
Sequence Mass (Da)... |
Q4WQN1 | MLATKVCFVTVGATASFEELVRAALDPSFVTALEENGYSHLLVQYGKNAVIYENFLKQYPPERRPWRRINISGFSFHEHGLGGDFALAQADISKGRSGGLVISHAGSGTILEVLRMGIPLIVVPNPSLQDNHQEELARQLQKQGYVVASHYQNLCQALHQAEQLRARMLRWPPVRGPDQKNQPTLEQVMSDEMGFVD | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity).
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
Sequence Mass (Da)... |
Q5ABE5 | MFDWRRLKPLRPHQIFFFYTTIQNYSDNGYQYSYKSNQIKSNQIKLNQQQQTSRQLIRINNQLPPSVVLHNIIMKSILITTGATITFKSLIQIILSPQFLNNLIRLKINKLIIQYGHEIKNSINLSESFFNETINKYDLINLFNLEIEETPIGDDDDDEGIRLFKNSDIEILAFSYSSNINKYIENVDLIISHAGTGSIIDCLHLNKPLIVIVNDKLMDNHQLEIAQQFTKLNYCIYYSIKELEQYVNNNDNNKDSRFWNQLNQLINGELQLNKLPQTDGSIIETIICEELEK | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity).
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
Sequence Mass (Da)... |
Q6FVR6 | MSAFVTCGATVPFPALVEAVLAPEFVGCLSREGYRVLCVQFGRGYDFEAQFTSVTCTRMPLESAEVSELRQLVRDERVTVMGYKVQDVVVLGFAYSNNILQIIDRYGDVVISHAGTGSILDSLRLNKKLIVVVNHTLMDNHQKQIAEKFQNLGHILATNPTAIELCDAMKRLKHEDLIPLSSETNTEFMERLKSIAYS | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity).
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
Sequence Mass (Da)... |
P0CN89 | MAHPFTLLVTVGSTLFPSLTSHVLLPTFLSLLQSLGVQRLVVQYGRAELKLQDDVKQTLNIDSQGDGIGVWSDNDGDRVRDEKQNGMVVEVMRFTNDFEGLVGKSDAVISHAGSGSILTVLRRAPPIPLLVVPNRSLMDDHQSELADALYKDGYVMVASVEDLEEKVQPFLKIWPSQAKLFPETRKEVFREVVDDLMGYD | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity).
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
Sequence Mass (Da)... |
Q6BST1 | MTSVLFTSGATVTFRELIEVITSYDFIVETIIGNGITRMIVQYGNEIETGTQKHVSEEFYRQCVEDKELKQSLQLEVVSGSQNDSNVVTYRSNKYRGFEMVVFPFSNDIGSFISESDVVISHAGTGSIIDTLRLEKPLIVVTNDKLMNKHQEEVADELVKLGCCRKMTIEDMKSSQLKDCISEILSGPETFNKLPECSTTEVEGIIYHELVK | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity).
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
Sequence Mass (Da)... |
Q6CXY0 | MNNTVLVTCGATVSFPRLVETVLDRSVTEKLKVLGYGRIVIQYGRGFSDTFLQLVEKHLGLFTEKKSCGIKVLDKIENLKVISVDGIEICGFEFSHDIEKLIANNIDLVISHAGTGSILDSLRVGKKLIVVVNDTLMDNHQQLIADKFEQQKLLWSVHANTEELLRALDRSENEELLKIDNTYNKQFEKLLYNVAID | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity).
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
Sequence Mass (Da)... |
O14190 | MNAFVTVGSTQFDDLIRAVLKPEFQHCLVKHGINQLIVQYGKGKQAFGDPKSVAGLTILGFDYAPEIESYIHDASIVISHAGAGSILQTLRSGKRLLVVPNESLMDNHQVELATKLASMNYLVTCSTSNLVEGLEELYPKILTPFPKSDCSTFQKVMQDVAR | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity).
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
Sequence Mass (Da)... |
Q6C3P1 | MHESSALSKLYNWDCSVVFIILNIYTTMLVLVTTGGTVPFEALIELVLSHESITTLSQLGFSKMRVQYGRGNRHIFTKHHKEGVMSITGFEYTDDLAGEMSRAHLVISHAGTGSVLDALRIGKHPVVVVNSKLMDNHQIEIAEELFRKRHLLVSGDTDSVGFIKALKMHREYLFETLPDPEEGILQRIIEETVSFM | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway (By similarity).
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
Sequence Mass (Da)... |
P53178 | MGIIEEKALFVTCGATVPFPKLVSCVLSDEFCQELIQYGFVRLIIQFGRNYSSEFEHLVQERGGQRESQKIPIDQFGCGDTARQYVLMNGKLKVIGFDFSTKMQSIIRDYSDLVISHAGTGSILDSLRLNKPLIVCVNDSLMDNHQQQIADKFVELGYVWSCAPTETGLIAGLRASQTEKLKPFPVSHNPSFERLLVETIYS | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway.
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N,N'-diacetylchitobiosyl diphosphodolichol + UDP
Sequence Mass (Da): 22661
Sequence... |
Q750Y9 | MAWLAIVCLLAATTALCVRMAALAPGVYGPAVCGGRSGGGRGPPRHVMIFLGSGGHTGEMLRLLEVYGAALVAGATVRVGYTDEASAERGRQSAALRAARGVEYVPLLKAREVGAGAGAAVRSTVRAAAQAFSAVRRARRALHTGPHVVVLNGPGTSVVVLFWLRVLDLLSLRRTRVVYVESLARTESLSLSGRLAYPFADEFVVQWPDLAQRYRRARWFGALV | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23809
Sequence Length: 224
Subcellular Location: Endoplasmic ret... |
Q4WNB5 | MFSMLRRMKLDPSTYTYRTYVVSSGDNFSAARAVEFETEWLKQSPKLSFPANGSNSTESYAVVTVPRARRVHQSYLTAPLSTLQCFYACFLVLCGRHPEQKSPLPTTNSPYPDVILTNGPATAVCMVLAAKSLRLFHYLKSLFYIKDHQDRDSSRSSQVKRSEDAPAPVHFQLRTIYVESWARVTTFSLSGKLLLPFADRFLVQWPDLAGKQAWRGMRETEYAGTLVD | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit alg13 to the ER (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 25865
Sequence Length: 228
Subcellular Location: Endoplasmic ret... |
Q5A5N6 | MDIETAACFSIAFIATPILIVLVRLLFILPSLRLPTSVKKKKKLIQECQLSILLGSGGHTGEMMRIISKLDMGKVSRTWIYTSGDNASLAKAQDYERKSGTSSQYIPIPRARTVGQSYISSIPTTIYSFLFSAIAMLKHRPAVILLNGPGTCVPVAYILFLYKLLGLCNTKIIYIESLARVNKLSLSGLLLLPISDRFIVQWESLYQQYSRVEYYGILI | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24460
Sequence Length: 219
Subcellular Location: Endoplasmic ret... |
Q6FV75 | MPFLSTAHLCALLLILGCFYIGRLIKVIPILRFACAGEAEIKPLFIQPKSNDGIHLFVFLGSGGHTGEMLRLLQNHQEVLLNKRNTFYIGYSDDDSKARFLSMVEKYDFKAERIHFYPFAKAREVNAGPIASIVTISKTLLTGFTNVLSIKMNTLGQPHLTLLNGPGTCCIINFWLKLLEWLIYIPYLSNGSNVVYIESLARIESLSLTGKILYLLADVFVVQWEELKVRKAPRSEYYGILV | Function: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27335
Sequence Length: 242
Subcellular Location: Endoplasmic ret... |
Q5PQ59 | MQACHNFPDLDSFLVEKIPLAAYYVPEYISKSEEEYLLRQVYNAPKPKWTQLSGRKLQNWGGLPHSRGMVQEKLPSWLQKYTDQISSLGVFGDHSANHVLVNEYNAGEGIMPHEDGPMYYPTVTTISLGSHTLLDFYVPINKECQETQNQDKVASTEEQRHMLSLLLEPRSLLVVREELYTSYLHGICPRTSDTLSPMVANLGNSTAHAGDTLQRGTRVSLTIRFVPKVLKTSLLLGKGR | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Probable dioxygenase that requires molecular oxygen, alpha-ketoglutarate and iron.
Sequence Mass (Da): 27077
Sequence Length: 240
Subcellular Location: Cytoplasm
EC: 1.14.11.-
|
Q9BT30 | MAGTGLLALRTLPGPSWVRGSGPSVLSRLQDAAVVRPGFLSTAEEETLSRELEPELRRRRYEYDHWDAAIHGFRETEKSRWSEASRAILQRVQAAAFGPGQTLLSSVHVLDLEARGYIKPHVDSIKFCGATIAGLSLLSPSVMRLVHTQEPGEWLELLLEPGSLYILRGSARYDFSHEILRDEESFFGERRIPRGRRISVICRSLPEGMGPGESGQPPPAC | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: May function as protein hydroxylase; can catalyze auto-hydroxylation at Leu-110 (in vitro), but this activity may be due to the absence of the true substrate . Required to induce programmed necrosis in response to DNA damage caused by cytotoxic alkylating agents. Acts... |
Q9D6Z0 | MAGSRRLAMRLLSGCAWVRGSDSAVLGRLRDEAVVHPGFLSQEEEDTLTRELEPQLRRRRYEYDHWDAAIHGFRETEKSCWSDASQVILQRVRAAAFGPDQSLLSPVHVLDLEPRGYIKPHVDSVKFCGSTIAGLSLLSPSVMKLVHTQEPEQWLELLLEPGSLYILRGSARYDFSHEILRDEESFFGEHRVPRGRRISVICRSLPEGMGPGRPEEPPPAC | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: May function as protein hydroxylase; can catalyze auto-hydroxylation at Leu-110 (in vitro), but this activity may be due to the absence of the true substrate. Required to induce programmed necrosis in response to DNA damage caused by cytotoxic alkylating agents. Acts ... |
Q8RWY1 | MVQPRFVRPTQSSPSSISGEPNSSNLYVANCGPAVGLTHNAIAAVFAEFGEVNGVYAADDSGVRVIVSFADPFSAKAALEALSGRPCPDLKGRSLHIRYSVLQLPSETQVNDCVPVSLIDSELNIPGLFLLPDFVTVAEEQQLLAAVDARHWIGLAKRRVQHYGYEFCYGTRNVDTKKRLGELPSFVSPILERIYLFPNFDNGSASLNLDQLTVNEYPSGVGLSPHIDTHSAFEDCIFSLSLAGPCIMEFRRYSVSTWKASTTDAEKSGDSSCIKKALYLPPRSMLLLSGEARYAWNHYIPHHKIDKVKDKVIRRSSRRV... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine.
Sequence Mass ... |
Q96BT7 | MDSNHQSNYKLSKTEKKFLRKQIKAKHTLLRHEGIETVSYATQSLVVANGGLGNGVSRNQLLPVLEKCGLVDALLMPPNKPYSFARYRTTEESKRAYVTLNGKEVVDDLGQKITLYLNFVEKVQWKELRPQALPPGLMVVEEIISSEEEKMLLESVDWTEDTDNQNSQKSLKHRRVKHFGYEFHYENNNVDKDKPLSGGLPDICESFLEKWLRKGYIKHKPDQMTINQYEPGQGIPAHIDTHSAFEDEIVSLSLGSEIVMDFKHPDGIAVPVMLPRRSLLVMTGESRYLWTHGITCRKFDTVQASESLKSGIITSDVGDL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain . Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble positi... |
Q80Y20 | MNINHKGVLKLTKMEKKFLRKQSKARHVLLKHEGIQAVSYPTQSLVIANGGLGNGVSRKQLLLTLEKCGPVEALLMPPNKPYAFVIFQTIEESKKAYFTLNGKEIIDDLGQKIFLYLNFVEKAQWKNMGLEALPPGLLVVEEIISSEEEKKLLESVNWTEDTGNQNFQRSLKHRRVKHFGYEFHYESNTVDKDKPLPGGLPEVCSSILEKLLKEGYIKHKPDQLTINQYEPGHGIPAHIDTHSAFEDEIISLSLGSAIVMDFKHPEGVTVQVMLPRRSLLVMTGESRYLWTHGITPRKFDTVQASEQFKGGIITSDIGDL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain . Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble positi... |
Q07G10 | MGSIDGTRPKLSKDNKKLLKKQAKAKHILLKHEGIETVLHLSQSLVVANGGLGNGVSRQQLLAVLERCGKVETLLMPPNKPYAFVTYSSAEEAIKAYSSLSGQELCGEDAEQPITLYLSFVEKVVVKEVLSPSLPPGLIIVEDFVSPEQERTMLESIDWDSETSSQKSLKHRQVKHYGYEFRYDNNNVDKDKPLPGGLPDFCTEALRKCVQRGLIKHDPDQLTINQYEPGQGIPPHVDTHSAFEDEILSLSLGAEIVMDFKHPNGSVVPVMLPQRSLLIMSGESRYLWTHGITPRKFDVIQVSEGQTVGTISGNSGELTL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain. Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble positio... |
Q9SA98 | MYESANVSDDADRTAFRRAEKKYKLYYEQDSKFSRKKKLPKPIDLSELLDFNLISQNFNNDGVLPDGIRVSKVDSSPVFCIDNRPGFYFIPDALSLKEQCKWIKESLTSFPQPPNRTNHNAIYGPIDDLFDSAKENKVLVQDDLTNNKWKFYEEVDIEKATRSSCKSVSASVLLRKLRWSTLGLQFDWSKRNYDVSLPHNNIPDALCQLAKTHAAIAMPDGEEFRPEGAIVNYFGIGDTLGGHLDDMEADWSKPIVSMSLGCKAIFLLGGKSKDDPPHAMYLRSGDVVLMAGEARECFHGIPRIFTGEENADIGALESEL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Putative dioxygenase that may repair alkylated DNA or RNA by oxidative demethylation. Requires molecular oxygen, alpha-ketoglutarate and iron (By similarity).
Sequence Mass (Da): 39020
Sequence Length: 345
EC: 1.14.11.-
|
O60066 | MLAGNMEQANVFRLEEKRYKCRADTIPDMSEVLDPNDPQSFGFEALVEIKPRVFSFQKAPGLLILKNYVSSELQMQLLKSIMFTQIQDPENKTNLSPFYQLPLGNDSIWRRYYNGDGESIIDGLGETKPLTVDRLVHKKLRWVTLGEQYDWTTKEYPDPSKSPGFPKDLGDFVEKVVKESTDFLHWKAEAAIVNFYSPGDTLSAHIDESEEDLTLPLISLSMGLDCIYLIGTESRSEKPSALRLHSGDVVIMTGTSRKAFHAVPKIIPNSTPNYLLTGNKAWDGWISRKRVNFNVRQVRPSR | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Putative dioxygenase that may repair alkylated DNA or RNA by oxidative demethylation. Requires molecular oxygen, alpha-ketoglutarate and iron (By similarity).
Sequence Mass (Da): 34348
Sequence Length: 302
EC: 1.14.11.-
|
O31250 | MNAPVHVDQNFEEVINAARSMREIDRKRYLWMISPALPVIGIGILAGYQFSPRPIKKIFALGGPIVLHIIIPVIDTIIGKDASNPTSEEIKQLENDPYYARLVKSFIPLQYIANVYACYLVSRKKTSFIDKILLGISMGAINGIAVNTAHELSHKADRLDHILSHLALVPTGYNHFRIEHPYGHHKRAATPEDPASSQMGETFYEFWPRTVFGSLKSAIEIETHRLKRKGKKFWSKDNELLQGWGMSAAFHSSIIAIFGKGTIPYLVTQAFYGISLFEIINYIEHYGLKRQKRADGNYERTMPEHSWNNNNIVTNLFLYQ... | Cofactor: Binds 2 Fe(3+) ions per subunit.
Function: Catalyzes the hydroxylation of n-alkanes in the presence of a NADH-rubredoxin reductase and rubredoxin. It preferably hydroxylases long-chain-length alkanes with at least 12 carbon atoms.
Catalytic Activity: 2 H(+) + O2 + octane + 2 reduced [rubredoxin] = H2O + octan... |
P0CAT7 | MAVVRRAVAARGLQMIAKPLTVVPGFDVWPGLLDISAQRALVEAVLAGAEQAPFSNYRTAYGKPMSVAMTALGSLGWTSDARGYRYVDRHPETGRPWPDMPPALLDLWTVLGDPETPPDSCLVNLYRDGARMGLHQDRDEADPRFPVLSISLGDTAVFRIGGVNRKDPTRSLRLASGDVCRLLGPARLAFHGVDRILPGSSSLVPGGGRINLTLRRARTA | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towar... |
Q54N08 | MYETEEDPTTSNVATTNNEKTASTAATTTEPVKKVTEFMRVQRLFRQVTKSANGKNIPKEKREPIDYSPVLDFHNLENNTEENKKLIIDCTSNVTTHDFEFNRDTEFYLHPREWKVYGLQGYPGFYFIKSPFTASQQKKWIKHALEDYADPPNNNNITLFHGPIKNLWKNGEKELINEELKSQGKHDDDEIEQPTRPLDKNGEPLPTYRQLLDKLAWSTLGYQYQWTPRLYSEEFYEEFPDDLQELVQKIAIATKFDPYVAEAATVNFYSEDSIMGGHLDDAEQEMEKPIISISFGSTAVFLMGAETRDIAPVPLFIRSG... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Putative dioxygenase that may repair alkylated DNA or RNA by oxidative demethylation. Requires molecular oxygen, alpha-ketoglutarate and iron (By similarity).
Sequence Mass (Da): 45446
Sequence Length: 393
EC: 1.14.11.-
|
P05050 | MLDLFADAEPWQEPLAAGAVILRRFAFNAAEQLIRDINDVASQSPFRQMVTPGGYTMSVAMTNCGHLGWTTHRQGYLYSPIDPQTNKPWPAMPQSFHNLCQRAATAAGYPDFQPDACLINRYAPGAKLSLHQDKDEPDLRAPIVSVSLGLPAIFQFGGLKRNDPLKRLLLEHGDVVVWGGESRLFYHGIQPLKAGFHPLTIDCRYNLTFRQAGKKE | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towar... |
P12691 | MLEKHRVLDSAPEYVDKKKYLWILSTLWPATPMIGIWLANETGWGIFYGLVLLVWYGALPLLDAMFGEDFNNPPEEVVPKLEKERYYRVLTYLTVPMHYAALIVSAWWVGTQPMSWLEIGALALSLGIVNGLALNTGHELGHKKETFDRWMAKIVLAVVGYGHFFIEHNKGHHRDVATPMDPATSRMGESIYKFSIREIPGAFIRAWGLEEQRLSRRGQSVWSFDNEILQPMIITVILYAVLLALFGPKMLVFLPIQMAFGWWQLTSANYIEHYGLLRQKMEDGRYEHQKPHHSWNSNHIVSNLVLFHLQRHSDHHAHPT... | Cofactor: Binds 2 Fe(3+) ions per subunit.
Function: Catalyzes the hydroxylation of n-alkanes and fatty acids in the presence of a NADH-rubredoxin reductase and rubredoxin.
Catalytic Activity: 2 H(+) + O2 + octane + 2 reduced [rubredoxin] = H2O + octan-1-ol + 2 oxidized [rubredoxin]
Location Topology: Multi-pass membra... |
P37462 | MLDLFADEAPWQEPLAPGAVVLRRFAFRAAQSLLDDIGFVASQSPFRQMVTPGGYTMSVAMTNCGALGWTTDRHGYCYAVRDPLTDKPWPALPLSFASVCRQAAIAAGYASFQPDACLINRYAPGAKLSLHQDKDEPDLRAPIVSVSLGVPAVFQFGGLRRSDPIQRILLEHGDIVVWGGESRLFYHGIQPLKAGFHPMTGEFRYNLTFRQAAEKE | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towar... |
O32149 | MEKQKLSVKNSITDYIEWLAQYGASADGGVTRLLYTKEWMDAQLAVKTEMSSFGLETRFDDVGNVFGRLSGTQSPDEVIVTGSHIDTVINGGKYDGAYGVLAAMLALKQLKETYGAPKKTLEAVSLCEEEGSRFPMTYWGSGNMTGVFSEQDAKEPRDESGVSLQTAMHESGFGKGVFQSAYRTDISAFVELHIEQGKTLEMSGRDLGIVTSIAGQRRYLVTLEGECNHAGTTSMKWRKDPLAASSRIIHELLLRSDELPDELRLTCGKITAEPNVANVIPGRVQFSIDIRHQHQHVLEQFHQDMVALINGICLQKGIRA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in the anaerobic nitrogen utilization via the assimilation of allantoin . Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolas... |
P82678 | MASTSHNPFYAAMQPQAQHWGATSPTSTGAGYDRPSAGYPAYTGYAAAGTSHPAPSSSSPSTALALYNPSSLYGLYYNEAVHGPFATGLQSNPFTPGLAPLSTVSRPSYATEDPLRQRYPATSANPHDPLNWITEDLFAIRMERAAISQQRTPLRSASVAAR | Function: Catalyzes the degradation of allantoate to (-)-ureidoglycolate and (+)-ureidoglycolate to glyoxylate.
Catalytic Activity: allantoate + H2O = (S)-ureidoglycolate + urea
Sequence Mass (Da): 17207
Sequence Length: 162
Pathway: Nitrogen metabolism; (S)-allantoin degradation; (S)-ureidoglycolate from allantoate (a... |
Q6DGA6 | MAKRQVQKETRSQPHFLQFNNLACETAGGKVIFATDEWFAPARNLLKRDPPEFIASAFTEFGKWMDGWETRRKRIPGHDWCIVQLGVPGIIHGFDVDTSFFTGNYAPFASIQATCLDQMPSIALEGDRTGMAASPSQFEAVAQLNSDSWKEVVPVTKLKAGYSDTCHNYLSVSYPHRVTHIRFNIYPDGGIARLKVYGIGKKDWSSVFGQDLVDLVALVNGGVCVGFSDAHYGHPRNMIGLGMAENMGDGWETARRLDRPRVLKEDENGILQVPGSEWAIFRLGHPGIISKIELDTNHFKGNFPDSCRIEACSLTEDEEN... | Function: Utilization of purines as secondary nitrogen sources, when primary sources are limiting.
Catalytic Activity: allantoate + H2O = (S)-ureidoglycolate + urea
Sequence Mass (Da): 44144
Sequence Length: 395
Pathway: Nitrogen metabolism; (S)-allantoin degradation; (S)-ureidoglycolate from allantoate (aminidohydrola... |
Q54VL5 | MVYANNNIDPNAPCYVSECAELLSDKVGGVVLGCTDQWFAECVNLIKHSAPVWDAEKYVDTGKWMDGWETKRHNPDHDWCIIKLGIPGVIYGFEIDTAYFTGNYPPHASIEALCDDSDPNFNTLKESNNWEVILNKSDLGSSCKKYFECKVEKRFTHIKFRIYPDGGVARLRAYGRVVKDWTLVIPGELVDLAAIENGGLVTQVSDHFYGNKNNIIMPGRSVNMGDGWETKRRRGPGNDWLTVKLAKEGIVKRIEVDTNWFKGNFPTSCSIDAIHSSSAPDETHLQDYEWTNILPNSPLCGHRRHFFQNELVNNDKPFTH... | Function: Utilization of purines as secondary nitrogen sources, when primary sources are limiting.
Catalytic Activity: allantoate + H2O = (S)-ureidoglycolate + urea
Sequence Mass (Da): 41778
Sequence Length: 369
Pathway: Nitrogen metabolism; (S)-allantoin degradation; (S)-ureidoglycolate from allantoate (aminidohydrola... |
P77425 | MITHFRQAIEETLPWLSSFGADPAGGMTRLLYSPEWLETQQQFKKRMAASGLETRFDEVGNLYGRLNGTEYPQEVVLSGSHIDTVVNGGNLDGQFGALAAWLAIDWLKTQYGAPLRTVEVVAMAEEEGSRFPYVFWGSKNIFGLANPDDVRNICDAKGNSFVDAMKACGFTLPNAPLTPRQDIKAFVELHIEQGCVLESNGQSIGVVNAIVGQRRYTVTLNGESNHAGTTPMGYRRDTVYAFSRICHQSVEKAKRMGDPLVLTFGKVEPRPNTVNVVPGKTTFTIDCRHTDAAVLRDFTQQLENDMRAICDEMDIGIDID... | Cofactor: Binds 2 Zn(2+) ions per subunit . Also able to bind Mn(2+) .
Function: Involved in the anaerobic nitrogen utilization via the assimilation of allantoin . Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S... |
P18407 | MTDIDYKLEAVPATRIAADDIDKTFRSSTIDLISGALGGKVLGFSDEWFAEAANLLTPTAPIRQPGKMVYTGAWYDGWETRRHNPAEFDWVVIRLGVASGTVEGVEIDTAFFNGNHAPAISVEGCFSQNDDEVLSWKGERGGWETILGVQECGPSQRFGWKLENPTKKQYTHVRLNMYPDGGIARFRLFGHAVPVFPDNTDAIFDLAAAQNGGVAISCSDQHFGTKDNLILPGRGKDMGDGWETARSRTKGHVDWTIIRLGAPGYIQNFMVDTAHFRGNYPQQVKLQAIEWKSEGEPGADSEGWTEVVEPIKCGPDQEHP... | Function: Utilization of purines as secondary nitrogen sources, when primary sources are limiting.
Catalytic Activity: allantoate + H2O = (S)-ureidoglycolate + urea
Sequence Mass (Da): 39073
Sequence Length: 354
Pathway: Nitrogen metabolism; (S)-allantoin degradation; (S)-ureidoglycolate from allantoate (aminidohydrola... |
Q5YP02 | MNETAADRVAPRGFTELPDLAVRSLGGAVIWADDEFFAEKENLIVPEAPEFRPATYGHRGQVYDGWETRRHRGLPGDDAAVVRLGVPGVIHGVVVDTSWFTGNYPPAISLSALAIDGYPPAADIAARTDWVPLLDRVPVRGDARNPFPIPSRDRWTHVRLTMHPDGGIARLRVHGEGRPDPALLGLGPVDLAALENGALVLDCSDRFYGSPHQLLHPGNARRMGDGWETARRRDDGNDWVRIRLAGPGLIRLAELDTSYFLGNSPAAARLTGRTTDGTEVELLPRTPLQPDTRHRFPTAAVAASVEEVRLDIYPDGGLAR... | Catalytic Activity: allantoate + H2O = (S)-ureidoglycolate + urea
Sequence Mass (Da): 35822
Sequence Length: 329
Pathway: Nitrogen metabolism; (S)-allantoin degradation; (S)-ureidoglycolate from allantoate (aminidohydrolase route): step 1/1.
EC: 3.5.3.4
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Q55320 | MKIKLLCISLAVLFCSSANAQKKQAKVQPSVFPQTVARPKLVVGMVIDQMRWDYLYRFYARYGNGGFKRLINEGFSAENTLIPYTPTLTACGHSSIYTGSVPAINGIIGNNWFDPQLGRDVYCVEDKSVKTVGSSSNEGLMSPKNLLVTTVTDELRMATNFRSKVISVSIKDRGAILPGGHTANGAYWYDDMTGSFISSTHYMQQLPTWVNDFNAQRLPNKYFEQDWNTLYPIETYTESTADAKPYERTFKGAKTSSFPHLFKQYANKNYSMMASMPQGNSFTLEFAKAAIPAEKLGQTGNTDFLAVSLSSTDYVGHQFG... | Cofactor: Binds 2 Zn(2+) ions.
Function: Alkaline phosphatase with broad substrate specificity.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 61325
Sequence Length: 550
Subcellular Location: Cell inner membrane
EC: 3.1.3.1
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Q5NNZ8 | MNSLLHHSFLKTVFSSLAIAIVTSSLSSVTIAATHPLDNHPKGEIAASSETAHNPWSGTRLIVAISVDQFSSDLFSEYRGRFRSGMKQLQNGVVYPMAYHSHAATETCPGHSVLLTGDHPARTGIIANNWYDFSVKRADKKVYCSEDPSLSADPQNYQPSVHYLKVPTLGDRMKKANPHSRVISVAGKDRAAIMMGGHMTDQIWFWSDNAYKTLADHKGEMPVTVKTVNEQVTRFMQQDEAPVMPSVCADHASALKIGNNRIIGLAPASRKAGDFKTFRVTPDYDRTTTDIAIGLIDELKLGHGNAPDLLTVSLSATDAV... | Cofactor: Binds 2 Zn(2+) ions.
Function: Alkaline phosphatase with broad substrate specificity. Has phosphatase activity towards nucleotide and sugar phosphates with a preference to nucleotide phosphates. Has no phosphodiesterase activity.
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequenc... |
Q9M2U3 | MGPIKTIKKKKRAEKKVDRNVLLAATAAATSASAAAALNNNDDDDDSSSQSLDWWDGFSRRIYGGSTDPKTFESVFKISRKTFDYICSLVKADFTAKPANFSDSNGNPLSLNDRVAVALRRLGSGESLSVIGETFGMNQSTVSQITWRFVESMEERAIHHLSWPSKLDEIKSKFEKISGLPNCCGAIDITHIVMNLPAVEPSNKVWLDGEKNFSMTLQAVVDPDMRFLDVIAGWPGSLNDDVVLKNSGFYKLVEKGKRLNGEKLPLSERTELREYIVGDSGFPLLPWLLTPYQGKPTSLPQTEFNKRHSEATKAAQMALS... | Function: Transposase-derived protein that may have nuclease activity.
Sequence Mass (Da): 45467
Sequence Length: 406
Subcellular Location: Nucleus
EC: 3.1.-.-
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P83610 | GSTSYIYDTSAGSGTYAYIVDTGIITSHNGFNWAANDIISKSYSNYGTVLDIFAPGTSVLSS | Function: Serine protease. May be involved in the invasion of grains and hydrolyzation of grain proteins.
Sequence Mass (Da): 6493
Sequence Length: 62
Subcellular Location: Secreted
EC: 3.4.21.-
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P58736 | MTDDFEDSFPDNETDAFEQAPLRLTVDLGALADNWRDMKKRSGRARTAAVVKADAYGLGIEDCGATLYHAGARDFFVATVAEGATLRSYAPEARIFVLSGIWQGQERQVFDNDLVPVLASEEQLSFWMATVAERGDHPCALHVDTGFNRLGLPLDDALFLADDVTRPASFDPVLVLSHLACADTPSSPMNRAQLESFRRVSAAFEGIESSLSASAGIFLGPDYHFDLTRPGIALYGGEAVNDVANPMRPVAKAEARIIQIREAGEGQTVSYGSSFLLKRASRLAIASVGYADGYQRSLSGSGIPLREMGHGGAYGVVNGH... | Function: Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis (By similarity).
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 42091
Sequence Length: 391
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: ste... |
P10725 | MSTKPFYRDTWAEIDLSAIKENVSNMKKHIGEHVHLMAVVKANAYGHGDAETAKAALDAGASCLAVAILDEAISLRKKGLKAPILVLGAVPPEYVAIAAEYDVTLTGYSVEWLQEAARHTKKGSLHFHLKVDTGMNRLGVKTEEEVQNVMAILDRNPRLKCKGVFTHFATADEKERGYFLMQFERFKELIAPLPLKNLMVHCANSAAGLRLKKGFFNAVRFGIGMYGLRPSADMSDEIPFQLRPAFTLHSTLSHVKLIRKGESVSYGAEYTAEKDTWIGTVPVGYADGWLRKLKGTDILVKGKRLKIAGRICMDQFMVEL... | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 43265
Sequence Length: 389
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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Q8EAI6 | MKPFPRAEISSSALQNNLAVLRQQASSSQVMAVVKANGYGHGLLNVAKCLNNADGFGLARLEEALELRAGSVKARLLLLEGFFRSTDLPLLVEHDIDTVVHHESQIEMLEQATLSKPVTVWLKVDSGMHRLGVTPEQFSAVYARLTACKNVAKPIHLMTHFACADEPDNHYTQVQMQTFNQLTADLPGFRTLANSAGALYWPKSQGDWIRPGIAMYGVSPVTGDCGANHGLIPAMNLVSRLIAVREHKANQPVGYGCYWTAKQDTRLGVVAIGYGDGYPRNAPEGTPVWINGRRVPIVGRVSMDMLTVDLGHDATDQVGD... | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 38942
Sequence Length: 358
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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Q2NTA8 | MPRPIVAKVDSAVLASNLSIVRRHAPQAQVWSVVKANGYGHGLNTVWQGLQQTDGFALLDLHEAVVLREKGWRGPILLLEGFFQPADLAVIDRYRLTTVVHSDWQIEALRRMTPRAPLDIYLKLNSGMNRLGFSERALPGAWQSLNALKHVATLTLMSHFAYADMPEGVEGQMAVVARAGEGLTGPRCLANSAATLWHPATHGQWVRPGIILYGASPSGNWQDIAASGLRPVMTLQSELIAVQSVPAGGRIGYGGRHRVSETHRVGVVACGYADGYPRHAPTGTPILVDGVRTSTLGAVSMDMLMVDLQLCPKARIGSAV... | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 38378
Sequence Length: 356
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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A9ESU7 | MRPTRAEVNLAHLRHNLRVLERGLTGATKPQIWGVLKADAYGHGAPAVARTLERAGIPGLCVALLEEAIELRDAGIRLPILVMGGYYGPRRDGFEEIIARDLVPVVYDAGQIERLASVVRLEQRGRVGVHLKVDTGMGRLGAASSEIEAVLATLAKHPEVKLDGLMTHLACADADDLGVTIEQMRLFGEIEQRAKSFGLTPRVRHASNSAAMLRLPAALLDIVRPGVALFGISPCAGLAPDLKPVIRVRSEIVALRTIAKGDRIGYGHTWQASRESVVATVPMGYADGLSRQLSNRGAALVRGQRAPIAGAVSMDLTMLD... | Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Catalytic Activity: L-alanine = D-alanine
Sequence Mass (Da): 40620
Sequence Length: 379
Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
EC: 5.1.1.1
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P00688 | MKFVLLLSLIGFCWAQYDPHTSDGRTAIVHLFEWRWVDIAKECERYLAPKGFGGVQVSPPNENVVVHNPSRPWWERYQPISYKICTRSGNEDEFRDMVTRCNNVGVRIYVDAVINHMCGAGNPAGTSSTCGSYLNPNNREFPAVPYSAWDFNDNKCNGEIDNYNDAYQVRNCRLTGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDAAKHMWPGDIKAVLDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAIKGSEYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGLVPSDRALVFVDNHDNQRGHGAG... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
Sequence Mass (Da): 57318
Sequence Length: 508
Subcellular Location: Secreted
EC: 3.2.1.1
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B6K9M7 | MPTESRSILARAEETRCRHLSRLLRAGLVFLLCDVLTSCLATPELQNTVIRSSKAHHLQLLFSSRSTPAVKFPLDATLSAPNSFGEQEARSVEAVKQNPWATTTAFADFMKRFNIPQVHGSGIFVDLGRDTEGYREVGGKCPVFGKAIQMHQPAEYSNNFLDDAPTSNDASKKPLPGGFNNPQVYTSGQKFSPIDDSLLQERLGTAGPKTAIGRCALYAYSTIAVNPSTNYTSTYKYPFVYDAVSRKCYVLSVSAQLLKGEKYCSVNGTPSGLTWACFEPVKEKSSARALVYGSAFVAEGNPDAWQSACPNDAVKDALFG... | Function: May play a role in host cell invasion.
PTM: Proteolytically cleaved within its transmembrane domain, releasing a soluble form from the cell surface.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 69944
Sequence Length: 651
Subcellular Location: Cell membrane
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P16445 | MKEIYYIVILCSLYLINLGNCSEGTDKIISENGDVKFDLIPKENTERSHKLINPWEKFMEKYDIEKVHGSGIRVDLGEDARVENQDYRIPSGKCPVMGKGITIQNSKVSFLTRVATGNQKVREGGLAFPQTDVNISPITIDNLKLMYKDHKEILALNDMSLCAKHASFYVPGTNVNTAYRHPAVYDKSNKTCYILYVAAQENMGPRYCSNEEDNENQPFCFTPEKKDEYKNLSYLTKNLREDWETSCPNKSIQNAKFGVWVDGYCSEYQKKEVHDNKTLLECNQIVFNESASDQPKQYEKHLEDTAKIRRGIVDRNGKLI... | Function: Involved in parasite invasion of erythrocytes.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63974
Sequence Length: 558
Subcellular Location: Membrane
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P22621 | MRKLYCVLLLSAFEFTYMINFGRGQNYWEHPYQKSDVYHPINEHREHPKEYQYPLHQEHTYQQEDSGEDENTLQHAYPIDHEGAEPAPQEQNLFSSIEIVERSNYMGNPWTEYMAKYDIEEVHGSGIRVDLGEDAEVAGTQYRLPSGKCPVFGKGIIIENSNTTFLTPVATGNQYLKDGGFAFPPTEPLMSPMTLDEMRHFYKDNKYVKNLDELTLCSRHAGNMIPDNDKNSNYKYPAVYDDKDKKCHILYIAAQENNGPRYCNKDESKRNSMFCFRPAKDISFQNYTYLSKNVVDNWEKVCPRKNLQNAKFGLWVDGNC... | Function: Involved in parasite invasion of erythrocytes.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 72010
Sequence Length: 622
Subcellular Location: Membrane
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B6KAM0 | MICSIMGGLRSLRAARPYSHQSNTETKHMGLVGVASLLVLVADCTIFASGLSSSTRSRESQTLSASTSGNPFQANVEMKTFMERFNLTHHHQSGIYVDLGQDKEVDGTLYREPAGLCPIWGKHIELQQPDRPPYRNNFLEDVPTEKEYKQSGNPLPGGFNLNFVTPSGQRISPFPMELLEKNSNIKASTDLGRCAEFAFKTVAMDKNNKATKYRYPFVYDSKKRLCHILYVSMQLMEGKKYCSVKGEPPDLTWYCFKPRKSVTENHHLIYGSAYVGENPDAFISKCPNQALRGYRFGVWKKGRCLDYTELTDTVIERVES... | Function: Essential microneme protein that plays an important role in host cell invasion. Part of the moving junction (MJ) complex, a ringlike structure formed between the plasma membranes of the apical tip of the parasite and the target host cell. During invasion, the MJ migrates from the anterior to the posterior of ... |
P37112 | MTKEEIKRLVDEVKTDVIAWRRHLHAHPELSFQEEKTAQFVYETLQSFGHLELSRPTKTSVMARLIGQQPGRVVAIRADMDALPIQEENTFEFASKNPGVMHACGHDGHTAMLLGTAKIFSQLRDDIRGEIRFLFQHAEELFPGGAEEMVQAGVMDGVDVVIGTHLWSPLERGKIGIVYGPMMAAPDRFFIRIIGKGGHGAMPHQTIDAIAIGAQVVTNLQHIVSRYVDPLEPLVLSVTQFVAGTAHNVLPGEVEIQGTVRTFDETLRRTVPQWMERIVKGITEAHGASYEFRFDYGYRPVINYDEGDPRHGGNGVRAVR... | Function: Hydrolyzes most efficiently N-acetyl derivatives of aromatic amino acids but is also active on other amino acids. L-stereospecific.
Catalytic Activity: an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid
Sequence Mass (Da): 41676
Sequence Length: 370
EC: 3.5.1.14
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Q80ZD5 | MAWLVLLGLLLCMLGAGSGTSDLEGVLPPDPHNCPNKCVCAADVLSCAGRGLQDLPAALPATAAELDLSHNALKRLHPGWLAPLSRLRALYLGYNKLDVLGRGVFTNASGLRILDLSSNLLRRLRTYDLDGLEELEKLLLFNNRLMHLDLDAFQGLSMLSHLYLSCNELSSFSFNHLHGLGLTRLRTLDLSSNWLGHVSVPELAALPTFLKNRLYLHNNPLPCDCSLYHLLRRWHQRGLSALHDFEREYTCLAFKVAESRVRFFEHSRVFKNCSVAAAPGLELPEEELHTHVGQSLRLFCNTTVPAARVAWVSPKNELLV... | Function: May mediate heterophilic cell-cell interaction. May contribute to signal transduction through its intracellular domain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 55565
Sequence Length: 508
Subcellular Location: Membrane
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D3FSJ2 | MKITSGDLPGVGKKISFITSEGSMVVLVIHHTGKREMYFFDDADDDEVSFSLTLSAEETKQMGAQLLGAILNPADTDKIDRIKLIRKQVVVEWIDITKHSPIISKSIAQIEKMKPKGISIVGVFKNDEMMVDPEPTLVLEKGDTLMAVGKRDAIQKFEELCACKENN | Function: Modulates the activity of the ammonium/proton antiporter AmhT.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18525
Sequence Length: 167
Subcellular Location: Cell membrane
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Q16671 | MLGSLGLWALLPTAVEAPPNRRTCVFFEAPGVRGSTKTLGELLDTGTELPRAIRCLYSRCCFGIWNLTQDRAQVEMQGCRDSDEPGCESLHCDPSPRAHPSPGSTLFTCSCGTDFCNANYSHLPPPGSPGTPGSQGPQAAPGESIWMALVLLGLFLLLLLLLGSIILALLQRKNYRVRGEPVPEPRPDSGRDWSVELQELPELCFSQVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLLSGPLLVLELHPKGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERW... | Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for anti-Muellerian hormone.
Cata... |
Q62893 | MLGTLGLWTLLPAAAQVSPNRRTCVFFEAPGVRGSTKTLGEVVDAGPGPPKGIRCLYSHCCFGIWNLTHGRAQVEMQGCLDSDEPGCESLHCDPVPRAHPSPSSTLFTCSCGTDFCNANYSHLPPSGNRGAPGPQEPQATPGGPIWMAQLLLGVFLVLLLSIIILALLQRKACRVQGGSDPEPEPGSGGDCSEELPELAELRFSQVIQEGGHAVVWAGRLQGEMVAIKAFPPRAVAQFRAERAVYQLLGLQHNHIVRFITAGQGGPGPLPSGPLLVLELYPKGSLCHYLTQYTSDWGSSLRMALSLAEGLAFLHGERWQD... | Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for anti-Muellerian hormone.
Cata... |
D3FSJ3 | MVIPELFSAGLILLLLFITGFVGMKMKIPDVVIFILLGIAVGGLLSGSHLLHFAGEVGIVLLFFMLGMEFPLKQLMSIAKKVLRAGILDVALSFGVTMAICMMMGLDVITSLIIGGVAYATSSSITAKMLESSKRMANPESEFMLGLLIFEDLVAPILVAVLVGLTAGMALTAGSMSLLVVKVVALVAGAVILGVFLFRKLGSFFDRHMKHDLFILFVIGLALMYGGLALYLDLSEVLGAFLAGIMLAEVKRTHELELMVVRFRDLLLPLFFLYFGTTISFSEGIPMIPLLILVLVWSVIAKVIVGVLGGRWYGLTKKVS... | Function: Ammonium/proton antiporter that mediates the efflux of ammonium ions. Can also transport potassium or rubidium, but not sodium or lithium.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41791
Sequence Length: 390
Subcellular Location: Cell membrane
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Q9FR37 | MATNNDFGAFIEKVTISPTSTSSSPPSLQGLTFAIKDIFDVEGRVTGFGNPDWLRTHSAATSTAPVVSSLLEAGATALGITIMDEMAYSINGENAHYGTPRNPIAFDRVPGGSSSGSAVAVAARLVDFSIGTDTGGSVRVPASYCGIFGFRPSHGAVSTVGLTPMAQSFDTVGWFARDTATLKRVGCVLLQQHHLNPIEPSQLIIADDCFKLCSVPHDLLVQPLVGSVEKSFGGNTVVKKVNLGEYIGQNVPSLKHFMTSDDVTTQQEFCIPSLMALSSSMRLLQRHEFKINHGAWISSVKPEFGPGISERIEEAIRTSD... | Function: Amidase involved in auxin biosynthesis. Converts indole-3-acetamide to indole-3-acetate . Converts phenyl-2-acetamide (PAM) to phenyl-2-acetate. Substrate preference is PAM > IAM . Can also use L-asparagine and 1-naphtalene-acetamide as substrates, but not indole-3-acetonitrile or indole-3-acetyl-L-aspartic a... |
Q7XTK3 | MAMAGGGRGDYGAFMERFVLPPPPSQQLPLHGLTFAIKDIFDIAGRVTGFGNPDWARTHAPAAATSPVVLAALAAGATSLGTTIMDEMAYSINGENTHYGTPTNPCAPGRVPGGSSSGSAVAVAANLVDFSLGTDTGGSVRVPAAYCGIFGLRPSHGLVSAENVIPMAQMFDTVGWFSRDLSTLSRVTKVLLPLPDDIVKQPTQVTIPMDCFQILGSLDDRTYQIINASVAKRFDSQILDNRNLGDFISDNVPSIGKFITDFSESELPSVPALSVISHVMRGLQRSQFKANHAEWVNTVKPNLGPGLRERILEAIASGDN... | Function: Amidase involved in auxin biosynthesis (Probable). Converts indole-3-acetamide (IAM) to indole-3-acetate, and phenyl-2-acetamide (PAM) to phenyl-2-acetate. Substrate preference is PAM > IAM .
Catalytic Activity: a monocarboxylic acid amide + H2O = a monocarboxylate + NH4(+)
Sequence Mass (Da): 46180
Sequence ... |
Q1PS23 | MKSILKAMALSLTTSIALATILLFVYKFATRSKSTKKSLPEPWRLPIIGHMHHLIGTTPHRGVRDLARKYGSLMHLQLGEVPTIVVSSPKWAKEILTTYDISFANRPETLTGEIVLYHNTDVVLAPYGEYWRQLRKICTLELLSVKKVKSFQSLREEECWNLVQEIKASGSGRPVNLSENVFKLIATILSRAAFGKGIKDQKELTEIVKEILRQTGGFDVADIFPSKKFLHHLSGKRARLTSLRKKIDNLIDNLVAEHTVNTSSKTNETLLDVLLRLKDSAEFPLTSDNIKAIILDMFGAGTDTSSSTIEWAISELIKCP... | Function: Involved in the biosynthesis of the antimalarial endoperoxide artemisinin . Catalyzes three consecutive oxidations of amorpha-4,11-diene to produce artemisinic acid, with artemisinic alcohol and artemisinic aldehyde as intermediates products, but is unable to oxidize germacrene A . No activity with limonene, ... |
P46883 | MGSPSLYSARKTTLALAVALSFAWQAPVFAHGGEAHMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPLALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEIKQAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVIMLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEFAAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGNYWAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTA... | Cofactor: Binds 1 copper ion per subunit. Can also use zinc ion as cofactor (By similarity).
Function: The enzyme prefers aromatic over aliphatic amines.
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + ... |
Q43077 | MASTTTMRLALFSVLTLLSFHAVVSVTPLHVQHPLDPLTKEEFLAVQTIVQNKYPISNNRLAFHYIGLDDPEKDHVLRYETHPTLVSIPRKIFVVAIINSQTHEILINLRIRSIVSDNIHNGYGFPILSVDEQSLAIKLPLKYPPFIDSVKKRGLNLSEIVCSSFTMGWFGEEKNVRTVRLDCFMKESTVNIYVRPITGITIVADLDLMKIVEYHDRDIEAVPTAENTEYQVSKQSPPFGPKQHSLTSHQPQGPGFQINGHSVSWANWKFHIGFDVRAGIVISLASIYDLEKHKSRRVLYKGYISELFVPYQDPTEEFYF... | Cofactor: Binds 1 copper ion per subunit.
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+)
Sequence Mass (Da): 76358
Sequence Length: 674
EC: 1.4.3.21
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P12807 | MERLRQIASQATAASAAPARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSKHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPYGSPEFPHQRKHALDI... | Cofactor: Binds 1 copper ion per subunit. Can also use zinc ion as cofactor .
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+)
Sequence Mass (Da): 77534
Sequence Length: 692
Subcellular Loc... |
H2A0M3 | MSLPKTANGMDKLKLCYLLLFYLGSSSLTEVSGAQTCEIDSVLCTSDLSEPDDPPIFHDLTTKEIKSVQTYLYHQRDLRLLRPGLAKINTSFIQGMELYLPNKKDVIHYLQSKVPTPKPPRAAVVTIFRGDCDPAVVEEYIVFPLPWPTQHRLHRKVPYYLRPFNDVEFATISDFLTKQVDGVLRQFLEESFGGRLINCGNRCLNFQFASPVGPSVSNEPGARKSWYWLHQLVEYSALHPVDFAVLMKIVGCVYTIEKVYFNNMYFNSLQEVALHYRNPSFPRLRIPYPVDSKQLFSKMERRGILFPEKPVSPPRQVEPE... | Cofactor: Binds 1 copper ion per subunit.
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Sequence Mass (Da): 89950
Sequence Length: 781
Subcellular Location: Secreted
EC: 1.4.3.-
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