ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6DER6 | MAGGKAGKDTGKAKATSITRSSRAGLQFPVGRIHRLLKNRTTSHGRVGGTAAVYTAAILEYLTAEVLELAGNASKDLKVKRISPRHLQLAIRGDEELDALIKATIAGGGVIPHIHKSLIGKKGQQKTV | Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication... |
Q75CC6 | MSGKVHGGKGKSGAKDGGPLGSQSHSARAGLQFPVGRIKRYLKKNAAGKTRVGSKAAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDDELDSLIRATIASGGVLPHINKALLLKVEKKTHK | Function: Variant histone H2A which can replace H2A in some nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal ... |
Q4WE68 | MPGGKGKSVGGKAGAKDAAGKTQKSHSAKAGLQFPCGRVKRFLKNNTQNKMRVGAKAAVYVTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDEELDTLIRATIAFGGVLPRINRALLLKVEQKKKNKSDA | Function: Variant histone H2A which can replace H2A in some nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal ... |
Q5ZMD6 | MAGGKAGKDSGKTKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV | Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication... |
P04913 | MSAAEKKPASKAPAGKAPRDTMKSADKKRGKNRKETYSSYIYKVLKQVHPDTGISNQAMRILNSFVNDIFERIATEASKLAAYNKKSTISSREIQTAVRLILPGELAKHAVTEGTKSVTKYSSSAQ | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P08993 | MAPKKAPAAAAEKKVKKAPTTEKKNKKKRSETFAIYIFKVLKQVHPDVGISKKAMNIMNSFINDSFERIALESSKLVRFNKRRTLSSREVQTAVKLLLPGELARHAISEGTKAVTKFSSSTN | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P35068 | MPPKVSGKAAKKAGKAQKNITKGDKKKNRKRKESYAIYIYKVLKQVHPDTGISSKAMSIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P02293 | MSAKAEKKPASKAPAEKKPAAKKTSTSTDGKKRSKARKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
A0A097I2B5 | MATQKETTRKRDKSVNFRLGLRNMLAQIHPDISVQTEALSELSNIAVFLGKKISHGAVTLLPEGTKTIKSSAVLLAAGDLYGKDLGRHAVGEMTKAVTRYGSAKESKEGSRSSKAKLQISVARSERLLREHGGCSRVSEGAAVALAAAIEYFMGEVLELAGNAARDSKKVRISVKHITLAIQNDAALFAVVGKGVFSGAGVSLISVPIPRKKARKTTEKEASSPKKKAAPKKKKAASKQKKSLSDKELAKLTKKELAKYEKEQGMSPGY | Function: Histone-like protein that is recruited to viral factories during viral replication and participates in viral DNA packaging and virion production probably by forming unstable nucleosome-like particles . May compact the viral DNA .
Sequence Mass (Da): 28829
Sequence Length: 269
Domain: The N-terminus is similar... |
Q6DN03 | MPEPAKFAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKRVHPDTGIWCKAMGIMNSFLNDIFERIAGEASRLAHYNKRSTITSRRSRRPCACCCPASWPSTPCPRAPRRSPSTPAPSESLPGPGARSLPPSLPPRVAGCFVSKGSFQGHLTTSVKESFLCCQSQLMFLASRLVNFRRAHNTKHR | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q5QNW6 | MPDPAKSAPAPKKGSKKAVTKVQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q9SGE3 | MAPRKPKVVSVTKKKKVVEETIKVTVTEEGDPCVITETANDQETQDLTFSIPVGENVTTVEIPVEVPDERSLPVGENVTTVKIPVDDRDESSPQPPETPVEVRDEPSPQPPETPASKSEGTLKKTDKVEKKQENKKKKKKKKRDDLAGDEYRRYVYKVMKQVHPDLGITSKAMTVVNMFMGDMFERIAQEAARLSDYTKRRTLSSREIEAAVRLVLPGELSRHAVAEGSKAVSNFVGYDSRKR | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q27894 | MAPPKPSAKGAKKAAKTVTKPKDGKKRRHARKESYSVYIYRVLKQVHPDTGVSSKAMSIMNSFVNDVFERIAAEASRLAHYNKRSTISSREIQTAVRLILPGELAKHAVSEGTKAVTKYTSSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q8SQP3 | MSRTKQTASKALGGKAPRKGISAKSIPSSGCSPAMPKRTRFKAGALALKEIRKYQKSTDLLIRKRPFQRMVRDLCKGREGVRFQASAIVAFQEAVENFLTSLMEDAYRCVLHAKRVTLMPKDICLVYKIKYANILYAALD | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P0DPK2 | MARTKQTARKATAWQAPRKPLATKAAGKRAPPTGGIKKPHRYKPGTLALREIRKYQKSTQLLLRKLPFQRLVREIAQAISPDLRFQSAAIGALQEASEAYLVQLFEDTNLCAIHARRVTIMPRDMQLARRLRREGP | Function: Primate-specific variant histone H3, which constitutes a core component of nucleosomes . Histone H3.Y-containing nucleosomes accumulate around transcription start sites and have flexible DNA ends, suggesting that they form relaxed chromatin that allows transcription factor access . Histone H1 binds less effic... |
Q757N1 | MARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRFQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQESVEAYLVSLFEDTNLAAIHAKRVTIQKKDIKLARRLRGERS | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q41811 | MSGRGKGGKGLGKGARKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVRKIFLENVIRDAVTYTEHARRKTVTAMDVVYALKRQGRTLYGFGG | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P70081 | MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQERTLYGFGG | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
A0A097I2D0 | MSKAGKKVKAQQHGHLADHVSVGETQIPKASTQHLLRKAGSLSAAGDTEVPIRGFVHMKLHKLVQKSLLAMQLAKRKTIMKSDVKKAAELMHLPVFAIPTKDSGAKGSVFLSCRQKGAGSAGTGSETNSQEVRSQMKSTCLIIPKERFRTMAKEISKKEGHDVHIAEAALDMLQVIVESCTVRLLEKALVITYSGKRTRVTSKDIETAFMLEHGPL | Function: Histone-like protein that is recruited to viral factories during viral replication and participates in viral DNA packaging and virion production probably by forming unstable nucleosome-like particles . May compact the viral DNA .
Sequence Mass (Da): 23520
Sequence Length: 216
Domain: The N-terminus is similar... |
P62793 | MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKIFLENVIRDSVTYTEHAKRKTVTALDVVYALKRSGRTLYGFGA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P59259 | MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKIFLENVIRDAVTYTEHARRKTVTAMDVVYALKRQGRTLYGFGG | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q7LKT3 | MTGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISAMIYEETRGVLKTFLEGVIRDAVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P0DPR0 | MSQTNANDLRNNEVFFISPSNNTNKVLDKISQSEVKLWNKLSGANQKWRLIYDTNKQAYKIKVMDNTSLILTWNAPLSSVSVKTDTNGDNQYWYLLQNYISRNVIIRNYMNPNLVLQYNIDDTLMVSTQTSSSNQFFKFSNCIYEALNNRNCKLQTQLNSDRFLSKNLNSQIIVLWQWFDSSRQKWIIEYNETKSAYTLKCQENNRYLTWIQNSNNYVETYQSTDSLIQYWNINYLDNDASKYILYNLQDTNRVLDVYNSQIANGTHVIVDSYHGNTNQQWIINLI | Function: Agglutinates human erythrocytes . The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of botulinum neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host . The hemagglutinin (HA) component is involved in binding to the upper small int... |
P46085 | MSLSIKELYYTKDKSINNVNLADGNYVVNRGDGWILSRQNQNLGGNISNNGCTAIVGDLRIRETATPYYYPTASFNEEYIKNNVQNVFANFTEASEIPIGFEFSKTAPSNKSLYMYLQYTYIRYEIIKVLQNTVTERAVLYVPSLGYVKSIEFNSEEQIDKNFYFTSQDKCILNEKFIYKKIDDTITVKESKNSNNNINFNTSQTILPYPNGLYVINKGDGYMRTNDKDLIGTLLIESSTSGSIIQPRLRNTTRPLFNTSNPTIFSQEYTEARLNDAFNIQLFNTSTTLFKFVEEAPTNKNISMKVYNTYEKYELINYQN... | Function: The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of botulinum neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host . The HA component is involved in binding to the upper small intestine through interactions with glycolipids and g... |
Q8KLS9 | MIDLPRHPPSMLPVIRTVPEHAATGELKRRYDAVKSAFDVPWMGVVAMAHTQYPRFFDALWEGFEPIAGTRAFQDACRAMRAATEAGVERSLGISPLAHRLQDLGYDPREIGEIRTIIEVFSHGNYPYILLATVSRYLLSGGDLSGEPQVFETSPRSPHIFHQPILMEPHHADEHTRGIFADIQATLALPILNTDYRALARWPSYFHLAWAELRPLIRTPSHAALSQQLHEQAIAVLRTLPNPARLKGDMVTRGCGR | Function: Catalyzes the hydrolytic dehalogenation of small (R)-2-haloalkanoic acids to yield the corresponding (S)-2-hydroxyalkanoic acids. Acts on acids of short chain lengths, C(2) to C(4), with inversion of configuration at C-2.
Catalytic Activity: an (R)-2-haloacid + H2O = a (2S)-2-hydroxycarboxylate + a halide ani... |
Q2UH56 | MKLAVFSAKSYDKHYFDATLRKHHPALCEITYHSFALSSETVSLAQDSDAVCVFVNDQLDAPVLETLYANGVRAILLRCAGFNNINLQVAEDLGFFVANVPSYSPEAVAEFAVALIQTLNRKTHRAFNRVREGNFNLEGFLGRTLYGKTVGVVGVGRIGLAFAKILHGFGCKLVAYDPFGGEEFKKYGEFVELGDLLAQSDVVSLHCPLTEGTRHVINDENLGRMKKGALLVNTSRGGLVNTKAVINALKSGQLGGVALDVYEEEGALFYNDHSGEIIHDDVLMRLMTFPNVLVCGHQAFFTEEALSEIAGVTLGNLEDF... | Function: 2-hydroxyacid dehydrogenase that is capable to reduce pyruvate, hydroxypyruvate and glyoxylate in a NADPH- or NADH-dependent manner . In contrast to 2-HadhD/morA, does not recognize 4-methyl-2-oxopentanoate (MOA) as a substrate .
Catalytic Activity: a (2R)-2-hydroxycarboxylate + NADP(+) = a 2-oxocarboxylate +... |
Q53464 | MDYIKGIAFDLYGTLFDVHSVVGRCDEAFPGRGREISALWRQKQLEYTWLRSLMNRYVNFQQATEDALRFTCRHLGLDLDARTRSTLCDAYLRLAPFSEVPDSLRELKRRGLKLAILSNGSPQSIDAVVSHAGLRDGFDHLLSVDPVQVYKPDNRVYELAEQALGLDRSAILFVSSNAWDATGARYFGFPTCWINRTGNVFEEMGQTPDWEVTSLRAVVELFETAAGKAEKG | Function: Catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids . Acts on acids of short chain lengths, C(2) to C(4), with inversion of configuration at C-2 . Active with 2-halogenated carboxylic acids and converts only the S-isomer (or L-isomer... |
O87871 | MAAKSSVSSWRSEMSSNPHRWMMTSPGAPMVRAEFEIGELSADQVVVAVAGCGVCHTDLGYYYDSVRTNHALPLALGHEISGRVVQAGANAAQWLGRAVIVPAVMPCGTCELCTSGHGTICRDQVMPGNDIQGGFASHVVVPARGLCPVDEARLAAAGLQLADVSVVADAVTTPYQAVLQAGVEPGDVAVVIGVGGVGGYAVQIANAFGASVVAIDVDPAKLEMMSKHGAALTLNAREISGRDLKKAIEAHAKANGLRLTRWKIFECSGTGAGQTSAYGLLTHGATLAVVGFTMDKVEVRLSNLMAFHARALGNWGCLPE... | Cofactor: Binds 2 Zn(2+) ions per subunit. One of the Zn(2+) is essential for catalytic activity while the other has a structural function.
Function: Involved in the central benzoyl-CoA catabolism. Catalyzes the oxidation of 6-hydroxycyclohex-1-ene-1-carbonyl-CoA to 6-oxocyclohex-1-ene-1-carbonyl-CoA. It is specific to... |
Q60099 | MIKAVVFDAYGTLFDVQSVADATERAYPGRGEYITQVWRQKQLEYSWLRALMGRYADFWGVTREALAYTLGTLGLEPDESFLADMAQAYNRLTPYPDAAQCLAELAPLKRAILSNGAPDMLQALVANAGLTDSFDAVISVDAKRVFKPHPDSYALVEEVLGVTPAEVLFVSSNGFDVGGAKNFGFSVARVARLSQEALARELVSGTIAPLTMFKALRMREETYAEAPDFVVPALGDLPRLVRGMAGAHLAPAV | Function: Catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids . Acts on acids of short chain lengths, C(2) to C(4), with inversion of configuration at C-2 . Active with 2-halogenated carboxylic acids and converts only the S-isomer (or L-isomer... |
P35647 | MVSALSCTHERRCYAIRTHLLQNYAGMGLSHYSGSSFVAAQHTGWYLRQAARIARAAEVFELQEDGTVLAEHILQPDSGVWTLYPQAQHKVEPLDDDFAVQLEFHCEKADYFHKKHGMTTTHSAIREAVQTVAPCKTLDLGCGQGHNALFLSLAGYDVRAVDHSPAAVASVLDMAAREQLPLRADAYDINAAALNEDYDFIFATVVFIFLQAGRVPEIIADMQAHTRPGGYNLIVSAMDTADYPCHMPFSFTFKEDELRQYYADWELLKYEEAVGLMHATDAQGRPIQLKFVTMLAKKPG | Function: Induces agglutination of neuraminidase-treated erythrocytes.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33460
Sequence Length: 300
Subcellular Location: Cell membrane
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Q0VBY3 | MKVKVIPVLEDNYMYLVIEERTREAVAVDVAVPKRLLEIVGRERVSLTTVLTTHHHWDHARGNAELARLLPGLVVLGADERICALTRRLAHGEELRFGAIHVRCLLTPGHTLGHMSYFLWEEECPDPPAVFSGTGCPVPTCPTSPCPIPLSLTHPTPQGMHCPWPAAAHAWRAQFSRCTRAWWRPWAPCPLRQ | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Hydrolase acting on ester bonds.
Sequence Mass (Da): 21696
Sequence Length: 193
EC: 3.1.2.-
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Q5ZLY2 | MKVKVISVLEDNYMYLVIEESTRDAVAVDAAVPKRLLEIVRKEDVVLRAVLITHHHWDHARGNEELVRLCPGLRVYGADERIGALTHRVAPDEELTFGAIRVRCLFTPCHTKGHMCYFMWEDGSLDAPALFSGDTLFVGGCGQFLEGTAEQMYTNLTQVLGDLPKETKVFCGHECTVRNLKFALKVEPENEAVKKKLAWARQRDDEDLPTVPSTLQEEFLYNPFLRVTEEAVQKFTGRKEPVEVLRALRTEKDNFKKPKERPHPQAMLAFDWGLFAPFLEKK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Hydrolase acting on ester bonds.
Sequence Mass (Da): 32228
Sequence Length: 282
EC: 3.1.2.-
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Q6PII5 | MKVKVIPVLEDNYMYLVIEELTREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLGADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTAGHMSYFLWEDDCPDPPALFSGDALSVAGCGSCLEGSAQQMYQSLAELGTLPPETKVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKARPLSRRGKRVGGEGTGFGVGGALRQGLMVTGACGHSRRGMRMTCPLCRRLWARSASTTPSCGWREYGCCPGASTVTWTLRKASGDCVLG | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Hydrolase acting on ester bonds.
Sequence Mass (Da): 31557
Sequence Length: 290
EC: 3.1.2.-
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Q9DB32 | MKVKVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLWEDDCPDSPALFSGDALSVAGCGWHLEDTAQQMYQSLAKTLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDIPTVPSTLGEELMYNPFLRVTEDAVRAFTGQVAPAQVLEALCRERARFQPAVEPPQPQVRALLALQWGLLSTHQKK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Hydrolase acting on ester bonds.
Sequence Mass (Da): 31490
Sequence Length: 283
EC: 3.1.2.-
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P96274 | MVSWPGLGTRVTVRYRRPAGSMPPLTDAVGRLLAVDPTVRVQTKTGTIVEFSPVDVVALRVLTDAPVRTAAIRALEHAAAAAWPGVERTWLDGWLLRAGHGAVLAANSAVPLDISAHTNTITEISAWYASRDLQPWLAVPDRLLPLPADLAGERREQVLVRDVSTGEPDRSVTLLDHPDDTWLRLYHQRLPLDMATPVIDGELAFGSYLGVAVARAAVTDAPDGTRWVGLSAMRAADEQSATGSAGRQLWEALLGWGAGRGATRGYVRVHDTATSVLAESLGFRLHHHCRYLPAQSVGWDTF | Function: Shows histone acetyl transferase (HAT) activity with recombinant eukaryotic H3 histone expressed in bacteria as substrate and acetyl-CoA as donor . May be involved in survival under stress conditions .
Catalytic Activity: acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]
Sequence Mas... |
P13231 | MGNRAFKSHHGHFLSAEGEAVKTHHGHHDHHTHFHVENHGGKVALKTHCGKYLSIGDHKQVYLSHHLHGDHSLFHLEHHGGKVSIKGHHHHYISADHHGHVSTKEHHDHDTTFEEIII | Function: May act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments.
PTM: Phosphorylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13456
Sequence Length: 118
Subcellular Location: ... |
Q9FJT8 | MVQKQQASAGPGTEPKKRRRVGFSPADTGVEANECIKIYLVSSKEEVDSSDISSVKPVDLNDFFDGDGKIYGYQGLKINVWINSISLHSYADITYQSTINGDKGITDLKSALQNIFAETIVDTKDEFLQTFSTQRDFIRNMVSNGEVMHAGATDGSSKNAEVVPSDPQVIRMEIGSPNAGLLYSRLVPLVLLFVDGSNPIDVTDPDWHLYLLIQKKEEKEDPLYRIVGFTAIYKFYRYPDRLRMRLSQILVLPSFQGKGLGSYLMEVVNNVAITENVYDLTVEEPSEKFQHIRTCIDINRLRSFDPIKPDIDSAVQTLTK... | Function: Acetylates soluble but not nucleosomal H4 (By similarity). Acetylates 'Lys-12' of histone H4.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Sequence Mass (Da): 52738
Sequence Length: 467
Subcellular Location: Nucleus
EC: 2.3.1.48
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P03138 | MGQNLSTSNPLGFFPDHQLDPAFRANTANPDWDFNPNKDTWPDANKVGAGAFGLGFTPPHGGLLGWSPQAQGILQTLPANPPPASTNRQSGRQPTPLSPPLRNTHPQAMQWNSTTFHQTLQDPRVRGLYFPAGGSSSGTVNPVLTTASPLSSIFSRIGDPALNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSPTSNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTCMTTAQGTSMYPSCCCTKPSDGNCTCIPIPSSWA... | Function: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specifici... |
Q8RFL1 | MDKMFCYQCQETAKGTGCTSIGVCGKTSETSGLQDLLLYTEKGVAAYSTVFRKNGKAKELLEGKVNRYLINSLFITITNANFDDNAILDEIKAGLKLREELKALATDEEKKEAEKYGADLVNWYYESNEDLIKFSENQSVVGVLRTENEDVRSLRELIMYGLKGMAAYAEHAFNLGKTSEEIFAFVEEALLGTMDDSLNAEQLVALTIKTGEYGVKVMALLDEANTSALGTPEITKVKIGAGKRPGILISGHDLWDLKQLLEQSKDSGIDIYTHSEMLPGHGYPELKKYSHFYGNYGNAWWDQRKDFTNFNGPIIFTTNC... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
Catalytic Activity: A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine
Sequence Mass (Da): 62678
Sequence Length: 566
Subcellular Location: Cytoplasm
EC: 1.7.99.1
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P80476 | TVADKQARLMPLFKHLTALTREKLPLDQRDERLKGVGILPRGTLFSCFHARHLAEATELYVALYGAKDFNDFIHLCEQARQIVNEGMFVYAVSVAVLHREDCKGITVPPIQEVFPDRFVPAETINRANKEASNHPDQQSIVVEAEETGNILDPEYKLSYFREDIGINAHHWHWHIVYPATWNPTVMGKEKDRKGELFFYMHQQMCARYDSERLSNGLQRMIPFHNFDEPLEGYAPHLTSLVSGLQYASRPEGYSIHDLSDVDVQDMVRWRERILDAINMHYIVDKDNNKIPLDIEHGTDILGDIIESSDESKNVEYYGSL... | Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
PTM: Three disulfide bonds are present.
Sequence Mass (Da): 71786
Sequence Length: 626
Subcellular Location: Secreted
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P84619 | LMRKDVDTLTD | Cofactor: Binds 2 copper ions per heterodimer.
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
PTM: Forms a thioether bond between 2 amino acids.
Sequence Mass (Da): 1306
Sequence Length: 11
Subcellular Location: Secreted
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Q8WUI4 | MDLRVGQRPPVEPPPEPTLLALQRPQRLHHHLFLAGLQQQRSVEPMRLSMDTPMPELQVGPQEQELRQLLHKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPNSPGIPYRTLEPLETEGATRSMLSSFLPPVPSLPSDPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPILGSEALLGQRLRLQETSVAPFALPTVSLLPAITLGLPAPARADSDRRTHPTLGPRGPILGSPHTPLFLPHGLEPEAGGTLPSRLQPILLLDPSGSHAP... | Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases a... |
Q8C2B3 | MHSPGAGCPALQPDTPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAGLHQQQRSAEPMRLSMDPPMPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPALGSEADGDRRTHSTLGPRGPVLGNPHAPLFLHHGLEPEAGGTLPSRLQPILLLDPSVSHAPLWTVPGLGPLPFHF... | Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases a... |
Q99P96 | TPGSQPQPMDLRVGQRPTVEPPPEPALLTLQHPQRLHRHLFLAGLQQQQRSAEPMRLSMDPPLPELQGGQQEQELRQLLNKDKSKRSAVASSVVKQKLAEVILKKQQAALERTVHPSSPSIPYRTLEPLDTEGAARSVLSSFLPPVPSLPTEPPEHFPLRKTVSEPNLKLRYKPKKSLERRKNPLLRKESAPPSLRRRPAETLGDSSPSSSSTPASGCSSPNDSEHGPNPALGSEADG | Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases a... |
Q9BY41 | MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTG... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) . Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation... |
Q8VH37 | MEMPEEPANSGHSLPPVYIYSPEYVSICDSLVKVPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDEDHPDSIEYGLGYDCPATEGIFDYAAAIGGGTITAAQCLIDGKCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFDRILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDMSDVGLGKGRYYSVNVPIQDGIQDEKYYHICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYVLQWQLATLILGGGGYNLANTARCWTYLTG... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation,... |
Q6GPA7 | MSRVVKPKVASMEEMAAFHTDAYLQHLHKVSEEGDNDDPETLEYGLGYDCPITEGIYDYAAAVGGATLTAAEQLIEGKTRIAVNWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDIGLGKGRYYSINVPLQDGIQDDKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPEGIGKCLKYVLQWQLPTLILGGGGYHLPNTARCWTYLTALIVGRTLSSEIPDHEFFTEYGPDYVLEITPSCRPDRNDTQKVQEILQSIKGN... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation,... |
Q5ZKH6 | MHSMISSVDVKSEVPVGLEPISPLDLRTDLRMMVPMVDPIMREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKLQQELLAIKQQQELLEKEQKLEQQRQEQELERHRREQQLPPLRGKERGRERAVASTEVKQKLQEFLLSKSATKDSPANGKNHSVSRHPKLWYTAAHHTSLDQSSPPLSGASPPYKYTLPGSQDAKDDFPLRKTASEPNLKVRSRLKQKVTERRSSPLLRRKDGNVVSSFKKRLFEVTESSVSSSSPGSGPSSPSNGPTSSITESETSVLPSSIQAEHLVSQQRLLIQDESVN... | Function: Devoided of intrinsic deacetylase activity, promotes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) by recruiting other histone deacetylases. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regul... |
Q9UKV0 | MHSMISSVDVKSEVPVGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVSRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDAKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNVVTSFKKRMFEVTESSVSSSSPGSGPSSPNNGPTGSVTENETSVLPPTPHAEQMVSQQRILIHEDSMNLLS... | Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-depende... |
Q99N13 | MHSMISSVDVKSEVPMGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDSKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESSVSSSSPGSGPSSPNNGPAGNVTENEASALPPTPHPEQLVPQQRILIHEDSMNLLS... | Function: Devoided of intrinsic deacetylase activity, promotes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) by recruiting HDAC1 and HDAC3. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell... |
Q70I53 | MAIGYVWNTLYGWVDTGTGSLAAANLTARMQPISHHLAHPDTKRRFHELVCASGQIEHLTPIAAVAATDADILRAHSAAHLENMKRVSNLPTGGDTGDGITMMGNGGLEIARLSAGGAVELTRRVATGELSAGYALVNPPGHHAPHNAAMGFCIFNNTSVAAGYARAVLGMERVAILDWDVHHGNGTQDIWWNDPSVLTISLHQHLCFPPDSGYSTERGAGNGHGYNINVPLPPGSGNAAYLHAMDQVVLHALRAYRPQLIIVGSGFDASMLDPLARMMVTADGFRQMARRTIDCAADICDGRIVFVQEGGYSPHYLPFC... | Cofactor: Binds 1 zinc ion per subunit.
Function: Exhibits significant levels of protein deacetylase activity comparable to those of eukaryotic HDACs in assays both with fluorogenic peptidic substrates and acetate-radiolabeled histones. Accepts proteins with epsilon-acetylated lysine residues and tritiated-acetate-prel... |
A6QQC6 | MWLRVFTAFLSFTAGACSGLKVAVPSHTVHGIRGQALYLPVHYGFHTPASDIQVIWLFERPHTMPKYLLGSVNKSVVPDLEYQHKFTMMPPNASLLINPLQFTDEGNYIVKVNIQGNGTLSASQKIQVTVDDPVTKPVVQIQPSSGAVEYVGNMTLTCLVEGGSRRVYQWLKNGRPVHTSSTNSFSLQNSSLHIAPVTKEDIGNYSCLVKNPVSRMESDIIMPTIYYGPYGLRVNSDRGLKVGEVFTVDIGEAILFDCSADSYPPNTYSWIQRTNNATYVIKHGPRLEVASEKIAQKTTDYMCCAYNNITGRRDETHFTV... | Function: Required during prometaphase for centrosome maturation. Following poly-ADP-ribosylation (PARsylation) by TNKS, translocates from the Golgi apparatus to mitotic centrosomes and plays a key role in the formation of robust microtubules for prompt movement of chromosomes: anchors AKAP9/CG-NAP, a scaffold protein ... |
A8MVW5 | MGQDAFMEPFGDTLGVFQCKIYLLLFGACSGLKVTVPSHTVHGVRGQALYLPVHYGFHTPASDIQIIWLFERPHTMPKYLLGSVNKSVVPDLEYQHKFTMMPPNASLLINPLQFPDEGNYIVKVNIQGNGTLSASQKIQVTVDDPVTKPVVQIHPPSGAVEYVGNMTLTCHVEGGTRLAYQWLKNGRPVHTSSTYSFSPQNNTLHIAPVTKEDIGNYSCLVRNPVSEMESDIIMPIIYYGPYGLQVNSDKGLKVGEVFTVDLGEAILFDCSADSHPPNTYSWIRRTDNTTYIIKHGPRLEVASEKVAQKTMDYVCCAYNN... | Function: Required during prometaphase for centrosome maturation. Following poly-ADP-ribosylation (PARsylation) by TNKS, translocates from the Golgi apparatus to mitotic centrosomes and plays a key role in the formation of robust microtubules for prompt movement of chromosomes: anchors AKAP9/CG-NAP, a scaffold protein ... |
Q14CZ8 | MKRERGALSRASRALRLAPFVYLLLIQTDPLEGVNITSPVRLIHGTVGKSALLSVQYSSTSSDRPVVKWQLKRDKPVTVVQSIGTEVIGTLRPDYRDRIRLFENGSLLLSDLQLADEGTYEVEISITDDTFTGEKTINLTVDVPISRPQVLVASTTVLELSEAFTLNCSHENGTKPSYTWLKDGKPLLNDSRMLLSPDQKVLTITRVLMEDDDLYSCMVENPISQGRSLPVKITVYRRSSLYIILSTGGIFLLVTLVTVCACWKPSKRKQKKLEKQNSLEYMDQNDDRLKPEADTLPRSGEQERKNPMALYILKDKDSPE... | Function: Involved in regulating cell motility and cell-matrix interactions. May inhibit cell growth through suppression of cell proliferation.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 46026
Sequence Length: 416
Domain: The cytoplasmic domain plays an important rol... |
Q5U5R9 | MSEAVRVPSPATPLVVAAPAPEERKGKESEREKLPPIVSAGAGATAGLDRGAKGQISTFSSFISAVSPKKEAAENRSSPAHLVFPNIKNVREPPPICLDVRQKQRTSMDASSSEMKAPVLPEPILPIQPKTVKDFQEDVEKVKSSGDWKAVHDFYLTTFDSFPELNAAFKKDATASFNTIEDSGINAKFVNAVYDTLLNTPQDVQKTVLKGIINSLLREWKGPRTKDDLRAYFILLQNPQFNNTSTYVIYAHLLRQIATLVEADHHFLVHWFKKLSQKRFKQLVERLLQFISLRLFPAKPEEFPPITKCSWWIPSAAKVL... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-... |
Q8CDU6 | MSEAARDLSPGAPPAVAAAAPEERKGKEPEREKLPPIVTAGAAAGLDRGSKGQISTFSSFVSTVTQKKEAAENRSSPTHLALPNIRNVRDLPPICLDVRQKQRMSVEALPSEVKVPPLPEPSLPSQPKTVKDFEEDLEKAEATGNWKTVHAFYITAFDSFTELNTAFKKDATASFNTIEDSGLNANLVNAVFDALLNTPQDIQKSVLKGIINSLLQEWKGPRTKDDLRAYFILLQNPQFNITSTYVIYAHLLRQIATLVEADHHFLVHWLKKLSQKKFKQLVERLLQFVSLRLFPAKPEEFPPLTKCTWWIPSAAKVLAL... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-... |
Q5T447 | MAGPGPGAVLESPRQLLGRVRFLAEAARSLRAGRPLPAALAFVPREVLYKLYKDPAGPSRVLLPVWEAEGLGLRVGAAGPAPGTGSGPLRAARDSIELRRGACVRTTGEELCNGHGLWVKLTKEQLAEHLGDCGLQEGWLLVCRPAEGGARLVPIDTPNHLQRQQQLFGVDYRPVLRWEQVVDLTYSHRLGSRPQPAEAYAEAVQRLLYVPPTWTYECDEDLIHFLYDHLGKEDENLGSVKQYVESIDVSSYTEEFNVSCLTDSNADTYWESDGSQCQHWVRLTMKKGTIVKKLLLTVDTTDDNFMPKRVVVYGGEGDNL... | Function: E3 ubiquitin ligases accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of TRIOBP and its subsequent proteasomal degradation, thus facilitating cell cycle progression by regulating the t... |
Q9PHX2 | MYYCISFTHKNTDIALREKLSFSNEAKKGEFLKIISTHENIEECLVISTCNRVEIVAFVKMACAEFIVKSLALLCDVDKDILLEKADIFEDSGAIHHLFSVASSLDSLVVGETQIAGQLKDAFAFAVKNNFCGVHLSRAVHSAFKCAAKVRNETQISKNSISVASVAVAKAKELADLTQKKAVVIGAGEMGELAAKHLIAAGAKVIILNRDLQKAKDLCERLGVLSEYDSLENLKKYLNQYEFFFSATNAPNAIITNSLIEELSYKRYFFDIAVPRDIDINENENISVFAVDDLEIVVQKNLALREQEARMAYGIIGRET... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 48697
Sequence Length: 432
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q3ACT4 | MYLVVVGVNHRTAPVEVREKLSFSDHQLKDAFSALLSYPSIDGSVILSTCNRTEVYVASLDVDTGLKVVREFLANWAGLSLSDIKNYTYNYTLYDAVHHLFRVASGLDSMILGETQILGQVRDAFLKASSLKASNKILNTLFQHAITVGKKVRTETGIDKNPVSISYAAVQLACSFFGSLKDKKALLIGAGKMSSLTAKHLSYYGIKEIIVANRSFEKAEQFAREFNGIAVPFAKIYDILAEVDLVISCTGAPHLIIHKEQLELVIGNRQHPLYLIDIAVPRDIDPEIAKLPNVFLYDIDKLQNVVTKNLEERKKLAEMA... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 50498
Sequence Length: 449
Domain: Possesses an unusual extended V-shaped dimeric str... |
A0RXF8 | MIPGLINARVTFHNSPVHALERFTFRDVGAALEGFRAGSGLDECVIVQTCNRVELFGASASPDMGSIRRTWASLAGIDESLFGGHLESSGGGEVLEHLLRLTSGLDSMVVGEEQILGQVKNAITSARTSGASGRRLNTLFDRAIRSGTRIRNSTGIGSGGVSVGSMAVRLVEENMDDLHSRSILLIGTGEVSTLVAKSLGKRGYDFSVASRTLQRSQAFCSAMGGSPVLFEDVLDGFGGYDVLFVATGAPYFLVTYDKISEVLESRGGMMILDLSNPRTVDEKVATLGGIKLMNLDQIAEMVSKNMRNRMSSVGKVEQMI... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 44658
Sequence Length: 417
Domain: Possesses an unusual extended V-shaped dimeric str... |
P07997 | MEAVVRRCPFLARVSQAFLQKAGPSLLFYAQHCPKMMEAAPPAAARGLATSASRGQQVEETPAAQPEAKKAKEVAQQNTDGSQPPAGHPPAAAVQSSATKCPFLAAQMNHKSSNVFCKASLELQEDVKEMQVDRKGKEFAKIPTNSVVRNTEAEGEEQSGLLKKFKDIMLKQRPESVSHLLQDNLPKSVSTFQYDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDYSDSLITKKEVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDAALLFSSCFVANDSTLFTLAK... | Function: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products.
Catalytic Activity: glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA
Location Topology: Peripheral membrane protein
Sequence Mass (Da):... |
A9WIS2 | MNLFLAGLDHTTAPVEIREQLAFSQTDLPSALMQLTSSETGTPPLFAEAVILSTCNRVELYGVTNPGTTAQHVVDFLAAFHRRPAASFVHTLYFYQGEAVARHLCATAAGLRSLVLGEAQIQGQVRNAYEAAQRIGSVGSILHRLFQIALVAGKRVRHETTIGKGAASVSQAGVELARRRLGDLRGREVLLIGGGEVSELAAQNLIANGADRLTIVNRTSARAAALAERYGAEMLDFGALPQALARADIVISSTAAPVPIIYRHHVAEAIAHKQRARACGECDPPTMLLIDLAVPRDIAADVAQIPGVHLFTVDDLREVV... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 47312
Sequence Length: 434
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q2FTL0 | MTHALFSPFTIAGISHHTASVADMESVRFPDEEAFLTRAGDWFKGVILLQTCNRIEIMVHGNADLLGTFLESEGRAGWQMWKDADALSHLLDLAAGLDSMVIGEDQILGQLRKSLSLSESMSVADPLITLCINKAIHAGSEARRISGINRGAVSIGSAAVLLAEEQLGSLAGRHILVLGTGEMGVLVTQALAAKQLSAIYVANRTFDRAQCLAEKVHGTAVPMADLYRYLTMSDVIICCTAAPHPVIKVQEVMEALKGRSWPLDHSRRPLIIVDIAQPRDVEEDVGKIPGVCLYTIDDLRKVNDDTAQFRKEAAEKVREF... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 46830
Sequence Length: 424
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q60172 | MIILKADYKKYNVSELEKLRMDEEKFYETFDNAILLQTCNRVEIIFDADSLEEIKGIENIDLEKFDILFGDKAIEHLFRVACGLESMIVGEDQILGQLKNAYLKAKEKGRISKKLEKIILKAIHTGQRARVETKINEGGVSIGSAAVELAEKIFGLEGKNVLLIGAGEMANLVIKALKEKNIKAIIVANRTYEKAEKLAKELGGMAIKFDKLEEALRYADIVISATGAPHPILNKERLKNAGKTIIIDIANPRDTTDDIRELPDIFLFTIDDLRLVAEENLKKRKEEIPKVEMIICEELERLKEFLDKMRFETAIKELGQ... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 44847
Sequence Length: 392
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q9UXR8 | MEDLVCVGITHKEAEVEELEKARFESDEAVRDIVESFGLSGCVLLQTCNRVEVYASGARDRAEELGDLIHDDAWVKRGSEAVRHLFRVACGLESMMVGEQEILRQVKKAYDRAARLGTLDEALKIVFRRAINLGKRAREETRISEGAVSIGSAAVELAERELGSLHDKTVLVVGAGEMGKTVAKSLVDRGVRAVLVANRTYERAVELARDLGGEAVRFDELVDHLARSDVVVSATAAPHPVIHVDDVREALRKRDRRSPILIIDIANPRDVEEGVENIEDVEVRTIDDLRVIARENLERRRKEIPKVEKLIEEELSTVEE... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + N... |
A2SQU1 | MTRTLLTDIAVATADHSKYGEEVLGLFRFKDETAFFEKASKIFPGVVLLETCNRVEILVHGSAKQLRDFLHGEQRFGFDILEGEAALMHLLELAAGTKSMIIGEDQILGQMRRALLLAESHDTNDVITDVCLNTAIREGVSIRQKTSINKGAVSIGSAAVLLAEELMGDLDGKNILVVGGGEMGTLVARALCEKNLRAIYVTNRSFDRAVLLAEEIKGRAMRLDQLYPCIALSDVVISCTGAPHLIIHADELAETMNERFWPLDLEPRHLLLIDIAQPRDIDDACRDVPGVSLKTLDDLKSISEKNLAARKTECEHADVL... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 46697
Sequence Length: 424
Domain: Possesses an unusual extended V-shaped dimeric str... |
A2SD47 | MSVFALGLNHTTAPVDLRGRFAFTLEQLAPTLQGFRERLTTGQRPGTPEAAILSTCNRTELYCAAEPQLVRPALEWLAGVGGVGADTLSHHAYMLEGGEAARHAFRVASGLDSMVLGEPQILGQMKQAVREADAAGTLGSTLHQLFQRSFAVAKEVRTATEIGTHSISMAAAAVRLAAQLFEDLREIRVLFVGAGEMIELAATHFSARAPARMAVANRTLERGERLASRFGAESIRLSDLPQRLHEFDAVVSCTASSLPLIGLGAVERALKVRRHRPIFMVDLAVPRDIEPEVARLDDVYLYTVDDLSAIVQSGGEKRLA... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 47837
Sequence Length: 443
Domain: Possesses an unusual extended V-shaped dimeric str... |
A4YD89 | MNPVNDIIDSYSAIVYTHKTVGVDKLASHYLGWNEIKELSKYYDGEMAVLQTCNRIEIYLFSRNESSVNEILHYLNEVHNKVISTDATILRGEEAIKHLFEVASGIDSLSVGEYEILKQIKDAMRDSIKLGIGSRYIRALLERSLKVGRRVRLETGISRGKVGVYSLAVEFAKSRFGDILGKKIAILGAGEIGGKLALILHNEGATDVTIFNRTFERGRNLAIKYGYSYFPLDFSRLHNYDIIFSAIFYPEKVKAPEGTVVIDLGSPPVFEGSNVYTLKDLEELSKATLEERQREIERAESIIREGLEEFRKDCLNLVYD... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 48090
Sequence Length: 424
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q2NEH4 | MLVNIRIDFKIADIETMEKSYAKLDMINAELHEKLDILEEVTLKTCNRYEIYLLIDEEVNIPTTTFIVEKNDMAINHLLRLASGLESMIMGEDQILGQIKTARKNAIKNKTIGPKLEKVFTKAIHVGQTIRKNTHINEGGVSVGSGAVELIEEKYGSLKGKNVLIIGAGEMGTVVSKALLEKETNTIVVANRTYDKARQLAQELDGEAIKFDEMNNELVNIDIVISSTGAPHSIISKERIAFLPEEHLHDMIMLDLANPHDIENDVQELGVKLYNLDDLRYVTDKNKERRNKEAIKAEAIIEDETLLLKESLKQMEITPI... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 44733
Sequence Length: 395
Domain: Possesses an unusual extended V-shaped dimeric str... |
P42809 | MILNIRLDHKTSDVKTMETASGRIEEIVGELEALGAVTEKVPLMTCNRVEYYLHVTGVPPEFDFNGFTVEKDEDALLHLLRLASGLESMIIGEDQILGQIKAARLQALREGTCGPLLDMVFTKAVHVGQTVRRKTKINRGSVSIGSAAVDLAESIHGDLKCKKVLVIGAGKMGTLVARALAEKHLKAIMVANRTYERAYQLACELGGDAIHFDRLNRALRDADVVISATGSPHYILTRERVMDAVPPERRSSIVMVDIANPRDIEESVRELGVRLFTIDDLRGVAEENRKRREAEAREAEGIVRAELELLLRAMKHREVE... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 44536
Sequence Length: 398
Domain: Possesses an unusual extended V-shaped dimeric str... |
A0B577 | MSRITSMLVTHKKASISEIENAWHGDVEALLKWVSSHDTVEECAVLKTCNRVEIYVVSPRGEKVLFEIAKKARVSSRIIDIHDHDESLLHLLRLASGLESMIIGEDQILGQMKELYRTAKSLGYTGWVLDTAFKKAIQVGKRVRKETAINERSVSVGSAAVDLAEQILGGLEGKSVLVIGAGETGELISKALVSKNIGSLYVTNRTFGTALSLAASLGGTAVPYEEMKRKIREADVVISATSAPHYILLKDDIERAMEGRKNKLLIIDIANPRDVDEAVREIEGVELHNIDSLKQISDENMRLRMREIERVEAIIEEELE... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 46840
Sequence Length: 417
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q92G23 | MSYYDIIFSKHIDKIKSEGRYREFKALKRQADNFPFAEHANKQIVMWCINDYLGMSKHAKVMHASIDALLKYGVGSGGTRNIGGNNIAILELEKELANLHKKQAALVFTSGFVANDTTLASLAKIMPDIVFFSDELNHASIIAGITSSRAEKYIYRHLDVKHLEELLQSVDINRPKIVVFESAYSMDGFFSPIKDIINLAKKYNALTFIDEVHTVGLYGKQGGGIAELLNCSDQIDIIQGTLAKAYGTIGGYITSNHNLVDAIRLTAPGFIFTTSLPPVISTAATHSIRHLKESNEERIKHQEVVTKLKNSFERFNIPYL... | Catalytic Activity: glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA
Sequence Mass (Da): 46238
Sequence Length: 414
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
EC: 2.3.1.37
|
A7NKU4 | MHITLIGVHQRNTPVTVRERLAFSLRELPDALLALRRYVEEGIILSTCNRVEVCAVTHDSVGGDAALKSFLAEQRGVDQAVFVPSLYIYHNEAVVRHLYRLAAGLDSMVLGEDQIVGQIKEALAIAHASGAIGPVLHRVLHGALAAGKRARTHTGIASGHVSVVSVAIDALRQHADLLKQGRALVIGAGHMAELTLKHLIAEGCSAITVINRTETRASALAQRYGVAWRPWGDLSDALAMSDMVVSCTSAPGIVVSWQMVERAAVGRSVPLLLFDLAVPRDIDQRVVEIPGVHLYDVDALEPICVTNRAMRAAEAQRAEA... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 46118
Sequence Length: 425
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q1AUK2 | MLIAVAGMSHRSAPVEARERVAFAPCAARSFLRRLREEDGVPEAVLLSTCNRTELYVVAEAEPARDRLLGLLAEDRGVEPGSLYRDTYWHTDAEAVRHLYRVSASLDSMVVGEAQILGQVRDAYRMATEERCTGPVLNRLFHTALRVGKRVRAETGIGDSSLSVPHVAAKLAGEVFGSLEGRRALVLGAGEMSELLVRHLRDRGVAEIRIANRTRERAERLAALFGGRAADLGDLPRELARADIVVSSTGSGEWVIRGPEVAAALESREEPLFLIDIAVPRDVDPVVQSIEGAFLYDIDDLQAVVERNAEDRQEAAAAAE... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 47130
Sequence Length: 429
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q980U7 | MSKDEELLQNYCSILFTYKTIGISNLHLYYFRETEIKSLKQLINAEFAILQTCNRVEIYLYSDTNTLKEVNKIIQYLNNIHNEPIGNQARVLCGKDAAKHLFLVASGADSLSIGEYEILSQIRSTIDMFKKLGFSGKYLQIFFERAIKVGRKVREETSISKGKVGIYSLAIDEAKKRFNDFYDRRILVIGAGEMAQKITSMLHNEGAKDVTIMNRTIEKAKQLALKFGYNYEKLDLDKLGNFDVAFISIYHENLRLENKWNTLIVDITVPPLFTGNNVITLEELERISNLNFKAREEELAKINKLVEDGINELLYDYKKE... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 49422
Sequence Length: 426
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q9KY00 | MRMSAPELIRIVSRDSPMALAQVERVRAELAALHPGVRTEVVPVRTTGDKWLGDLSQVEGKGAFTKEVDAALLSGEADLAVHCVKDVPADRPLPAGTVFAAFLKRDDVRDALVHPDGLTLDELPDGTRVGTSSVRRVAQLAATHPHLRCVPFRGNANRRLAKLAAGEADALLLAVSGLERIGRTDVISEVLSTETMMPPIGAGILALQCREGDRALIEAVSALGDPRTHREATAERMFLHVLQGHCNSPIAGHAQVDRSGELSLRACVFTPDGKVRLNAHEWAGRLDPATLGTSVAVALLRQGAREIIDGIAH | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33413
Sequence Length: 313
Pathway: Porphy... |
A0LRF1 | MTTAAALSVLRLGTRRSTLARAQTEEIAGALRAAGCRVEIVGIQSTGDRHADVPLHEFAGSGVFVAELRAALLRGEVDVVVHSMKDLPTAEIPELAIAAIPRRADPRDALVTGAGCRLAELPTGAIVGTGSPRRAAQLRLLRPDLEIRPIRGNLDTRLGKLHAGGYAALIVAAAGLARLHRSEEAAEFFDPTVMLPAPGQGALAVECRRADIADGGRLAGILAGLDDPATRAAVTAERALLAAVGAGCSAPVGALGVVTADTLQLDAVVVDPSGTTAFRRSLTGTPDDASDLGRRLAADLIRAGADQLLQAPKQTGEPHD... | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 34137
Sequence Length: 331
Pathway: Porphy... |
Q9Y9J0 | MRVRVAARGSRLSLLQVEQALEELSRYAGVSMHWEVVRVKSAGDVWSDRPLESIGVVGVFTREVDRAVASGAADIAVHSLKDMPTSGYGGPLKIVYIASRPSARDALISRQGPGRVEDLEPGSTLGTSSARRRALSLHYNPRIRVENLRGNLDTRLRKLREGLYDAIIASEAGLIRLGVDVEYTPLDPSYFPPAPGQGFVAVVARVGSNVEKMLRDLDKPPWWHVAWAERGVLEGARAGCRTPVAAYAEPLGRSMVRVTAAALSPDGSRAYWARAEGRIEEARRIGVSLGEELSRVVEGWHKTGGGS | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33341
Sequence Length: 307
Pathway: Porphy... |
Q8UC46 | MQTKPFRIGTRGSPLALAQAYETRSRLMAAHGLPEEMFEIVVLSTKGDRITDRALSEIGGKGLFTEELENQLLSGELDIAVHSSKDMPTVLPEGLHLSAFLPREDMRDAFIGRTAPKLLELPQGAVVGSASLRRQALIRRLRPDLNVIVFRGLVDTRLRKLEEGQADATLLAFAGLKRLGKDNVPTEILDPKEFPPAPAQGAIGVESRIGDARMDKLLAPINDRPTYDAVTCERAFLAALDGSCRTPIAGYATCEGDNLHFSGLILTPDGQTSHGVEISGNRRDALILGKKAGEEVRAKAGSNFFEGWS | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33494
Sequence Length: 309
Pathway: Porphy... |
A1WVT9 | MAAESLRIATRRSQLAMWQAEHIAAELQRLHPGLEVELVPMSTRGDEILDQPLARIGGKGLFMKELEDGMLRGEADLAVHSMKDIPWRLPEGFDLAAVSDRADPRDAFVSNHYSDLDELPHGARVGTASLRRQCQIMDRRPDLQIEVLRGNVQTRLRKLDDGVYDAIILAASGLDRLELTHRIAGRLTPEQSLPAVGQGALGIECREGDERVMKLVEGLNHEATRIRINAERGMNARLEGSCQVPIGGYAELDGDEVHLRGLVGAIDGSEVIRGEIRGPAAEAENLGRQLGDDLLARGADRILKAVAEQQ | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33984
Sequence Length: 310
Pathway: Porphy... |
Q9HMY5 | MSSQQIRLATRGSDLALRQAGEVVDTLEDRRHDVELVEVETEGDRVTDALISDLGKTGAFVRALDQEVMEGTVDAAVHSMKDVPTEVPEDLVVAAVPHRENPADVLVTPDGTDLEDLPAGSVVGTASLRRGAQVQAHRPGLDVEPIRGNVGTRVEKLLAPALHREHERRTEAEKEAQSRDAREQRRGDYTADIEAGVENLDTEDGEEGAADDGDDTASSSEFEQSVTEWFDSLTPLQQSAMERDPDTEYDALVMARVGLERTGLLHHVGIEELSTGTHVPATGQGALCVTARRDSDVVDTLRDALEHVRTRVEVTAERVV... | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 42813
Sequence Length: 396
Pathway: Porphy... |
P56140 | MGNLVIGSRGSELALWQANHIKERLKKECLIESEIQIVKTKGDKILDTPLNKIGGKGLFTKELEELLLKGAIDLAVHSLKDVPVVFEKGLDLACITKRADVRDTFLSVKFPDLMSLPKGAKVGTTSLRRSMQIKLKRQDLDTESLRGNVQTRLKKLECGEFDAIILAEAGLCRLEIQGAKYRKAFSVEEMIPSMGQGALGVEMLKNHKHFATLQKLNDEKSAFCCRLEREFIKGLNGGCQIPIGVHASLMGDRVKIQAVLGLPNGKEVITKEKQGDKTKAFDLVQELLEEFLQSGAKEILEKAQLF | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33940
Sequence Length: 306
Pathway: Porphy... |
P08397 | MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTGDKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPHDAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQQEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHDPETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIHVPAQHEDGPEDDPQLVGITA... | Cofactor: Binds 1 dipyrromethane group covalently.
Function: As part of the heme biosynthetic pathway, catalyzes the sequential polymerization of four molecules of porphobilinogen to form hydroxymethylbilane, also known as preuroporphyrinogen . Catalysis begins with the assembly of the dipyrromethane cofactor by the ap... |
A2BL26 | MKLRVATRGSKLSIAQTMIALEAIKRVEPSLEYELVIVKTRGDIHQDKPFTAIGGKGLFEKEVNLAVLEGRADIAVHSLKDVPSAISPGLVLAMTPPRDPPYDVLVVRGGKEKTIWDLPSGAIVGTSSARRVAMLKHVRRDLVFKVLRGNVDTRLRKLEQGQYDAIVLAEAGLKRLGVDIEYWRIPPDILPPAPGQGIIGVYTLSSRSDILPILEKASDQKAMAEARAERAFLAYAGGGCHTPLGAYAELRGNTLYFHAALASPDGSRRVEVRVEGDPDKPTQVGLEAAFELRRLAAREGISL | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 32926
Sequence Length: 303
Pathway: Porphy... |
Q0BX92 | MTQIDPPKGGKRLRLGTRGSPLALAQAHQIADGIRAASAGAYDCEIVAFTTTGDKLTTERLINSGGKGLFTRELDDALSRGELDLAVHSLKDVPSVLPPGQIFAAFPKREDPRDGFLSHGAKSIQDLPEGATLGTASLRREAQALALRPDLKVVTFRGNVATRMRKLEEGLADATFLAMAGLTRLGLSEVATPIPLEDMLPAAGQGIIGVVTRDDVDTELLEILGQLSHEPSRVAAIAERAFLEKLDGSCRTPIAAHLFDRGDEWQLIGEVLSPGGTTRWRGDGVCRKDATDAQLVLLGRAVAQEIIFAAKEALPVFGDE... | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 34257
Sequence Length: 321
Pathway: Porphy... |
A8AAB4 | MKIKIAARGSKLSLKQVSMFTSYLLKFFPDLEYEVITVKTTGDKANAPFEELAKRGLTGLFEKEVNKAVLEGKADVAVHSLKDLPTELDPRLEIAAFLPRDPPYDVLISRAGNYDIFDLPKGSVVGTSSARRKALIKNLRPDLVVKDLRGNVDTRLEKLRRGEYDAIVLAEAGVSRLGLNVDYVRLDWRLFPPSPGQGIIVAVTRKGSEISDLLKSISDVKSEKLATAERTVLKEFGGGCFVALGAIAFEEGSLIRLRATVLSPSGRERVDVELIGKGPEEVGMRAAERLKALNPMKTTVGSEE | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33281
Sequence Length: 304
Pathway: Porphy... |
Q8KCJ3 | MKTVLVTRPKHQAEPFVRELAQYGLDSVVFPTIEIRPVTGWSVPDLTRFAGIFFTSPNSVQFFLERLLEESPDELPNLQQARVWAVGKTTGGDLEKHGVSIEPLPKSADAVSLMSGIDASEIEGKTFLFVRGSLSLGTIPEVIAKRGGICVELTVYDNIQPSLEETQKIKSLLTEGKIDCLSFTSPSTAINFFEAIDSKEVPSDVLIAAIGTTTSSALEKLGVKVDIIPEYFDGPNFAKAIAAALS | Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Mass (Da): 26616
Sequence Length: 246
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis;... |
P09126 | MSILVTRPSPAGEELVSRLRTLGQVAWHFPLIEFSPGQQLPQLADQLAALGESDLLFALSQHAVAFAQSQLHQQDRKWPRLPDYFAIGRTTALALHTVSGQKILYPQDREISEVLLQLPELQNIAGKRALILRGNGGRELIGDTLTARGAEVTFCECYQRCAIHYDGAEEAMRWQAREVTMVVVTSGEMLQQLWSLIPQWYREHWLLHCRLLVVSERLAKLARELGWQDIKVADNADNDALLRALQ | Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Mass (Da): 27798
Sequence Length: 246
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis;... |
P10746 | MKVLLLKDAKEDDCGQDPYIRELGLYGLEATLIPVLSFEFLSLPSFSEKLSHPEDYGGLIFTSPRAVEAAELCLEQNNKTEVWERSLKEKWNAKSVYVVGNATASLVSKIGLDTEGETCGNAEKLAEYICSRESSALPLLFPCGNLKREILPKALKDKGIAMESITVYQTVAHPGIQGNLNSYYSQQGVPASITFFSPSGLTYSLKHIQELSGDNIDQIKFAAIGPTTARALAAQGLPVSCTAESPTPQALATGIRKALQPHGCC | Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins . Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell... |
Q58401 | MKVVITRPKERADVFASLLKKEGFEPIIFPTLEIVYNKDLDVNLDSYDWIAFTSPSGVIGLYNILTENERENVKNKKIAVIGEKTAKTFKKYFGRDPDIMPNEYTAESLLREIKKVSKEEEKFLIPTTPSTRDVLKNNLNADLLFVYKSAEPENLKEDIKKLKELIAKDKFILTFTSGLTAKNFFKYVDDEFAEIIKDNYIVAIGPITAKVIEKFGFKPLIPKVYTIEGMLEVIRTLKER | Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Mass (Da): 27614
Sequence Length: 240
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis;... |
O26268 | MAVTRPPERSAEAVELIEGAGGRALVAPTLELKEAHTESLREVCRRADEWDLVIFTSQAAVESLFQLCREFAGKIRKDCLVAVIGPRTARVAGEHGLRVDIVPEDYTAEGLLDALTGLNIEGWKVALPRTLSARKVLPRGLEMMGAEVLVAEAYRSGLPEDTGPAEELIDGLLDGKVDAVTFTSPLTVENLFKIAGNRRKELIEVLKRVKVAAIGPITLRKLEEHGITAVTPERYTVKDMIAALAVSMGEDVD | Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Mass (Da): 27462
Sequence Length: 253
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis;... |
P51163 | MKVLLLKDAKEDDSGLDPYIQELRLCGLEATLIPVLSFEFMSLPSLSEKLSHPEGFGGLIFTSPRAVEAVKLCLEKDNKTEAWEKSLKDRWNAKSVYVVGSATASLVNKIGLDAEGAGSGNAEKLAEYICSKPSSELPLLFPCGTIKGDTLPKMLKDKGIPMESMHVYQTVPHPGIQGSLKSYYEDQGIPASITFFSPSGLKYSLEYIQALSGSSFDQIKFIAIGPSTTRAMAAKGLPVSCTAESPTPQALAAGIRNVLKPNHCC | Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell ... |
Q10QR9 | MALSSSSHLLPFSRPPATFPRARHAGGGRGRAGATGRFIACSSPPPPDVVVTRERGKNAKLIAALEKHNVQSLELPLIKHVEGPDTDRLSAVLRDEKFDWITITSPEAAAVFLEGWKAAGNPKVRIAVVGAGTERVFDEVIQYNDGSLEVAFSPSKAMGKFLASELPRTTETTCKVLYPASAKAGHEIQNGLSNRGFEVTRLNTYTTVSVQDVDPLILKPALSAPVVAVASPSALRAWLNLASQVDNWGNAIACIGETTASAAKKFGLKSIYYPTTPGLDGWVESILEALRAHGQSKEAPGC | Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, a precursor of tetrapyrroles such as chlorophyll, heme and phycobilins.
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Mass (Da): 32123
Sequence Length: 302
Pathway: P... |
Q59683 | MSILITRPSPAGEQLTQRLIDAGKHAFHAPLIEIAAGKELSILENKLNKLSTGDYLFLLSKNAVWYANWQLNQLQQSWPDTLFYYGIGQSTAEEFQQLTAHSIRYPEFGETSEDLLALSSLQQIENKRVLLLRGNGGRELLATTLRQRGAIVDECECYQRLFIDYVSEEFALKWKNAQVEYLCGHQCEMLQQLLSSRWI | Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Mass (Da): 22799
Sequence Length: 199
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis;... |
P48246 | MSGWRLLLTRPDEECAALAASLGEAGVHSSSLPLLAIDPLEETPEQRTLMLDLDRYCAVVVVSKPAARLGLERLDRYWPQPPQQTWCSVGAATAAILEAYGLDVTYPEQGDDSEALLALPAFQDSLRVHDPKVLIMRGEGGREFLAERLRGQGVQVDYLPLYRRRAPDYPAGELLARVRAERLNGLVVSSGQGLQNLYQLAAADWPEIGRLPLFVPSPRVAEMARELGAQRVIDCRGASAPALLAALTSAA | Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Mass (Da): 27279
Sequence Length: 251
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis;... |
Q59294 | MEHGFVALVGAGPGDKGLITIRGAELLSQADVVVYDRLVSQEIIKMIPTTAEKIDVGKENKFHPVKQEEINHILLEKSLEGKKVIRLKGGDPFVFGRGGEELELLYENNIPFEVVPGVTSAVAALCYGGIPATHRDFCSSLHIITGHAREGGQLSIPFHELKELNGTIVFLMGDSSLSYLMNGLINAGMEKDMPAAIVENGTRPNQRKLVATVGTLEQKALEMEIKSPAIIAVGKVCSLSEKFSWFMKKPLFGTKILVTRPKESSGTLVEKLRQLGAEPVEYPCIEVVPIPQNEKLYHACENIREYGWILLTSKNGIQIF... | Function: May catalyze sequential reactions to synthesize uroporphyrinogen III from hydroxymethylbilane (HMB) and then precorrin-2, which are intermediate compounds in both vitamin B12 and siroheme biosyntheses.
Catalytic Activity: 2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) + precorrin-2 + 2 S-adenosyl-L-h... |
P87214 | MKTALLLKTKSQPFDPYVEAFEKYGRDTAFIPVLRHKRVHEEQLRDKLKNVRKTYCGLIVTSQRVSETLDEALKQEDETERQKILMETPIFTVGPATDDSIRRLGFQQTHGKDCGRGEVLADLIEEWYTTTKQHKPLLFLVGEKHRDIIQRKLGDDRVDSLIVYATQELENTETQIKDTIRKHPTIDWIVAFSPTSICSLLNTFELKIATIGPTTGDYLKKLGTQPNVVSPAPNPESLASSIVAFDEENSS | Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Mass (Da): 28515
Sequence Length: 251
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis;... |
P42452 | MAEQPLIGKTILTTRAAGQSSPFAAQLRAAGAAVIEMPTLEIGPPSSWLPLDEAIAAIADFDWLILASANAVEAVQQRLAAQQKSWSDVPCAIAVVGQKTAQVLAAQGGKADYIPPEFIAESLVEHFPQPVAGQRLLFPRVETGGREQITQALQSQGAIVVEVPAYESRCPSQIPDDALIALRQAHLNLISFTSSKTVRNFCQLMASNLGVDWSARISGVAIASIGPQTSITCQELLGRVEVEAQEYTLDGLLLAIEQWARQTT | Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Mass (Da): 28196
Sequence Length: 264
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis;... |
P06174 | MSSRKKVRVLLLKNKTVPIDKYELECRSKAFEPIFVPLIKHTHVIQDFRNVLNTIPNYLNTINYIIITSQRTVESLNEAIIPTLTSEQKAALLSKTVYTVGPATANFIRRSGFINVKGGEDAGNGSILADIIIDDLSTDIKACPPSELLFLVGEIRRDIIPKKLHSKGIKVREVVTYKTEELSDGFKRFIHAMKECDEDEVFSDWVVVFSPQGTKEITQYLGDSNRLPGSHLRVASIGPTTKKYLDDNDVTSDVVSPKPDPKSLLDAIELYQRHK | Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the fourth step in the heme biosynthetic pathway.
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Mass (Da): 30912
Sequence Length: 275
Pathway: Porphyrin-containing co... |
Q9LR75 | MASHSSTLLSSPTFAPFSSHRLHYSPNPSTLRFSRPIRNKPNLALRCSVSIEKEVPETERPFTFLRDSDDVTPSSSSSSVRARFETMIRAAQDSVCDAIEAIEGGPKFKEDVWSRPGGGGGISRVLQDGNVFEKAGVNVSVVYGVMPPEAYRAAKGSASDQKPGPVPFFAAGVSSVLHPKNPFAPTLHFNYRYFETDAPKDVPGAPRQWWFGGGTDFTPAYIFEEDVKHFHSIQKQACDKFDPSFYPRFKKWCDDYFYIKHRDERRGLGGIFFDDLNDYDQEMLLSFATECANSVVPAYIPIVEKRKDMEFTEQHKAWQQ... | Function: Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III.
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Mass (Da): 43796
Sequence Length: 386
Pathway: Porphyrin-... |
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