ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q03393 | MSTEGGGRRCQAQVSRRISFSASHRLYSKFLSDEENLKLFGKCNNPNGHGHNYKVVVTVHGEIDPATGMVMNLADLKKYMEEAIMQPLDHKNLDMDVPYFADVVSTTENVAVYIWDNLQKVLPVGVLYKVKVYETDNNIVVYKGE | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.
PTM: Phosphorylation of Ser-19 is required for maximal enzyme activity.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + triphosphate
Sequence Mass (Da): 16386
Sequence Length: 145
Pathway: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
EC: 4.2.3.12
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Q9R1Z7 | MSAAGDLRRRARLSRLVSFSASHRLHSPSLSDEENLRVFGKCNNPNGHGHNYKVVVTVHGEIDPVTGMVMNLTDLKEYMEEAIMKPLDHKNLDLDVPYFADAVSTTENVAVYIWESLQKLLPVGALYKVKVFETDNNIVVYKGE | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.
PTM: Phosphorylation of Ser-18 is required for maximal enzyme activity.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + triphosphate
Sequence Mass (Da): 16188
Sequence Length: 144
Pathway: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
EC: 4.2.3.12
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Q90W95 | MAESSGNPPAERIGYITRVQSFSACHRLHSLRLSDEENKEVYGKCNNPYGHGHNYKVEVTVRGKIDPVTGMVMNLTDLKKCIEEVIMIPLDHKNLDKDVPYFADVVSTTENLAVYIWDNMAKALPASLPYEIRIHETDKNIVVYRGE | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + triphosphate
Sequence Mass (Da): 16679
Sequence Length: 147
Pathway: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
EC: 4.2.3.12
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P80081 | AQADATANEVAERIGYITRVQSFCASHRLHSPTLVMNITNIKEHIEEVIPLDHKNLDKDVPYFANVNVAVYIXDNMVKQLPANLLYEVKIHETDKNIVVYRGE | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + H(+) + triphosphate
Sequence Mass (Da): 11729
Sequence Length: 103
Pathway: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
EC: 4.2.3.12
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O52787 | MQFKNILVVCIGNICRSPMAEYLLKQNYPQLTIHSAGISGMIGYSADEKAQLCMERIGIDMSPHIAKKLNAELLKQADLILVMSQNQQKHIEQTWPFAKGKTFRLGHWQGKNIPDPYQHDQAFFDETSLLIQTCVADWTKHI | Function: Dephosphorylates ptk. May be involved in the production and the transport of exopolysaccharides.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 16215
Sequence Length: 142
Pathway: Glycan metabolism; exopolysaccharide biosynthesis.
EC: 3.1.3.48
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P24656 | MFPARWHNYLQCGQVIKDSNLICFKTPLRPELFAYVTSEEDVWTAEQIVKQNPSIGAIIDLTNTSKYYDGVHFLRAGLLYKKIQVPGQTLPPESIVQEFIDTVKEFTEKCPGMLVGVHCTHGINRTGYMVCRYLMHTLGIAPQEAIDRFEKARGHKIERQNYVQDLLI | Function: Plays a role in the regulation and processing of late viral mRNAs by displaying RNA 5'-triphosphatase and diphosphatase activities.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 19288
Sequence Length: 168
EC: 3.1.3.48
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Q7MUW6 | MKKTIFQQLFLSVCALTVALPCSAQSPETSGKEFTLEQLMPGGKEFYNFYPEYVVGLQWMGDNYVFIEGDDLVFNKANGKSAQTTRFSAADLNALMPEGCKFQTTDAFPSFRTLDAGRGLVVLFTQGGLVGFDMLARKVTYLFDTNEETASLDFSPVGDRVAYVRNHNLYIARGGKLGEGMSRAIAVTIDGTETLVYGQAVHQREFGIEKGTFWSPKGSCLAFYRMDQSMVKPTPIVDYHPLEAESKPLYYPMAGTPSHHVTVGIYHLATGKTVYLQTGEPKEKFLTNLSWSPDENILYVAEVNRAQNECKVNAYDAETGRFVRTLFVETDKHYVEPLHPLTFLPGSNNQFIWQSRRDGWNHLYLYDTTGRLIRQVTKGEWEVTNFAGFDPKGTRLYFESTEASPLERHFYCIDIKGGKTKDLTPESGMHRTQLSPDGSAIIDIFQSPTVPRKVTVTNIGKGSHTLLEAKNPDTGYAMPEIRTGTIMAADGQTPLYYKLTMPLHFDPAKKYPVIVYVYGGPHAQLVTKTWRSSVGGWDIYMAQKGYAVFTVDSRGSANRGAAFEQVIHRRLGQTEMADQMCGVDFLKSQSWVDADRIGVHGWSYGGFMTTNLMLTHGDVFKVGVAGGPVIDWNRYEIMYGERYFDAPQENPEGYDAANLLKRAGDLKGRLMLIHGAIDPVVVWQHSLLFLDACVKARTYPDYYVYPSHEHNVMGPDRVHLYETITRYFTDHL | Function: Serine proteinase. Releases tripeptides from the free amino terminus of proteins. Has a requirement for Pro in the P1 position, but is inactivated by Pro in the P1' position.
PTM: The N-terminus is blocked.
Catalytic Activity: Hydrolysis of Xaa-Xaa-Pro-|-Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline.
Sequence Mass (Da): 82266
Sequence Length: 732
EC: 3.4.14.12
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P69793 | MMDLDNIPDTQTEAEELEEVVMGLIINSGQARSLAYAALKQAKQGDFAAAKAMMDQSRMALNEAHLVQTKLIEGDAGEGKMKVSLVLVHAQDHLMTSMLARELITELIELHEKLKA | Cofactor: Can also use copper and nickel with lower efficiency.
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ChbABC PTS system is involved in the transport of the chitin disaccharide N,N'-diacetylchitobiose (GlcNAc2).
Sequence Mass (Da): 12748
Sequence Length: 116
Domain: The PTS EIIA type-3 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-3 domain.
Subcellular Location: Cytoplasm
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P69830 | MEKKHIYLFCSAGMSTSLLVSKMRAQAEKYEVPVIIEAFPETLAGEKGQNADVVLLGPQIAYMLPEIQRLLPNKPVEVIDSLLYGKVDGLGVLKAAVAAIKKAAAN | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ChbABC PTS system is involved in the transport of the chitin disaccharide N,N'-diacetylchitobiose (GlcNAc2).
Catalytic Activity: N(pros)-phospho-L-histidyl-[protein] + N,N'-diacetylchitobiose(out) = diacetylchitobiose-6'-phosphate(in) + L-histidyl-[protein]
Sequence Mass (Da): 11427
Sequence Length: 106
Domain: The PTS EIIB type-3 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-3 domain.
Subcellular Location: Cytoplasm
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P30335 | MPITDLVAPEAILPALKVNSKKQALQELAAKAAELTGQNERAVFEVLLQREKLGTTAVGYGVAIPHGKLPKLEKIFGLFARLDRPIDFESMDGQPVDLVFLLLAPEGAGADHLKALARIARLLRDQDIAKKLRASRDAQAIYSVLALPPATAA | Function: Seems to have a role in regulating nitrogen assimilation.
Sequence Mass (Da): 16455
Sequence Length: 153
Domain: The EIIA domain is phosphorylated by phospho-NPr on a histidyl residue.
Subcellular Location: Cytoplasm
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P69829 | MTNNDTTLQLSSVLNRECTRSRVHCQSKKRALEIISELAAKQLSLPPQVVFEAILTREKMGSTGIGNGIAIPHGKLEEDTLRAVGVFVQLETPIAFDAIDNQPVDLLFALLVPADQTKTHLHTLSLVAKRLADKTICRRLRAAQSDEELYQIITDTEGTPDEA | Function: Seems to have a role in regulating nitrogen assimilation.
Sequence Mass (Da): 17960
Sequence Length: 163
Domain: The EIIA domain is phosphorylated by phospho-NPr on a histidyl residue.
Subcellular Location: Cytoplasm
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Q9HVV4 | MIRLEQILTPGRSLVNVPGGSKKRVLEQIANLVARELPEFDAQTIFENLVAREKLGSTGFGNGIAIPHCRLSGCQSPISAVLHLDAPVDFDALDGAPVDLLFVLLVPEAATEEHLELLRQIAAMLDRADVRDRLRSAPTAEALYQIVVDVQNGQ | Function: Seems to have a role in regulating nitrogen assimilation.
Sequence Mass (Da): 16730
Sequence Length: 154
Domain: The PTS EIIA type-2 domain may serve a regulatory function, through its phosphorylation activity.
Subcellular Location: Cytoplasm
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P33670 | MIRLETILTPGRSLVNVPGGSKKRALEKVATVIADQVPELEMQDVFEKLVAREKLGSTGFGNGIAIPHCRLEGSSAPVSALLHLEAPID | Function: Seems to have a role in regulating nitrogen assimilation.
Sequence Mass (Da): 9488
Sequence Length: 89
Domain: The PTS EIIA type-2 domain may serve a regulatory function, through its phosphorylation activity.
Subcellular Location: Cytoplasm
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Q00576 | MASCVGSRTLSKDDVNYRMHFRMINEQQVEDITIDFFYRPHTITLLSFTIVSLMYFAFTRDDSVPEDNIWRGILSVIFFFLIISVLAFPNGPFTRPHPALWRMVFGLSVLYFLFLVFLLFLNFEQVKSLMYWLDPNLRYATREADIMEYAVNCHVITWERIVSHFDIFAFGHFWGWAMKALLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMVVCRFLEMRTYHWASFKDIHTTTGKIKRAVLQFTPASWTYVRWFDPKSSFQRVAGVYLFMIIWQLTELNTFFLKHIFVFQASHPLSWCRILFIGCITAPTVRQYYAYLTDTQCKRVGTQCWVFGVIGFLEAIVCIKFGQDLFSKTQILYVVFWLLCVAFTTFLCLYGMVWYAEHYGHREKTYSECEDGTPEISWHHGKGSKGSEDSPPKHSSNNESHSSRRRNRHSKSKVTNGVGKK | Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine . Catalyzes mainly the conversion of phosphatidylcholine . Also converts, in vitro and to a lesser extent, phosphatidylethanolamine .
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55350
Sequence Length: 471
Pathway: Phospholipid metabolism; phosphatidylserine biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.8.29
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P31452 | MLSQIQRFGGAMFTPVLLFPFAGIVVGLAILLQNPMFVGESLTDPNSLFAQIVHIIEEGGWTVFRNMPLIFAVGLPIGLAKQAQGRACLAVMVSFLTWNYFINAMGMTWGSYFGVDFTQDAVAGSGLTMMAGIKTLDTSIIGAIIISGIVTALHNRLFDKKLPVFLGIFQGTSYVVIIAFLVMIPCAWLTLLGWPKVQMGIESLQAFLRSAGALGVWVYTFLERILIPTGLHHFIYGQFIFGPAAVEGGIQMYWAQHLQEFSLSAEPLKSLFPEGGFALHGNSKIFGAVGISLAMYFTAAPENRVKVAGLLIPATLTAMLVGITEPLEFTFLFISPLLFAVHAVLAASMSTVMYLFGVVGNMGGGLID | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This operon may be cryptic in wild-type K12 strains (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39692
Sequence Length: 368
Domain: The EIIC domain forms the PTS system translocation channel and contains the specific substrate-binding site.
Subcellular Location: Cell inner membrane
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O69053 | MSSHYDVQALPAEQREHILRGFGLGWWRQLGQVAIVFGVVLLACWYVGLLDATTLLNGLPSIATLAGEAMPPDFSGYRSWIRPLIDTLAMSIAGTAIAVVFSLVVAFVAARNTAPHPLVFGVARVLLNALRSVPELIMGIIFVAAVGFGALPGVLALGLHSVGMVGKFFAEAIEHVDEAPVEAARAAGATPMQVLLHAVLPQVTPQFADVAIYRWEYNFRASTVMGMVGAGGIGFELMGSLRIMQYQEVAAILLVILAMVTLVDAFSGVLRKHFK | Function: Probably forms part of a binding-protein-dependent phosphite transporter. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29396
Sequence Length: 275
Subcellular Location: Cell inner membrane
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O69054 | MLPKLVITHRVHDEILQLLAPHCELMTNQTDSTLTREEILRRCRDAQAMMAFMPDRVDADFLQACPELRVVGCALKGFDNFDVDACTARGVWLTFVPDLLTVPTAELAIGLAVGLGRHLRAADAFVRSGEFQGWQPQFYGTGLDNATVGILGMGAIGLAMADRLQGWGATLQYHEAKALDTQTEQRLGLRQVACSELFASSDFILLALPLNADTQHLVNAELLALVRPGALLVNPCRGSVVDEAAVLAALERGQLGGYAADVFEMEDWARADRPRLIDPALLAHPNTLFTPHIGSAVRAVRLEIERCAAQNIIQVLAGARPINAANRLPKAEPAAC | Function: Catalyzes phosphite (phosphonate) oxidation.
Catalytic Activity: H2O + NAD(+) + phosphonate = H(+) + NADH + phosphate
Sequence Mass (Da): 36415
Sequence Length: 336
EC: 1.20.1.1
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Q6CSN3 | MYQLLFQRLGVTLTAGNDKKTSIPSNQLVGHLIGLILLCDDLNEAFADFQALLQNGIAISSSDRGYLVFDAHVTDCGCHLRAQMIQDVFSYFKNHEVTKLYIFDAVAKKLNELKRHCISLIQTLCWENTSAQKLGFPKNIKSYEELLKLLQWDTADISSAIADSFPMNPNNADQNEKGLVWNVTKLEVVLEFLYCSHFLSKNKIYNKKENLDSVTIDFNNAFEKRQLLSNKFHCQGTGKLGVGCRYLKHAKQSKNSFISVVSNLQSRLALLSIAFLKSRCTLPCDIEALQKNSPRNVSAIPNFLHFLILEREWSQNETPILLAVRKLHEHEHCDLYFEARINPHTFEWTLQHKECCEFEHHTPYIVITALATGSSTTKTAQLLAWELMKAQKNFRQFWLTFMSQHRQYPFEIEHDEDQLLETQVSQDIFELYCQSKREDRNQILFDDSTSLLPKHIFTEYPSIFFNFQKNVCSKHGALVI | Function: Probable cyclodipeptide synthase; part of the PUL gene cluster that mediates the formation of pulcherrimin, a red iron-containing pigment composed of two cyclized and modified leucine molecules that acts as a siderophore, a chelator that binds iron outside the cell for subsequent uptake . Two leucine molecules are cyclized via a cyclodipeptide synthase, and the resulting diketopiperazine is oxidized by a cytochrome P450 monooxygenase to generate pulcherriminic acid (PA), which can then spontaneously bind iron to form pulcherrimin . The probable cyclodipeptide synthase PUL1 and the cytochrome P450 monooxygenase PUL2 encode the enzymes responsible for the two-step pulcherrimin biosynthesis pathway (Probable).
Sequence Mass (Da): 55417
Sequence Length: 480
Pathway: Siderophore biosynthesis.
EC: 6.-.-.-
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Q6CSN2 | MLADILIPLIKKNWMAFVYFTPVLFVVLYLLKEWRAAYGFNNLGQTVAAPFGYERKTLPYNKENCARTKFLDGKSLSIKNRDQCGDLYLQRSGTYKEIVLTTPKQLMEYYKSNSKNHSKLDSFGAGAFLVALLGECLGFQNGSEWLSMRKVFDSFFTHKAAVENFPVMIDYISEWIKDLDTEQISDIDPLQLVSDLPFTCIAKYLYGSELCSKQFLQALKDLIPMHTELMHYSFLTVAGRFKIFQYFPSKKMKQVSQFQRQFIDLSLKQVELSRQSGQETVVEKLYRHVESGKFTFNNWIQTIDEILFANIEVTSTVMAWALVEMGSNIEEQNRLRCEILKVKEQSSKDDFNKETDPMQRYMKLTDTYLQYCVWETLRMHPLLWFSFPEISSETLFIDGIRISPNTPIVVDQYQINYNSPIWNPSDKPKDFGKKFAPSRFENITLRDALYSQVTFGAGSRKCLGRNFAELLIKSELAYILSKYKVTLTEKVEFSKDTFVVQPKTKIQLTAL | Function: Cytochrome P450 monooxygenase; part of the PUL gene cluster that mediates the formation of pulcherrimin, a red iron-containing pigment composed of two cyclized and modified leucine molecules that acts as a siderophore, a chelator that binds iron outside the cell for subsequent uptake . Two leucine molecules are cyclized via a cyclodipeptide synthase, and the resulting diketopiperazine is oxidized by a cytochrome P450 monooxygenase to generate pulcherriminic acid (PA), which can then spontaneously bind iron to form pulcherrimin . The probable cyclodipeptide synthase PUL1 and the cytochrome P450 monooxygenase PUL2 encode the enzymes responsible for the two-step pulcherrimin biosynthesis pathway (Probable).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59318
Sequence Length: 511
Pathway: Siderophore biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q6CSN0 | MKLTDSQKHLYSQYLAVTLIAVQFSFDTCVYLSSVVQYVKECGSDDPENYLFILQAVSAAVQVFFSFIIGDIASYVGSIKWVIIFLYFLSFVGNFLYSCAGAVSLNTLLGGRIICGAASSSGAVVYSYITAISKDRTTIFKLFSIYRTSAGICMALAQLVAILFALCDFTVRGYRITSYNAPTFASSFIILLICVLLMFVLENPPVKSARNPKNYLDAWKKFFSAGSNRLIASLILLWNMFLSTFFMCEVLYFMPIFLTLNVGWKTEYEGVAFMVSAVLGVAGSFFAPDLVKLFAKLNTPSTQDETDTSDNDKIEKEESEQKSDINTLHRNQVSLTIFALFVALIGQAFMIGASEALSNDKLPKTNSGIFFTAGLSITMLGYNFMGSSVPALFSMYIDPQVKVQLMPFIGAIAGVGKLVAPIVLAALYKTPLGLPIGVGFGMILVGISIPSLVYLRRNKM | Function: MFS-type transporer required for the uptake of iron via the uptake of the siderophore pulcherrimin-iron complex.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50444
Sequence Length: 460
Subcellular Location: Cell membrane
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Q8GTR4 | MALTLTPTSSVHLLSSISVARPRIFAADFNLRSRWRRRRPVTSISNFRLRLPSKTSLHCLCSSSSASSPMSLEVSSPNSQFLDCLIYSRAYWVTQGVIAWNVDVGEGSCYFYASKSAGLSFSEDGIDGYDLRIKLEAESGSLPADVIEKFPHIRNYKSFKVPKDLDIRDLVKSQLAVVCFDAEGRLIQGTGLQLPGVLDELFSYDGPLGAHFTPEGVSLHLWAPTAQAVSVCIYKNPLDKSPMEICPLKEANGVWSTEGACSWGGCYYVYKVSVYHPSTMKLETCYANDPYARGLSADGRKTFLVNLDSDDLKPEGWDNLADKKPCLRSFSDISIYELHVRDFSANDETVEPENRGGYLAFTSKDSAGVKHLQKLVDAGLTHLHLLPTFQFGDVDDEKENWKSVDTSLLEGLRPDSTEAQARITEIQNDDGYNWGYNPVLWGVPKGSYASDPTGPCRIIEFRKMVQALNCTGLNVVLDVVYNHLHASGPHDKESVLDKIVPGYYLRRNSDGFIENSTCVNNTASEHYMVDRLIRDDLLNWVVNYKVDGFRFDLMGHIMKATIVNAKSAIGSLRKETDGVDGSRIYLYGEGWNFGEVAENGRGINASQFNLGGTGIGSFNDRIRDATLGGSPFGHPLQQGFITGLLLQPNAHDHGSEATQELMLSTAKNHIQTGMAANLKDYMLTNHEGKEVKGSEVLMHDATPVAYASLPTETINYVSAHDNETLFDIISLKTPMEISVDERCRINHLASSMIALSQGIPFFHAGDEILRSKSLDRDSYNSGDWFNRLDFSYSSNNWGVGLPPKGKNEHNWPLIKPRLQDPSFKPKSSHIVATLHNFLDLLRIRYSSPLFRLDTARAIQERVRFHNTGPSSIPGAIVMSIEDGHRGIPSVSQIDPIYSLIVVIFNARPSEFSYPSPALKDRKLELHPVQVMSADEIVKKSVYDSFSGGFTVPARTTTVFVESRNG | Function: Involved in starch degradation and also probably in the trimming of pre-amylopectin chains during starch synthesis.
Catalytic Activity: Hydrolysis of (1->6)-alpha-D-glucosidic linkages in alpha- and beta-limit dextrins of amylopectin and glycogen, and in amylopectin and pullulan.
Sequence Mass (Da): 107067
Sequence Length: 965
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 3.2.1.142
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P20440 | MRNFILFPMMAVVLLSGCQQNRPTTLSPAVSGQAQLEQLASVAAGARYLKNKCNRSDLPADEAINRAAINVGKKRGWANIDANLLSQRSAQLYQQLQQDSTPEATKCSQFNRQLAPFIDSLRDNK | Function: Involved in the secretion of pullulanase.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13808
Sequence Length: 125
Subcellular Location: Cell outer membrane
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Q9LP21 | MEIFNFGQASDHRRLPDFGSGGFLQSLDTNPFLKNQYYNNSVEALELCKKLNKMGISCDMSIWTKPEEPFRVDPGDFGAKTLHESFGFDQNLTGASQIHDGFRNFSSVRVQNNNFHGVSPSPGLLGLQDSFNPNGFEEMMAFKDHKDFLLDHINEPIKRSPFLRGNDAFKGSLMFEGIRVSQILAAMEGSGASYPDEPKINGGLPLDLVSMVEIYGSVNLMARDQIGCRALQKLVEEGTVLDSKVIFLEIIDHVVELSMDPLGNYIVQKLLVVSDEEQRTMIVSVLTSKPRELIKICLNTNGTRVIQKMIKTVKTKQQIALVKSALEPGFLVLVNDSNGYHVLQSCLEFLVPNDNKFVVEAATEYCAQLATHQYGCYVLQCSLINTVGLQHERLVAEISRDSLRLSQDPFGNYVVQCLIDQQVSSVNLLLPFRTHCIELATQKFSSHVIEKCLRKYPESRAEIVRELLSYPNFEQLLQDPYANYVIQTALSVTKGAVRARLVEKVKRFGKLQSNPYCKKIFSKTILKK | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence Mass (Da): 59381
Sequence Length: 528
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Cytoplasm
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Q9LVC3 | MDQRRGNELDEFEKLLGEIPKVTSGNDYNHFPICLSSSRSQSIKKVDQYLPDDRAFTTSFSEANLHFGIPNHTPESPHPLFINPSYHSPSNSPCVYDKFDSRKLDPVMFRKLQQVGYLPNLSSGISPAQRQHYLPHSQPLSHYQSPMTWRDIEEENFQRLKLQEEQYLSINPHFLHLQSMDTVPRQDHFDYRRAEQSNRNLFWNGEDGNESVRKMCYPEKILMRSQMDLNTAKVIKYGAGDESQNGRLWLQNQLNEDLTMSLNNLSLQPQKYNSIAEARGKIYYLAKDQHGCRFLQRIFSEKDGNDIEMIFNEIIDYISELMMDPFGNYLVQKLLEVCNEDQRMQIVHSITRKPGLLIKISCDMHGTRAVQKIVETAKREEEISIIISALKHGIVHLIKNVNGNHVVQRCLQYLLPYCGKFLFEAAITHCVELATDRHGCCVLQKCLGYSEGEQKQHLVSEIASNALLLSQDPFGNYVLQYVFELQLQWATFEILEQLEGNYTELSMQKCSSNVVEKCLKLADDKHRARIIRELINYGRLDQVMLDPYGNYVIQAALKQSKGNVHALLVDAIKLNISSLRTNPYGKKVLSALSSKK | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence Mass (Da): 68671
Sequence Length: 596
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Cytoplasm
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Q4PSD1 | MDKNFRVNTNDERNIWLSTAVNENLTMASSSSQPQPISSPFHQPENQVNRVNPGSHYYDLETLESSFGGLSFNDSSVGQNGDSIHLPRRTNQVFTGSSSGGAGDDNGYLLPPMGSHHHRELEELQRHNYLNQLRMSYQNDYAHQSYWYNTDGDGNGMLNNGFLNDVPSSSRDRVSDYYTNRFGYEGYNYWRGNEGFDYNQCQASFSAFAKDKEMSERLGMSIFQGTKETVDAIYNGLIGDICELMVDPYGSDVVQLLMRRCSSEQIVQLVDIVTQQMFQFVNICIDSLGTNAIQVLLTCINERAKDQIPRIVDVVRTVALQLSKSNHAIFVILACFRLFPLHCRLLLELIVQNCHQIAIDQHGCCLLQLCFNKDRVPNLEIRQRLIMEAIANALRLCLNCYGNYVVQYIVELNNRYLIDALVRQLIGNYAHLARNKYGSHAVQKLLKLRWIDSRVIVIDLLREIDTLLLDPFGNYVIQTAWFVSKDDVRRMLRYHIERNIPMMRCNKFGNKVLEKLNI | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence Mass (Da): 59449
Sequence Length: 518
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Cytoplasm
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P0DN95 | MSNQNERVAAAPFQEAVESPAQRILWERLRTYDHSFPLSDYSPETLFSSDLQTLEHEFRRFGVSELDRGDQDNYVNGYDALRSFHERSRSASVMGSPYGNLEDVPYLPSNPFFDQTPWSDDAYGYMYGIRNTLLSRAKDGIESHMLQYVIAKGLKETIDKIFDNLISHVCELMLDYYGHKVFRKLMEKCTDEQITRVLDIVLEEPFEFVRLCVHTHGTHAIQGLMRSLCSEEQISRFMETLCYVSLLLTKDVIAHRVILFCFNQFSPSHTRYLLEVIVQNCYQVAIDQNGCCMLKKLIRQSSRELRDPLIKEIISIAVRLCGNCYGNYVVQYLLRLKDYEVTSALSKHLDGNYVQLSYDKYGSHVVQKCLESREFSSRRIIAELLSDIDSLLVDPYGDYVIQTAWIVSEDHVRHVLLFYINRNVPFMRCNVYGRKLLQKLNIWT | Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence Mass (Da): 51705
Sequence Length: 444
Domain: The pumilio repeats mediate the association with RNA by packing together to form a right-handed superhelix that approximates a half donut. The number as well as the specific sequence of the repeats determine the specificity for target mRNAs (By similarity).
Subcellular Location: Cytoplasm
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Q46482 | MKILIVGSGGREHALAWKAAQSPQVEQVFVAPGNGGTASEPGVENVAIAADDIAGLVEFARRESIGLTIVGPEAPLVLGLVDAFAEAGLPCFGPRQASAQLEGSKAFAKDFLHRHGIPTAAYGVFTELEPALAYLRQVGAPVVVKADGLAAGKGVILADDLATAEAAVHDMLGGGRFGRAGARVVIEEFLTGEEASFIAMVDGRHILPLASSQDHKARDDGDRGPNTGGMGAYSPAPIVTPEIHDRIMREVMEPTVAGLAAEGLPYLGFLYAGLMIGADGTPKVLEFNCRLGDPETQPLLMRLQSDLVELCLAALDGRLDQVTADWDARPALGVVMAAGGYPDDYETGHVISGLDAVPSSEAKVFQAGTRCEGDAILTNGGRVLCVTALGANVAEAQHLAYQAVDRIQWTDAFCRRDIGHRAIARERS | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 44805
Sequence Length: 428
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
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O66949 | MKVLVVGNGGREHAIAWKVAQSPLVKELYVAKGNAGIWEIAKRVDISPTDVEKLAEFAKNEGVDFTIVGPEAPLVEGIVDEFEKRGLKIFGPNKEAAKLEGSKAFAKTFMKKYGIPTARYEVFTDFEKAKEYVEKVGAPIVVKADGLAAGKGAVVCETVEKAIETLDRFLNKKIFGKSSERVVIEEFLEGEEASYIVMINGDRYVPLPTSQDHKRLLDEDKGPNTGGMGAYSPTPVINEEVEKRIREEIVERVIKGLKEEGIYYRGFLYAGLMITKEGPKVLEFNVRLGDPEAQPILMRVKNDFLETLLNFYEGKDVHIKEDERYALDVVLASRGYPEKPETGKIIHGLDYLKSMEDVVVFHAGTKKEGNFTVTSGGRVLNVCAYGKTLKEAKERAYEAIRYVCFEGMHYRKDIGDKAFKYLSE | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 47430
Sequence Length: 424
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
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P52420 | MSSLCASNCYPSSSSINLFSNNNNPTKPFLLSLRFASSNSLPFVAPLKFSTTNHVLSNSRFSSNRIQRRLFLLRCVSEESQPSLSIGNGGSEERVNVLVIGGGGREHALCHALKRSPSCDSVLCAPGNAGISSSGDATCVPDLDISDSLAVISFCQKWNVGLVVVGPEVPLVAGLANDLVKAGILTFGPSSQAAALEGSKNFMKNLCHKYNIPTAKYKTFSDASAAKEYIQEQGAPIVIKADGLAAGKGVTVAMELEEAFEAVDSMLVKGVFGSAGCQVVVEEFLEGEEASFFALVDGENAIPLESAQDHKRVGDGDTGPNTGGMGAYSPAPVLTKELQDFVMESIIHPTVKGMAEEGCKFVGVLFAGLMIEKKSGLPKLIEFNVRFGDPECQVLMMRLESDLAKVLLAACKGELSGVSLDWSKDSAMVVVMASNGYPGSYEKGSIIKNLEEAERVAPGVKVFHAGTGLDSEGNVVATGGRVLGVTAKGKDLEEARERAYSAVQQINWPGGFFRHDIGWRALRQKQVATKEE | Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 56473
Sequence Length: 532
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
Subcellular Location: Plastid
EC: 6.3.4.13
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O29108 | MKVLVVDAGGRGNAIAHAFSRSEQVKEIYIAPGNGGSEFFEKCKIAELDGKKIPSIRAIDEIVRFAKKCEVDLAYIGPEEPLSLGLVDRLEEEGIPAVGPKKEATILEASKCWAKDFLKRIGVPIPEYANFDNPEEAKEYIREKFNNGIVVKADGLAAGKGVYVCDSVEEALRAVDEIMVQKKFGEAGNRIVVEERLRGIEVAFTAMTDGKTVKPFGHARDYKRAFDSDDIEGLRDFYIGLTKKFYTKAQIEQLYREGKLINPNTGGMGAVSPHPAVTEEVEQRIMEMVVEPIIENFDKEFKGVLYPVIMLVEENGELIPKVLEINVRDCDPGAEAKLPRLKSDMAEISMAVVEGRLDEVEMRFSSDYCVAVCAVSGALKGREGLKPGYPADHYTSQPITGIEEAMKEAIIYANGIAKTNGYVTTGGRVLTVVGMGQSIEEARSKAYSALEKISFPGMRYRRTIGLDVPE | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 51750
Sequence Length: 470
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
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P12039 | MNVLIIGKGGREHTLAWKAAQSSLVENVFAAPGNDGMAASAQLVNIEESDHAGLVSFAKQNQVGLTIVGPEVPLIEGLVDEFEKAGLHVFGPSKAAAIIEGSKQFAKDLMKKYDIPTAEYETFTSFDEAKAYVQEKGAPIVIKADGLAAGKGVTVAMTEEEAIACLHDFLEDEKFGDASASVVIEEYLSGEEFSLMAFVKGEKVYPMVIAQDHKRAFDGDKGPNTGGMGAYSPVPQISEETVRHAVETIVKPAAKAMVQEGRSFTGVLYAGLMLTENGSKVIEFNARFGDPETQVVLPRMESDLVQVLLDLLDDKEVDLRWKDTAAVSVVLASEGYPESYAKGTPIGSLAAETEQVVVFHAGTKAEGGEFVTNGGRVANVTAFDETFEAARDRVYKAVDEIFKPGLFFRKDIGARALKAAQK | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 45280
Sequence Length: 422
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
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Q8RC54 | MKVLVVGGGGREHAIVHKLSQSDRVEKIYCAPGNAGIGQLAECVNISVEEIEKLKEFALQNKIDITIVGPELPLVEGIVDEFERTGLKIFGPSKKAAMIEGSKYFAKQIMAKYEIPTGRFKAFDRYQEALKFLKETWYPVVIKADGLAQGKGVFIVRDFIEAKEVLDLMMKKRVFGPSGDIVIVEEMLYGKEASIFAFVDGENVLTMMTAMDYKKVYEKDEGPNTGGMGSIAPNPHIDKKTLNEIEEKILKPVVYALKKEGIVYKGVLYAGLMLTKEGPKVLEFNARFGDPETQAILPLLKTDFLEIIEATLEGKLKNLKLEWEDKKAVCVIAASKGYPGEYKKGFEIRGLEEVKEAFVYHAGTSFKDGKIVTSGGRVFGIVALGDSYKEAREIAYREIEKISFEGIYYRKDIAAGY | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 46436
Sequence Length: 417
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
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Q9PN47 | MKIMILGSGAREYSIALALRRVDKNLEFYFAPGNGATESLGTNLNLKDPVVLATYAKEKGFDLCIVGSESFLAEGVVDIFKQQGLAIFGPSKAAAMLETSKSFMKSFLKKYRIKTAKFLNTNDIEKAKNFIYSLTPPIVVKADGLCAGKGVIIAKTHEEAIEETAKMLSGESFGDAGKLVVIEEFLDGYELSIFAVCDGNDFVLLPAAQDHKKLLDNDQGPNTGGMGAYAPSSLANESLLRKVQKDIILPTLAGMKKEGAEFCGVLFIGAMIVGNKPYVLEFNVRFGDPECEVLMPLIEDPLELILAATQRRLRHSKIKIKKEFAVGVVCASENYPYKSSPKSEITVNNIPENSHISYAGVSLEDGKLMADGGRVLVCVGTGKSIEEAQKNAYKLCDNVNFKGKQYRKDIAHQVLK | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 45316
Sequence Length: 416
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
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Q8KBV8 | MKVLIIGSGAREHAMAWAVARSSKVSTVFVAPGNGGTATMGGKVRNTPVKATDIDALLELVAKESIGLTVVGPEQPLEAGIVNRFREAGFKVVGPTAEAAQLETSKVFAKEFMKRHGIPTAGYEVFRDYASAKAFLETCPTFPQVIKASGLCAGKGVVVAMSRDEALEAIHEFFESRIFGDAADEVVIEAFLSGQEASVFALTDGQNYQLFLSAQDHKRIGEGDTGKNTGGMGAYAPAPLVTPEVMRRVEEEVIRPTLAGMRADGYAYTGFLYVGLMIDKGVPSVVEYNARLGDPETQVVLPMLKSDLFDALLASVEGGLEVVPFEMQEGAAATVVMASAGYPDAYETGKVITIDPTVNDMEGVLVFHAGTRRDGDALVTSGGRVLSVTACAGSLKEALDRVYRAVDAIEFEGAYCRRDIGAKAL | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 45064
Sequence Length: 425
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
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Q97J90 | MKILLIGSGGREHAMAWKMAQNKSVERIYCAPGNGGTAKENKCENVNLEKTEELIEFASKNNIDLTVVGPEAPLVDGIVNEFKEKGLKIFGPGKVGAQLEGSKSFSKDFMKKYNVKTAEYAVFENSEESLEYLKKCTYPIVIKADGLAAGKGVVICEDYKLAEETIKAFMVKDVFKGSGKKVVIEEYLEGVEASILSITDGKAIIPFVSSKDHKQIFDGNKGPNTGGMGAISPNPYCTEEVLKSFEEEILKPTLIGIQEERMDFTGIIFFGLMITKKGVYLLEYNVRLGDPETQVVLYLMKSDFVDLINAAMDKKLSDFDIEWYDGNACCVVAASKGYPKNYSTGYEISGIDDAGDKVFCAGVKLENGVYKTSGGRVLCASARGITLDEAIKKAYTDIERIKFDGIYYRKDIGKSK | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 45754
Sequence Length: 416
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
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Q8NMH3 | MRILVIGSGAREHALLRGLSTDPATTELHVAPGNAGLGSIATVHPGIKADDPEAVTALAKELNSDLVVIGPEIPLVAGVADALRAAGIAVFGPNKDAARIEGSKAFAKDVMAAQGVRTAHAEAITPGASSEDIDAAIDRFGPTWVVKDDGLAAGKGVVVTPDRAAARAHVDAVLEGGNPVLLESFLDGPEVSLFCLVDGETVVPLLPAQDHKRAYDNDEGPNTGGMGAYAPLPWLPEDGVQRIVDEVCVPVAREMVARGCAYSGLLYAGIAWGAEGPAVVEFNCRFGDPETQAVLALLKTPLAVLLNAVATGTLAEQPALEWEDAYALTVVLASYNYPEAPRTGDVIRNADADNVLHAGTALNAEGELVSAGGRVLNVIGVGETLEAARDNAYTTIKDIELEGSHYRSDIALAALEGRISI | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 43545
Sequence Length: 421
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2.
EC: 6.3.4.13
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O27272 | MVTYSESGVDIDLEELTVSSLTSRLSDTLKYCDVITGAGHFAALVRMGDVAIAMSTDGVGSKILVAEMMNRYDTVGIDCIAMVVNDILCVGARPAALVDYLAVERPDPEVAGEIGKGLAMGAEMARVAIIGGETASLPGIIRNLDLAATGIGFVDVDRIITGEDVSPGDTVIGLESSGIHSNGLSLARRVFFDELELSPEDEMPGSSSSVGDELLRPTRIYVEPIMELIESDVDVHGLAHITGGGFGNLKRLRKDVGYRLDSLPEPQQIFRVIHEAGVDIREMYRVFNMGVGFCAVVAPDDVDEALSILGDRAHPIGEVTDRGSEVELEACTGETIKL | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 35983
Sequence Length: 338
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.1
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Q1D8V5 | MGTTYKQSGVDIEAGDAFVERIKPHAARTMRPEVMGGVGGFGGLFALPPGKYQQPVLVAGTDGVGTKLKVAFAAGRHGTVGIDLVAMSVNDILTCGAEPLFFLDYFATGRLEVDDAAEVVKGIALGCEQAGCALLGGETAEMPGFYARGEYDLAGFCVGVVERAAIIDGKSVKPGDALIGLPSSGLHSNGYSLARKVLLDDGKLALDATPEGLDRPLVDALLEPTRIYVKDVLALLQAVKVKGLAHITGSGIPGNLPRCLPDGTRAVLSEQTWPKPPIFDLIAKLGSVARDEMFNTFNMGLGLILVVAKEDVAQALSVLSGRGVQAFEVGRVEAGQGEATAVIDP | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 35858
Sequence Length: 345
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.1
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Q9JZ80 | MSTSLSYRDAGVDIDAGDQLVENIKPFAKRTMRPEVLGDLGGFGALVEIGKKYQNPVLVSGTDGVGTKLKLAFDWDKHDTVGIDLVAMSVNDILVQGAEPLFFLDYFACGKLDVPRATDVIKGIAQGCEESGCALIGGETAEMPGMYPVGEYDLAGFAVGVVEKENVITGRSIGVGDVVLGLASNGAHSNGYSLIRKIIERDNPDLDAEFDNGKTLREAVIAPTRLYVKPILAALEKFTIKGMAHITGGGITENVPRVLPENTVAQIDAKSWELPKLFQWLQKAGNVETQEMYRTFNCGIGMVVIVAAEDADAVQGLLGEQGETVYRLGLIRERQGDEHQTQVA | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 36974
Sequence Length: 344
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.1
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A1JKZ7 | MTNKTSLSYKDAGVDIDAGNDLVDRIKGVVKQTRRPEVMGGLGGFGALCALPQKYREPILVSGTDGVGTKLRLAMDLKRHDTIGIDLVAMCVNDLVVQGAEPLFFLDYFATGKLDVDTAASVITGIAEGCKQSGCALVGGETAEMPGMYHGEDYDVAGFCVGVVEKSEIIDGSKVAPGDALVALGASGPHSNGYSLVRKILEVSNTDPEQTQLDGKSLADHLLEPTKIYVKSILSLIEQLDIHAIAHLTGGGFWENIPRVLPQGTQAVIDEASWQWPAVFSWLQETGNVSRHEMYRTFNCGVGMVVALPAELADKAVELLTASGEKAWKIGVIAAAAEGAEQVIINP | Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Mass (Da): 36823
Sequence Length: 347
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Subcellular Location: Cytoplasm
EC: 6.3.3.1
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Q5WW20 | MPFCLTETSLPFGKKYKGKVRDTYDLGDQLILVTTDRQSAFDRCLAAVPYKGQVLNLTSVWWFKNTQSIVPNHLIAVPDPNVAIAKKCKIFPVEFVVRGYISGSTSTSLWTQYQKGVREYCGITFPDGLRKNQKLESPVITPTTKETIHDRPISPHEIVAEGWMTQEDWDETSSYALRLFQHGMEVAQQHGLILVDTKYEFGRDAEGRIVLVDEIHTPDSSRYWLFNGYQERFDAGKEPENIDKEFLRLWFVDHCDPYKDEVLPQAPQELIVTLASRYIQLYEMITGESFVYDSNPGPVNDRILHNIQHWLG | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 35911
Sequence Length: 312
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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Q72UH8 | MNPSYKGKVRDIYDLGDKLILSSSDRISAFDVVFPQLVPDKGKVLNRISVSWFEFFKDVPNHILETDVKYFPIPFQNHPDLEGRSVLVKKCKRIDYECVVRGYISGSGWKEYKNDGTLAGIKLPSGFKESQKLPEPVFTPAVKNDQGHDENISEKEMENRIGKELFNILKEKSISIFLRASEVVDKAGIILCDTKFEFGILDGQVILIDELLTPDSSRYWSTDTYSVGISPPSLDKQILRNYLETTSWNKMPPAPNLPAELIQELREKYQKIEDLILSCTSQKSK | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 32472
Sequence Length: 285
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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B2GF71 | MEEKLLYAGKAKEMWTTEDEDQLRVVYLDQATQLNGKQKEHFAGKGAAAHAISDLVFHYLIDHGIETHFIKKLSATEDLVEKCAMVPLEFVTRNTVAGHFASRFGLEEGTALPQPVEENFYKDDELDDPFINESAAVALKMVTPAEFDRCWAICRQVDQLLTPLFEKAGMQLVDFKLEFGRRSRDNQIILADEFSPDNCRLWDTTTHHHLDKDVFRRNLADLTATYQEVYARLQAALKED | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 27483
Sequence Length: 240
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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Q8Y6B9 | MTNELVYEGKAKRLFKTEEAGVLRVAYKDDATALNGVRKESFAGKGELNNQITSLIFSHLAEAGIESHFIRAISETEQLVKEVSIIPLEVVVRNVMAGSLAKRLGKEEGEQIPNAIVEFYYKDDALDDPFINDDHVLYLEVATTSEMDTIRQAARSINKVLQELFNQMNITLIDFKLEFGRDAAGEILLADEISPDTCRLWDKETNQKLDKDVFRRNIGNLTDVYTEVLNRLKQVQN | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 26841
Sequence Length: 237
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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Q9A1Z3 | MTNQLIYKGKAKDIYSTKDENVIRTVYKDQATMLNGARKETIDGKGALNNQISSLIFEKLNKAGVVTHYIEQISKNEQLNKKVDIIPLEVVLRNVTAGSFSKRFGVEEGHVLETPIVEFYYKNDDLDDPFINDEHVKFLGIVNDEEIAYLKGETRRINELLKGWFAQIGLNLIDFKLEFGFDQEGTIILADEFSPDNCRLWDKNGNHMDKDVFRRDLGNLTDVYQVVLEKLIAL | Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 26837
Sequence Length: 234
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
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P31335 | MAARQQLALLSVSEKAGLVEFARSLNALGLGLIASGGTATALRDAGLPVRDVSDLTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMNKQDFSLVRVVVCNLYPFVKTVSSPGVTVPEAVEKIDIGGVALLRAAAKNHARVTVVCDPADYSSVAKEMAASKDKDTSVETRRHLALKAFTHTAQYDAAISDYFRKEYSKGVSQLPLRYGMNPHQSPAQLYTTRPKLPLTVVNGSPGFINLCDALNAWQLVKELKQALGIPAAASFKHVSPAGAAVGIPLSEEEAQVCMVHDLHKTLTPLASAYARSRGADRMSSFGDFIALSDICDVPTAKIISREVSDGVVAPGYEEEALKILSKKKNGGYCVLQMDPNYEPDDNEIRTLYGLQLMQKRNNAVIDRSLFKNIVTKNKTLPESAVRDLIVASIAVKYTQSNSVCYAKDGQVIGIGAGQQSRIHCTRLAGDKANSWWLRHHPRVLSMKFKAGVKRAEVSNAIDQYVTGTIGEDEDLVKWQAMFEEVPAQLTEAEKKQWIAKLTAVSLSSDAFFPFRDNVDRAKRIGVQFIVAPSGSAADEVVIEACNELGITLIHTNLRLFHH | Function: Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis . Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR) . Can use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor in this reaction. Also catalyzes the cyclization of FAICAR to IMP. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (By similarity).
Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 64415
Sequence Length: 593
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
Subcellular Location: Cytoplasm
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A9WEK8 | MIGEERVVRALMSVYDKTGIVEFAQALHNLGIEIISTGQTQRVLREAGIPALPVSDVTGFPEILDGRVKTLHPAIHAGLLARRDVPAHMAELAAHNLQPIDLVVVNLYPFAATIARPDVTMAEAQEQIDIGGVALLRAAAKNFPAVLVLVDPADYAGVLDGLRAGDVPLSERQRLAAKAFAHTAEYDATIAAYLRTEPLPDVLPLAWRKYQPLRYGENPHQAAALYGDFGAFFHQLHGKELSYNNILDTAAAQELIEEFPATEAAAVAIIKHTNPCGVAIAADLHRAWEAAFATDREAPFGGIIAVNRPVDIAFAEAVDEIFSEIIIAPDFAPDALALLRRKKNRRLLQSVRPITGADRWQLRSVPGGVLVQEPDHAPLVAEEWRVVTKRAPTDAEAAALRFAWRVVKHVKSNAIVYAAHDRTLGIGAGQMSRVDSSRLAVWKAQQAGIDLRGSVVASDALFPFADGVEAAIAAGATAIIQPGGSVRDEEVIAAADAAGAAMVFTGRRHFRH | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 55050
Sequence Length: 512
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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B3QS62 | MAERKIKRALISVSDKTGIIDFAKSLAEFGVEIFSTGGTLKKLIEAGIAAKSISEITKFPEIMDGRVKTLHPAIHGGLLAVRGNSDHEKQAAENNINFIDLVAVNLYPFEATVAKPDVTFADAIENIDIGGPSMLRSAAKNHKSVTVITDAADYQCVLEEMRANDGATTEATRLYLAKKVFALTARYDGAISNYLEKISQTDESVLPNHLSVSLTKEIDMRYGENPHQKAGFYAMKVGEQNLSFDEFFEKLHGKSLSYNNLLDISAAAGLIEEFRGAEPTVAIFKHTNPCGVAQADSLETAYRKAFSTDTQAPFGGIIAVNRPLDMATAKAINEIFTEIVIAPEFEEGVLEYLMKKKDRRLIRQLKALPSSALEFRSTVCGLLVQDKDAKTATKEELKVVTKRQPTEAELEDLLFAWKICKHVKSNTIVYAKDMQTVGVGAGQMSRVDSSRIARWKAGEVNLELKNSVVASDAFFPFADGLIAAAEAGASAVIQPGGSIRDEEVIAAADERNIAMVFTGTRHFRH | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 57327
Sequence Length: 525
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q8KFK6 | MLDPVIKRALVSVSDKTGIVDFCRELASMDVEIFSTGGTLKLLQGAGIVAQSISTITGFPEIMDGRVKTLHPKIHGGLLAVRDNAEHQKAARENGIQFIDLVVVNLYPFEATIAKADVTFEEAIENIDIGGPSMLRSAAKNNESVTVVTDVADYATVLDEMRSNGGATTRATRLTLAAKVYALTSRYDTAIAAYMAKAAGVKGAGDTMTLKLEKELSMRYGENPHQSAGLYKMDDGNGVRSFSAIFEKLHGKELSYNNMLDIAAATGIIEEFRGEEPSVVIVKHTNPCGVAQAPTLCEAYRKAFSTDTQAPFGGIIAFNRPLDMETASAVNEIFTEILIAPAFEDGVLEMLMKKKDRRLVLQKQPLPKAGWEFKSTPFGMLVQERDSKTVAPEELKVVTKRQPTAEELADLMFAWKIVRHIKSNTILYVKNRQTFGVGAGQMSRVDSSKIARWKASEVALDLRGSVVASDAFFPFADGLLAAAEAGVTAVIQPGGSIRDNEVIEAADANNLAMVFTGMRHFKH | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 56743
Sequence Length: 523
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q97J91 | MIKRALISVFNKNGILKLAKFLNEKGVEILSTGGTYKHLKENGIPVIEVSEVTGFDEILDGRVKTLHPKIHGGILAIRDNKEHMDTIKNKGITPIDMVVVNLYPFFDKVKENISFEEKVEFIDIGGPTMIRAAAKNFQDVVVLTDVNDYDDVIDQIEKTGEVAYNTKKRLAGKVFNLMSAYDGAISRFLLEDEYPEYLAVPYKKKMDLRYGENPHQTAAFYEAAFGDGAMKGFEQLNGKELSYNNIKDMDIAWKVVNEFDETVCCALKHNSPCGVAIGENPLDAYKKAFECDDTSIFGGIVALNKVIDKPAAEEMVKIFLEIVIAPDFTADALEVLKSKKNLRVIKANEKPSDNFELAKVDGAMLVQSADNKLTEKMEVVTDKKPTDEEMRDMIFGMKVVKYVKSNAIVVVKNGAAVGIGGGQVNRIWPAKDAMERGKGAAVLASDAFFPFGDIVEEAHKNGIKAIIQPGGSIRDQESIDGCNKYGISMVMTGIRHFKH | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 55238
Sequence Length: 499
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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Q7UKJ8 | MSDVVPVRNALISVSDKMGLADFAAGLSAAGVTIYSTGGTRAHLEQSGIKVEDVAEYTGFPEMLDGRVKTLHPRIFAGILARRDLDDHMDTIADHDIEPFDLVVVNLYPFAATVSRSGATRAECIEQIDIGGPSLVRAAAKNHGDVAIATSPEQYGDVLDQLETLGGTTDELRTQLAAEAFDHTAGYDRAIADYMQGDAVGGEFPASMHVSLRRKTQLRYGENPHQRAALYSDSSDRSANLVSARQISGKELSYNNLLDLDAALDIARGFAEPAVSVIKHNNPCGAATGDTLSEAVDKAMAGDPLSAFGSVIGMNRTLDEATAEFLCQPGLFIEAIVAPDFEAGAVGLLTTKPRWKDNVRLMQVGRLDEPARKVSRRFISGGMLVQDADRMVSSPLQWNTVTETPVDDDLWDDISFGWEMVRHVKSNAIVLAKDTSLIGVGAGQMSRVDSVEISIKKAAERSEGSILASDAFFPFPDSIEAAAKAGVLAIIQPGGSRRDDEVIAACDEHEIAMVFTGRRHFKH | Catalytic Activity: (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Sequence Mass (Da): 56202
Sequence Length: 523
Domain: The IMP cyclohydrolase activity resides in the N-terminal region.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.
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O67321 | MEKLIILGAQWGDEGKGKIVDLLSEHFDITVRYQGGSNAGHTVVVNSQKFILHLLPTGILHEHVKGVIAQGMVVDLEVLHKEVKNLEEKGIYVKERLFISDRAHLVMPYHKLLDSLFEKKKGIGTTLRGIGPAYMFKYGRKGIRISDLKDEKRFYTLLEDNLDFVKNICEKVFCEKFDLDINQIYEEQLRYFEEFKENVVDLLRFFNTQKGSVLFEGAQGTLLDVDMGTYPYVTSSNASALGLSNGTGMPPKYFSDAFFLGVAKAYTTRVGEGPFPTELKGEEGEKLRELGGEYGSTTGRPRRCGWLDLVALKYAVQVNGLDGFVITKLDVLDTFDEVKVCVAYELDGEVIDYFPASYSELIRVKPVYKTLKGWKKSTKGAKDVSELPKEALDYVKFIEEYTGVPVVMLSTGPKRDEYIWLKEILRTRSGYS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 48854
Sequence Length: 432
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q96529 | MSLSSLTLDSNPRFAVGGPYHRRYPPLHHPRSFVSCSAKRPAVSASLSVAADSAATESLGRIGSLSQVSGVLGCQWGDEGKGKLVDILAQHFDIVARCQGGANAGHTIYNSEGKKFALHLVPSGILNEDTTCVIGNGVVVHLPGLFKEIDGLESNGVSCKGRILVSDRAHLLFDFHQEVDGLRESELAKSFIGTTKRGIGPAYSSKVIRNGIRVGDLRHMDTLPQKLDLLLSDAAARFQGFKYTPEMLREEVEAYKRYADRLEPYITDTVHFINDSISQKKKVLVEGGQATMLDIDFGTYPFVTSSSPSAGGICTGLGIAPSVVGDLIGVVKAYTTRVGSGPFPTENLGTGGDLLRLAGQEFGTTTGRPRRCGWLDIVALKFSCQINGFASLNLTKLDVLSDLNEIQLGVAYKRSDGTPVKSFPGDLRLLEELHVEYEVLPGWKSDISSVRNYSDLPKAAQQYVERIEELVGVPIHYIGIGPGRDALIYK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 52964
Sequence Length: 490
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Plastid
EC: 6.3.4.4
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B6YR45 | MKVSVLLGLQWGDEGKGKVVDVLTPKYDIVARFQGGPNAGHTLLFADRKYVLCSIPSGVFQGKVNIIGNGVVLDPILFKAETETLTSSCSNLVDKIYISRKAHLILPTHRLLDVAYETQKGNNKIGTTGKGIGPAYTDKVSRNGLRIGDIDYNFEEKYRYAIARHKELLHQMNFQYDLLPLEREWKKSIEVIKRFKRINSDNFINKALIGGRTVLAEGAQGTMLDVDFGSYPFVTSSNTICASACTGLGVAPAKIGDVFGIFKAYCTRVGSGPFPTELSDEIGEKLRNIGNEYGSITKRPRRCGWIDLVALRYAVMINGVTQLIMMKSDVLDTFDTVKACIAYEVNGQKMEDFPFEIGSSVKPIYTELVGWKTNMTKIKSENEFPKAFKDYLLFLEESLGVSIKIVSLGPDREQTIIRE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 46614
Sequence Length: 419
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q83CV4 | MNIVILGTQWGDEGKGKIVDMLTEDVAAVVRFQGGHNAGHTLIIDGEKTILRLIPSGILREGVLCLIGNGVVLSPPALMEEIEELNAKGIPVTEQLRISSACNLLLPYHVALDKAREAELGTKAIGTTGRGIGPAYEDKVARRGIRAMDLLHPDQLLEKIKKATAYHNIQLEHYYHQTPLDYQSIYNQLMEFREKIKPMIGDVSALLGNLRRQNKHIIFEGAQGSLLDIDLGTYPYVTSSNTTAGSAATGSGFGPLYFDRVLGITKAYVTRVGAGPFPTELTNEEGKKMAKRGNEFGSVTGRPRRCGWFDVISMRRTIQINSLTGIVLTKLDVLDEFAKIHLCTAYRCDGEVVNEPPFDQSLLESCEPVYEEMPGWQTSTYGLTDYSEMPKEARNYISRLEELLGVPITIISTGPDRKHTIVRQAVFNQVITAKG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 47989
Sequence Length: 435
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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P0CQ34 | MAPSPEGVTVVLGAQWGDEGKGKLVDILAAEADICARCAGGNNAGHTIVVRNDKGEKTSYAFNLLPSGLINPECTAFIGSGVVVHVPSLFNELDTLERKGLKVAGRLFVSDRAHLVMGFHQIVDGLKEVELGGSSIGTTRKGIGPAYSSKASRSGLRVHHLFDPTFPAKFRKLVEGRFKRYGHFEFDTEGEIEMYLAFAERLRPFIVDGPTFMHNAVNSGKRVLVEGANALMLDLDYGTYPFVTSSSTSIGGVVSGLGISPFAIKRVVGVIKAYTTRVGGGPFPTEDLATVGETLQEVGAEYGTVTGRRRRCGWLDLVVMKYSTMINGYTSLNLTKLDVLDGFDEIKVATGYKIDGVEVEGFPADLDRLAKVEVQYATLPGWKTDISNCKTYEEFPENAKAYIKFIEDYLGVKVQYVGVGPGRDQNVIIF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 46643
Sequence Length: 430
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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B0W9B4 | MEEPSKVSAPTAVNGHPVVQSHAEMHQRCLNPYRSKVTVVLGAQWGDEGKGKVVDMLATEADIVCRCQGGNNAGHTVVVNGVDFDFHLLPSGIINERCKSIIGNGVVIHLPGLFEELAKNEAKGLTNWESRLIISNRAHLVFDLHQQVDGLQEAEKGGKSLGTTKKGIGPCYSSKATRNGIRVSDLLGDFKVFGEKFESLVNMYKRLFPNFEVDIAAELARYRDYADRLRPLVQDTVSFLHGSLREGKSVLVEGANAAMLDIDFGTYPYVTSSNCSIGGVLTGLGLPPQTIGEVIGVVKAYTTRVGDGPFPTELHDEVGSLLQTRGGEIGVTTKRVRRCGWLDLALLRYTAMVNGYTALCVTKLDILDTLKEIKVAVSYNLNGERINYFPGSITALGQVEVNYITVPGWLTSTEGVREFSELPPQAQDYIRLIENDLGVPVKWIGVGKGRESIINVKD | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 49945
Sequence Length: 458
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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A5FQS4 | MPVTAIVGGQWGDEGKGKVVDMLAQEADYVVRFSGGDNAGHTVINPMGEFKLHIIPSGVFYPGVKCIIGNGVVINPDVFIRERNELISRGVNVSNVFISDRAHLVLPYHILLDGLEEEARGNKSLGTTRRGIGPAFVDKYARMGIRVGDLLLPEYLRERLEYVLECKNQILTKVYDAAPISLDEIYETCLKWGKELAPNIRETTHIIEEAISQDKKIIMEGAQGALLDPDFGTYPYGTSSSPLAAGGCLGIGIGPASVSATLGVFKAYSTRVGGGPMPTELLDKTGDTIRNEAHEYGTTTGRPRRIGWFDAVAGRFSCQINGMTTAIMTRLDIMDILPKISICTAYELNGKIIKYFPANSGELAKCKPIYEEMPGWLCSTKEVRNYDDLPEAAKAYICRIEKLIGCQMSAVCIGPSREQTIYK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 46283
Sequence Length: 423
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q9RYB5 | MPGIAIVGAQWGDEGKGKIVDFLAPEAEYVVRYQGGANAGHTVNAKGKTFKLNLLPSGVLHEGATSILGDGMVIDPEKFIEERRNLMEGGLNPRLKISDRAHIVLPHHKYVDGRKDFVGTTGKGIGPAYADRARRVGIRFGDLLDEGVLRERIERLLEAKPNSTRDAGWATVEDGLKSLAPIREQLAPFIADTGSELRQAIKDGRKVLFEGAQATLLDLNYGTYPFVTSSHPTVGGILVGTGVNHKALHRVYGVAKAFNTRVGHGPFATEVHDEAGILRLRGDGSQPWDEYGTTTGRPRRVGWLDLELLKYAVDVNGLDGLVINKMDILGGLDEIPVCTGYDEGGQPVFKKMKGWSSTDGVTSRATLPKEAQAYLDLIEDTVQCPVVIFSAGPEREKTYGEVHWG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 43974
Sequence Length: 405
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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A5UN95 | MTCSILVGGAWGDEGKGKCITYLCGNDKPDIIARAGVGPNAGHSVEFNGEKYGLRLIPSGFVHTDAKLMIGAGVLVDKDVLFKEFEDLKKYNVKERTFVDPRCAIITKDHRERDKKSEHLAKKIGSTGSGCGPANSDRVLRTVKLANDVPELEDYLADVSLETNDVLDNGGDVFIEGSQGFALSLYYGTYPFVTSKDTTASTFAADVGVGPTKVDEVINVFKAYITRVGEGPFPTEISQEEAESKNIEEYGVVTGRRRRVGLFDMELAKESCRINGATQIALTCVDRLYPDCARTQSYDDLSAETKKFVEEIQSETGVPVTIISTGPDLKDTIDLRKELL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 37115
Sequence Length: 340
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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B6JUV1 | MALVSETGVDVSTDGITVVLGSQWGDEGKGKLVDILCDNVDICARCAGGNNAGHTIVANGQTYDFHILPSGLVNPKSVNLIGSGVVVYLPAFFHELENLVKKGLDCTNRIFISDRAQLVFDYHQRADALNEAELGGKSIGTTGKGIGPAYSTKATRSGIRVHHLYNWPEFESRYRKNVRDLQKRYGAFEYDVEGELVRYKELAAKLQPYVVDSIAFIHTGLKEKKRILVEGANALMLDLDFGTYPYVTSSNTTIGGVCTGLGVPPRAIANVIGVVKAYTTRVGAGPFPTEQLNEIGDHLQKVGREFGVTTGRKRRCGWLDLVVLKYSTLINGYDSLNLTKLDILDDFKEIKVAVAYIVDGKRIETFPADLDSLESAEIIYETFPGWQTKTTGITRWEDMPENAKKYIEFIEKFLGVPIKYIGVGPGRDEVLVKH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 47819
Sequence Length: 434
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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C4QCD2 | MTKSVEGLVSVVLGAQWGDEGKGKLVDLLSESCSVVCRCQGGNNAGHTVVAGGQEYFFHLLPSGIVNPNVLAVIGNGVVVNLQALFQEIDEAVCKGLLDVSSRLRISDRCHLVFDIHQEIDRMEEELRGENSLGTTKKGIGPTYSSKVTRNGLRVCDLMGDWVQFTAKYKELVKYVKRRYPKLGINVEESLEKLSGMVCDSVILINKLVKSKQANILVEGAQSCMLDIDFGTYPHVTSSNCSVGGVCTGLGLSPSRVGRVYGVIKAYTTRVGSGPFPSELLDGIGEFIQKKGCEWGVTTKRKRRIGWLDTVVIRYAHIINDFNALALTKIDVLDDLEEVKIAKAYIDPETGRELDSFPSDSSVLNHVVVVYETLPGWKTSTHGCRVYEELPTAAKVFVETVEKLLNIPIRWIGTGASRDSIIIRSV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 46669
Sequence Length: 426
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q02787 | MASVRETGVNVSNDGITVVLGSQWGDEGKGKLVDILCDNVDVCARCQGGNNAGHTIVANGVTYDFHILPSGLVNPKCQNLIGSGVVVYLPAFFSELEKLEQKGLKCRDRIFISDRAHLVFDYHQRADALNEAELGKQSIGTTGKGIGPAYSTKATRSGIRVHHLYHWAEFEARYRKNVADLQKRYGAFEYDVEAELIRYKELAQRLKPFVIDAVAFMYEALQSKKRILVEGANALMLDLDFGTYPFVTSSNTTVGGVCTGLGVPPQRIANSIGVVKAYTTRVGAGPFPTEQLNEIGDHLQSVGREVGVTTGRKRRCGWLDLVVVKYSTMINGYTSLNLTKLDILDALDEIKVAVAYIINGKRIETFPADLDSLEEAEIVYETFPGWKVPTTGITHWDQMPENAKKYIEFIEKFVGVPITFIGVGPGRDEMLVKE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Mass (Da): 47877
Sequence Length: 434
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.4.4
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Q55498 | MTSPSPLVGIIMGSDSDLPTMAAAIAVCEEFAVPTEVAIISAHRTPERMVEYAQTAHQRGLRIIIAGAGGAAHLPGMVAALTPLPVIGVPVQTKTLQGVDSLYSIVQMPGGIPVATVAIGNAKNAGLLAVQILASHNPVLLEKVQQYRQSLETMVLDKQAELERLGYRAYLDQQNQ | Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Sequence Mass (Da): 18604
Sequence Length: 176
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
EC: 5.4.99.18
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Q9WYS7 | MPRVGIIMGSDSDLPVMKQAAEILEEFGIDYEITIVSAHRTPDRMFEYAKNAEERGIEVIIAGAGGAAHLPGMVASITHLPVIGVPVKTSTLNGLDSLFSIVQMPGGVPVATVAINNAKNAGILAASILGIKYPEIARKVKEYKERMKREVLEKAQRLEQIGYKEYLNQKE | Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Catalytic Activity: 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Sequence Mass (Da): 18618
Sequence Length: 171
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
EC: 5.4.99.18
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Q73PV9 | MRPLVIILMGSSSDMGHAEKIASELKTFGIEYAIRIGSAHKTAEHVVSMLKEYEALDRPKLYITIAGRSNALSGFVDGFVKGATIACPPPSDSFAGADIYSSLRMPSGISPALVLEPKNAALLAARIFSLYDKEIADSVKSYMESNAQKIIEDDSKLKR | Function: Catalyzes the reversible conversion of 5-aminoimidazole ribonucleotide (AIR) and CO(2) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR). Does not accept N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) as a substrate.
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + H(+) = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CO2
Sequence Mass (Da): 17196
Sequence Length: 159
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.
EC: 4.1.1.21
|
O66608 | MLTVGILGGGQLGWMTILEGRKLGFKFHVLEDKENAPACRVADRCFRTGQISEFVDSCDIITYEFEHIKDEVLEKCESKLIPNPQALYVKKSRIREKLFLKKHGFPVPEFLVIKRDEIIDALKSFKLPVVIKAEKLGYDGKGQYRIKKLEDANQVVKNHDKEESFIIEEFVKFEAEISCIGVRDREGKTYFYPQPFNKHEEGILIYNYVPYAKLKEAEEITKRLMELLDIVGVFTVEFFLLKDGRVLINEFAPRVHNTGHWTLDGAYTSQFENLLRAITEMPLGSTELKLPSGMVNILGKSYEEIPLKEILSVEGAKLYWYGKEKKPRRKVGHVNVVGRSKEEVVEKVERVFTLLKGSREKLPAP | Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 41988
Sequence Length: 365
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
EC: 6.3.4.18
|
P12045 | MSKQIIYPGAVIGIIGGGQLGKMMAVSAKQMGYKVAVVDPVKDSPCGQVADVEITAHYNDREAIRKLAEISDIITYEFENIDYDALHWLKDHAYLPQGSELLLITQNRETEKKAIQSAGCEVAPYSIVKTKNELKQAVQELRLPAVLKTCRGGYDGKGQFVIKEEAQMEQAAALLEHGTCILESWVSFKMELSVIVVRSVNGEISTFPTAENIHHNNILFQSIVPARVEKGIQQKAADLAVKLADELNLVGPLAVEMFLTEDGELLVNELAPRPHNSGHYTLDLCETSQFEQHIRAVCGLPLGKTDLLKPGMMVNLLGDEVKLVEEDPELLKEAKLYIYGKHEIKKGRKMGHITFMKQPEDEWIQEITNKWMNRDGGQAE | Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 42320
Sequence Length: 380
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
EC: 6.3.4.18
|
P52559 | MDKTSLKPGSTIGIIGGGQLGRMLAMAAARFGYETIILEPQAGCPAAQVANRQIVAAYDDPKALAELAAASDVITYEFENVPVSAADKLAETALVLPPPAALEISQDRFTEKQFLNESGIETAPWRLVDDEETLIAALGALGGRGILKIRRLGYDGKGQVRLASLDETQACNAFAAINKAPAILEGFVEFEREVSVIAARDRSGNVAIFDLAENVHKDGILATSTVPAAISVQTAEAARTAAEKLLHALDYVGVLGLEFFVLKDGTLLANEFAPRVHNSGHWTEAACAISQFEQHIRAVAGLPLGNTDRHSDCVMENLIGDDIEKVPAILCEKNAVLHLYGKKEARAGRKIGHVTRIKPRTI | Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 38682
Sequence Length: 362
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
EC: 6.3.4.18
|
Q44678 | MKRVSEQAGNPDGNPQAHVPGMPVIAVIGDGQLARMMQTAAIELGQSLRLLAGARDASAAQVCADVVLGDYTNYDDLLKAVDGATAVTFDHEHVPNEHLTALIDAGYNDQPQPAALINAQDKLVMRERLAELGAPVPRFAPIESAQDAYDFWTLTSGQVCLKARRGGYDGKGVWFPNNESELTALVSDLSRRGVALMAEEKVGWSRELSVLVARTPSGEVATWPLTESVQRNGVCAEAVAPAPGVDPQLQQRAETLGEKIATELGVTGVLAVELFAFANESGAEDIAVNELAMRPHNTGHWTLVGSVTSQFEQHLRAVMDEPLGDTSTLAPVTVMANVLGADEDQRCQWASVPRSGAPVPATKVHLYGKGIAQGRKIGHVNLTGEDEEATRRDARLAADFLVNAAWSDNWSAK | Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 44111
Sequence Length: 413
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
EC: 6.3.4.18
|
P09029 | MKQVCVLGNGQLGRMLRQAGEPLGIAVWPVGLDAEPAAVPFQQSVITAEIERWPETALTRELARHPAFVNRDVFPIIADRLTQKQLFDKLHLPTAPWQLLAERSEWPAVFDRLGELAIVKRRTGGYDGRGQWRLRANETEQLPAECYGECIVEQGINFSGEVSLVGARGFDGSTVFYPLTHNLHQDGILRTSVAFPQANAQQQAQAEEMLSAIMQELGYVGVMAMECFVTPQGLLINELAPRVHNSGHWTQNGASISQFELHLRAITDLPLPQPVVNNPSVMINLIGSDVNYDWLKLPLVHLHWYDKEVRPGRKVGHLNLTDSDTSRLTATLEALIPLLPPEYASGVIWAQSKFG | Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 39461
Sequence Length: 355
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
EC: 6.3.4.18
|
P43850 | MQNSTLYPTVYVLGNGQLGRMLRYAGAPLDIYVEPLAFNAPVFDLPENAIITAEIERWEKTPLTELLGNHKNFVNQHIFGLLADRFTQKSLLDELNLSTSPWCLLKDKNQWNDLFQTVGEKVVVKRRTGGYDGRGQWIIRDENRADITDDLFGEVIAEKFIPFDYEVSIVGARFKNGEKRFYPVTHNLQQNGILRYSVVDCAFPQQSVQQKQAETMLGKIMDKLGYVGVMAMECFVVGDKLLINELAPRVHNSGHWTQLGCSISQFELHLRALLNLPTPELQTFAPSVMINLIGTNHNPKWLNIPFAQLHWYGKEVRIGRKVGHINLSHPNKAVIIQQLEKLCTELPEDYQSGLNWAIEKLK | Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 41273
Sequence Length: 362
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
EC: 6.3.4.18
|
P65899 | MMAVASSRTPAVTSFIAPLVAMVGGGQLARMTHQAAIALGQNLRVLVTSADDPAAQVTPNVVIGSHTDLAALRRVAAGADVLTFDHEHVPNELLEKLVADGVNVAPSPQALVHAQDKLVMRQRLAAAGVAVPRYAGIKDPDEIDVFAARVDAPIVVKAVRGGYDGRGVRMARDVADARDFARECLADGVAVLVEERVDLRRELSALVARSPFGQGAAWPVVQTVQRDGTCVLVIAPAPALPDDLATAAQRLALQLADELGVVGVLAVELFETTDGALLVNELAMRPHNSGHWTIDGARTSQFEQHLRAVLDYPLGDSDAVVPVTVMANVLGAAQPPAMSVDERLHHLFARMPDARVHLYGKAERPGRKVGHINFLGSDVAQLCERAELAAHWLSHGRWTDGWDPHRASDDAVGVPPACGGRSDEEERRL | Function: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR).
Catalytic Activity: 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ATP + hydrogencarbonate = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + 2 H(+) + phosphate
Sequence Mass (Da): 45695
Sequence Length: 429
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2.
EC: 6.3.4.18
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B2IU46 | MTATSPAFFSPQEIAAEGLKPEEYAEIVRRLGRHPNKAELGMFGVMWSEHCCYKNSRPLLKQFPTEGPRILVGPGENAGVVDLGDGLQLAFKIESHNHPSAVEPFQGAATGVGGILRDIFTMGARPIALLNSLRFGSLEDAKTQRLFQGVVAGISHYGNCVGVPTVGGEVYFDPAYSGNPLVNVMALGLMETQEIVKSGASGLGNPVLYVGSTTGRDGMGGASFASAELSDQSIDDRPAVQVGDPFLEKSLIEACLEAFKTGAVVAAQDMGAAGITCSTSEMAAKGGVGIELDLDKIPARETGMVPYEYLLSESQERMLFVAHKGREQELIDIFHRWGLQAVVAGTVIAEPIVRILFQGGVAAEIPAEALAENTPLYNRELLAEPPEYARQAWEWTPDSLPACTTAGIEIQGGQQSWNDILLTLLDTPTIASKNWVYRQYDHQVQNNTVILPGGADAAVIRLRPLEEIPNLKSKIPNLKLGVAATVDCNPRYVYLHPYEGAKAVVAEAARNLSCVGAEPLAVTDNLNFGSPEKPIGYWQLAEACRGLAEGCRELATPVTGGNVSLYNETLDSQGIPQPIYPTPVVGMVGLIPDITKICGQGWQASGDVIYLLGLPLASKISLGASEYLATIHNTVAGKPPLVDFDLERRVQKVCREGIRNGWIRSAHDSAEGGVAIALAECCIAGNLGAEINLEIAPMQNRVDEMLFAEGGARILVSVTSAQQAIWESYLQEHLGQQWQILGTVGNFETGLGVFTTDNQILIKVSIEDMSDRYSHAIARRIATNTAVS | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 84417
Sequence Length: 788
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q8ES96 | MQLTHDIQPEKIEKDRLYLDMGLSDEEFQRIKQILGRHPNFTETGIFSVMWSEHCSYKTSKPLLKKFPTDGPHVLQGPGEGAGVIDIGDEQAVVFKIESHNHPSAVEPYQGAATGVGGIIRDVFSMGARPIASLNSLRFGPLTNNRTKYLFSEVVAGIAGYGNCVGVPTVGGEVQFDESYEDNPLVNAMCVGLINHKDVQKGIAAGIGNTILYAGPPTGRDGIHGATFASDDLAEDSNKDRPAVQVGDPFMEKLLIEACLEVIQSDALVGIQDMGAAGLTSSASEMASKAGTGLEMNLDLVPQREQGMTAYEMMLSESQERMLLCVQAGREQEIIDIFEKYGLKSVPVGKVIEEKVFRIKHLDEVVADIPVDSLADDAPVYNMPSKEAAYYRAFQQMDIATPAIEDYANTLKQLLQQPTIANKEWVYDQYDSMVQTNTVVTPGSDAAVVRIKGTEKALAMTTDCNSRYIYLDPETGGKIAVAEAARNIVCSGAKPLGLTDGLNFGNPTNPEIFWQMEKSVEGMSAACDALHTPVISGNVSLYNQSKGKSIYPTPIVGMVGLHESTQHITPSYFQEKEDVIYCIGEAKAEFGGSELQHLYSGKYEGKAPHIDLDVEAERQEKLLSAIKEGIISSAHDISEGGLAIALAESLFNGQGLGAEINVVGDATVELFSESQSRFLVSVNKKHANAFESHFPEAAKLGKVTDQGQLTISISDKTIIHERVEELENLWKGAIPCLLKSKA | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 80444
Sequence Length: 742
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q4FLJ4 | MIVNEQLAIDHGLKKDEYKKICDLLKRVPNITELGIFSAMWNEHCSYKSSRFHLKNLPTKGKNVIQGPGENAGVIDIGDDDAIVFKIESHNHPSFIEPYQGAATGVGGIMRDVFTMGARPIANLNSIHFGSPQHKKTKNLLRGVVHGIGGYGNCMGVPTIAGQTSFDESYNGNILVNAMTLGHVKKDKIFYSKAAGLGKPVIYVGSKTGRDGIHGASMASASFDDKIEEKKPTVQVGDPFTEKLLLEACLELMAGDSIIAIQDMGAAGLTSSSIEMASKGNLGIEINLSKVPCREANMSPYEIMLSESQERMLIVLENGKEEMAKKIFDKWNLDFAVIGQTTKSKKIELYFNEEKVADIPVNTLVENSPMYDRKWKKAKLPKRIKVDKEQFKTLKVKNVLNKILSNPNVCSKEWIWQQYDHTVMGDTIQKPGGDAGVVRVHGTNKAVAASVDSSAVYCWAHPLSGGKQIVCESWRNLISVGAKPIAITNCLNFGSPENEENMGEFVECVQGLGEASAYLEFPVVSGNVSFYNQTKDIGIKPTPAIGGVGLIKDYQNMVTMDLKEADNILLVIGKTEGHLDQSLFARDILNEKNGPPPEINLFNEKNNGETILKLINKKFIKSAHDVSLGGIITALSKMCIKGKKGATLKKSNYLINQFEYLFGEDQGRYIIEISKDDLENATKILQENSVHFDELGLVNEDGLIIDDKTKVSIDDLIKSHTNWLTNYMEN | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 80411
Sequence Length: 730
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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A9BIH4 | MQNQLTIKEIALELGISREEFDLIEEKLGRIPNEFETYLFSAQWSEHCGYKHSKHYLKKINESYESENAGYVQIGGKAVVFKVESHNHPSAVEPYQGAATGIGGIVRDILAMGARPIALLDSLKFGNVFDPKVKNIFEGVVSGISDYGNSIGVPTVGGETSFNEIYSTNPLINVMCVGVANKNHLASSHADGPDKLLVYVGSKTGRDGIHGASFASKKLSGKDDRPSVQVGDPFTEKNLIEATLEILKIKGVRACQDMGAAGVLSSTSEMAYKGGVGCELYLDNIPKRQEDIEPWEIMLSESQERMLFLVNPGTEKKVEAICNKYLIDFAVIGKTISTPHYVVKENSEGKVLADLPIDILVNAPEYYRNNTIPSTYILNKAKKYPKTKIKDIDKILKILLSNHNISSKKWIYQQYDYKVETNTIFIPEQADSAVLWLKKTQKAIAVTIDSNELYTYLDPFEGTKNVVYEAARNLISVGAKPLAITDNLNFGDPDDPEVSWQFEKSIEGLIEASKELSTPVVSGNVSFYNSYHETSIFPTPVIGMIGEIKDIKKIVNLKFKDCGDVVYLIGKTDINVDKIGGSFYLKVLEGFVGGEIDFVNPMYERYLQNFILDLIDKGILKSVHDVSKGGLLTALAVSCILSNRGFKGILDASIEELFGENQGRFIVSVRSKDSRIFEDIAKSSNINVKKLGEIKSSDDGIDICSAYFDLKELKSIYFDSISKSVEE | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 80462
Sequence Length: 727
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q59042 | MKIAVTKFLGTNCDLDVCHAVKLAGGEPELVFFTQENLDSYKGAVIPGGFSYGDYLRAGAISARTPIIKGLKKMVEEGKPVLGICNGAQIGLEAGFSKGTLTNNLNAKFICKWVYIRVENNKTPFTQYYKKGEVLKIPIAHAEGRFYADDETLDYMYKNNMIVFKYCDETGEVTEEANPNGSIDNIAGVCNENQNCVLLMPHPERASEKILGSDDGLKMFKGMIDYAKRI | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 25417
Sequence Length: 230
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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Q8TX85 | MVRVAVIRFPGTNCDLEMAWAVKLAGGDPEFVWHEDGGLDDFDAVIIPGGFTYGDYIRAGAIAALSPILEEIRECAEDGRPVLGVCNGMQILAEAELIPGTLTVNVGNRFICDWVYLRVERTDTPFTTKYQEDEVIRVPIAHAEGRYYYENPEEIEDNVVFRFCGPDGDVSEEYNLNGSVGGITGVVNDDGNVLGMMPHPERAAHRLLNSDDGLRLFESLVEWCRS | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 25032
Sequence Length: 226
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
|
A4G010 | MVPKVLVMSGYGINCETETAHAFQKAGAETDIVHINDLIAGKKKMADYEIIMFPGGFSYGDDTGSGNAFANKIKNNLFDDLKEFINSGKLILGICNGFQVMTNLGLFALPSTDYGERISALEANTNNRYECRWVHVKENDSICVFTKGITITHVPIAHGEGRFYCDEKTYFELKENKQIVFSYCDSEGNSANQEYPLNPNGAYYDIAGICDKTGRIMGLMPHPERSLYSISEPEYQLKKEIAKRNREIIPEFIESNLQIFKNAVEYFNK | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 30314
Sequence Length: 269
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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O26270 | MRVGVIRFPGSNCDRDVHHVLELAGAEPEYVWWNQRNLDHLDAVVIPGGFSYGDYLRAGAIAAITPVMDAVRELVREEKPVLGICNGAQILAEVGLVPGVFTVNEHPKFNCQWTELRVKTTRTPFTGLFKKDEVIRMPVAHAEGRYYHDNISEVWENDQVVLQFHGENPNGSLDGITGVCDESGLVCAVMPHPERASEEILGSVDGFKFFRGILKFRG | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 24274
Sequence Length: 218
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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A0B5C6 | MRIAVIQFPGTNCEHETLVAVRECGMDGEIFRWNRPEQELCEFDGYVIPGGFSYQDRVRAGVIASKEPVMATLREEAANGKPIIGICNGFQILVESGILPFGDGVRLALAQNVMIRGGEIVRRGYYCAWTMLRHDAEEKRCSGSYILRRGEILSIPIAHAEGNLVASDRKVIERLIEDDQIVFRYCSPQGEIINEFPVNVNGSTENIAGISNPEGNVLGMMPHPERAFFAWQLPRKHPRIPGYGPGRKIFDSMKRYIEERRS | Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 29483
Sequence Length: 262
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Subcellular Location: Cytoplasm
EC: 6.3.5.3
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P46456 | MATIKDVAKMAGVSTTTVSHVINKTRFVAKDTEEAVLSAIKQLNYSPSAVARSLKVNTTKSIGMIVTTSEAPYFAEIIHSVEEHCYRQGYSLFCVTHKMDPEKVKNHLEMLAKKRVDGLLVMCSEYTQDSLDLLSSFSTIPMVVMDWGPNANTDVIDDHSFDGGYLATKHLIECGHKKIGIICGELNKTTARTRYEGFEKAMEEAKLTINPSWVLEGAFEPEDGYECMNRLLTQEKLPTALFCCNDVMALGAISALTEKGLRVPEDMSIIGYDDIHASRFYAPPLTTIHQSKLRLGRQAINILLERITHKDEGVQQYSRIDITPELIIRKSVKSIL | Function: Is the main repressor of the genes involved in the de novo synthesis of purine nucleotides, regulating purB, purC, purEK, purF, purHD, purL, purMN and guaBA expression. PurR is allosterically activated to bind its cognate DNA by binding the purine corepressors, hypoxanthine or guanine, thereby effecting transcription repression.
Sequence Mass (Da): 37508
Sequence Length: 336
Domain: Consists of two structural and functional domains: an N-terminal DNA-binding domain, approximately the first 60 residues, and a larger C-terminal domain, approximately 280 residues, which imparts the function of corepressor binding and oligomerization.
Pathway: Purine metabolism; purine nucleotide biosynthesis [regulation].
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Q0I600 | MTNFPKTVMLLGSGELGKEVAIAAQRLGCHVIACDRYADAPAMQVADQAEVLTMTDPNALKTVVNKHQPDVLIPEIEALAVDALQALEDTGICVIPTARATAVTMNRDRIRNLAAGELGLRTARFAYASDAQELQRAAAPLGWPVVVKPVMSSSGKGQSVVHSAAELDKAWEIAMAGARGSSAQVIVEEFLDFDLEITLLTIRQHDGTTLFCPPIGHQQANGDYQCSWQPASISPSQLQQAQTMARTVTDNLGGAGLFGVEFFLCGDEVVFSELSPRPHDTGLVTLISQNLSEFDLHLRAVLGLPIPSITAADAAASRVILAESQGHHVQFSGVEQALTEPDTNLLLFGKREARPGRRMGVALARGTQINEALAKADRCAAAVKVQVMD | Function: Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
Catalytic Activity: ATP + formate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 41492
Sequence Length: 389
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (formate route): step 1/1.
EC: 6.3.1.21
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Q3AUF2 | MTAFPRTVMLLGSGELGKEVAIAAQRLGCRVIACDRYANAPAMQVADTAEVFQMTDATALKEVVQRHRPDVVIPEIEALAVEALAELEQDGITVIPTARATAFTMNRDQIRDLASGELGLHTARFAYASNAAELKKVAAPLGWPVVVKPVMSSSGKGQSVVQTPEQLDQAWEAAMANARGTSNQVIVEEFLEFDLEITLLTIRQRNGETLFCPPIGHEQERGDYQCSWQPAQMSDAQLQQAQTMARTVTDNLGGAGLFGVEFFLCGNEVIFSELSPRPHDTGLVTLISQNLSEFELHLRAVLNLPIPQLTTAPAAASRVILADRELKTVAYEGLEQALREAGTQVLLFGKPNARPNRRMGVALARGEDLSEVRAKADRAAACIQVLDGSARR | Function: Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
Catalytic Activity: ATP + formate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 42485
Sequence Length: 392
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (formate route): step 1/1.
EC: 6.3.1.21
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Q8D2R3 | MVTINTALCKNSTRVMILGSGELGKEIAIECQRLGIEVISVDSYSNAPAMHVSHRHHVIDMLNPKEIKRCINLEHPDFIVPEIEAISTNALIELEKNGYNIVPSAKTIHITMNRKLIRVLVSKKLNILTSEYQFASSFDELKIKTKVIGYPCLIKPIMSSSGKGQSVIYNEKELRHSWEKSQTYGRTSLGEVIIEKIIPFDFEITLLVVNSVDGMHFCLPIGHRQEKGDYQESWQPHKMDNVIFEKAKKISKKIVSYLGGYGIFGVEFFIYKDKVIFSEISPRPHDTGMVTLISQNLSEFALHVRSFLKLPIGKIRQYGPSSSVVICGNELYGNKISFSNIECINTNQQIRIFSKPNIKGYRRLGVILDQDETIERSLRKAKKTASKILIKT | Function: Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
Catalytic Activity: ATP + formate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Mass (Da): 44417
Sequence Length: 392
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (formate route): step 1/1.
EC: 6.3.1.21
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Q94JZ8 | MEGMLSSGDQQRLVSSFLEIAVGQTAETARQFLQATSWKLEEAIQLFYIGNEGGMLQSGTHTQPASNDDAAAQSWGAATGTGNEMILPNDVDEVRAPLPVVRETLYGESMYYGAMRVGNSQPEPNSLIAFRNFSEEPKSPGIWEPDEGDSSASASASASASESASAPRDSLASLYRPPFHLMFQGSFEQAKTTSSSQDKWLLVNLQSTTEFSSHMLNRDTWANDAVSQTIKANFIFWQVYDDTTEGRKVCTYYKLESIPVVLVIDPTTGQRMRMWTGMVDPENLLEDLVPFMDGGPREHFASLSKKRPRGSFSLTPHSKPKEDVAKDEEEEELQRALAASLEDNNMKESSDDQSTIIPEEVAVEAVTSAVLPTFPPLPEEPKGGDRSLQCRVGIRLPNGQRLQRNFLKTDTIQLLWSFCYSQLEESERKKPLKLTQAIPGESKTLEYESNLTLEQSGVANSMISATWE | Function: Acts as a bridge between CDC48A and ubiquitin, suggesting a role in targeted protein degradation.
Sequence Mass (Da): 51808
Sequence Length: 468
Domain: The UIM (ubiquitin-interacting motif) is required to engage the NEDD8 modification on cullins.
Subcellular Location: Nucleus
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O42173 | MVQQGFSIDLILARSREEAADGKDSMSSRPHIPCAPQPLPPNKYAKEMPRRKDGQDVQEHSSWSLGEQGKKLQYSSPSSAALHRSWGSSDDFSSVGSEDDSTEGSPSPMRNSQETETDHRGESPKSDLQRHLRTAFTPQQISKLEQAFNKQRYLGASERKKLATSLRLSEIQVKTWFQNRRMKLKRQIQDQQHNMVPPPVCYPQTFPYYPGVLPVPLNSGSFYQPPAHPFQAPQNSYIPDPRFIPQPLPHHIRMSVALQQQYPPLGLPPGRYFTGLASKNDG | Function: Transcriptional repressor. Acts in a ventral signaling pathway downstream of bmp4, which suppresses dorsal mesoderm formation and leads to both ventral mesoderm and ventral ectoderm formation. Acts in the ectoderm to simultaneously specify epidermal lineages and restrict neuralization. Represses transcription of dorsal-specific genes. Binds to DNA, with preference for the target sequences 5'-TAATGC-3' and 5'-TAATTG-3'. Acts in a pathway downstream of bmp4 and fgf to negatively regulate erythroid specification.
Sequence Mass (Da): 31846
Sequence Length: 282
Domain: The repressor activity is mostly localized to the C-terminal region.
Subcellular Location: Nucleus
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P0C8G6 | MSQLRWWVVSQLLLLIVVCILDHSEGARVCPKIVPGLDKLRVGVDITKLDLLPLFDLGDNGFRSAVADYTCDRGQTTVVDGESFDVPDQVDSVVIESSGQQTSSVTTIKSESQISQALSISAGISVDTAKAGFSSSASYAEMQEAITKYGRTVSQMSAVYTTCSANLSPNLLLGQNPLQTLSRLPSDFTADTEGYYDFIKTYGTHYFNKGKLGGMFLFTSETDMSYFQNKNSQQVEANIKATFASILSTETGGSSDQSKEVIEFKESSLITAKFFGGRTNLAADGLTKWQPTIAKLPYFMSGTLSTISSLIADTTKRASMELAVKNYLLKAKVANLDRLTYIRLNSWTVGHNELRDLSAQLQNLKKKTIFSDEDEKLLQSIEDQVSVPAWFSDRTTFCFRSTAVGSADQCNGQSTSTLCAEPNRYTQQYMDKTYLGDTGCRLVWKLSTTESSDWFKSVKVNFRWYPTWSPCACGPVGTPFTISAPANSWTQDYLDVTNPKFGECMLQWMIEVPPTATLWAKNLEFCIDFTCGKKKQCVDANHWTEPYLDISAHEACGMSWALIAK | Function: The egg defensive protein perivitellin-2 is a pore-forming two-subunit glycoprotein that affects both the nervous and digestive systems of mammals . In addition, it is a source of both structural and energetic molecules during embryonic development (Probable). The tachylectin subunit (31 kDa) binds target membranes while the MACPF subunit (67 kDa) disrupts lipid bilayers forming large pores altering the plasma membrance conductance . Both in vivo and in vitro, the protein shows wide pH range stability and is resistant to enzymatic proteolysis from gastrointestinal environments . It specifically binds mature enterocytes but does not cause cell disruption on caco-2 (human colorectal adenocarcinoma cells) or rat intestinal cells . After oral administration to mice, it binds enterocytes and induces large dose-dependent morphological changes on their small intestine mucosa, reducing the absorptive surface (By similarity). Additionally, it is detected in the Peyer's patches where it activates lymphoid follicles and triggers apoptosis (By similarity). The toxin can also traverse the intestinal barrier and induce oral adaptive immunity with evidence of circulating antibody response . The toxin also shows hemagglutination properties thanks to the tachylectin subunit, but does not show hemolytic activity . In addition to enterotoxin activity, the toxin also acts as a neurotoxin, since an intraperitoneal injection induces paralysis of the mice rear limbs, followed by death .
PTM: Glycosylated. Contains four O-linked and one N-linked oligosaccharide bonds. The protein contains 2.5% of carbohydrates (high levels of mannose, galactose, and NAcGlucosamine, and small amounts of NacGalactosamine).
Sequence Mass (Da): 62518
Sequence Length: 565
Subcellular Location: Secreted
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P0C8G7 | MVKKIHFIMERHASIVAFLLAVLALTESQAFTSVKLPRDEHWPYNYVSIGPAGVWAVNRQNKLFYRTGTYGDNANMGSGWQFKQDGVGQVDVGKDKVGYINLSGGSLFRIDGISQGNPVGGSPKSWEWWTKYIGMSLREDTRFSSRIENQNKVLTFTFRTCFWASRITNWCFADSSYTETVTAGGSGTWITKSQLKYKSGTFGNPDTEGGDWITVDSGSFQHVSSGSGVVLAVRSNGELVKRTGITCSLPQGSGWTSMLNGMSRVDTYGTVAWAVDTYGDLYFINL | Function: The egg defensive protein perivitellin-2 is a pore-forming two-subunit glycoprotein that affects both the nervous and digestive systems of mammals . In addition, it is a source of both structural and energetic molecules during embryonic development (Probable). The tachylectin subunit (31 kDa) binds target membranes while the MACPF subunit (67 kDa) disrupts lipid bilayers forming large pores altering the plasma membrance conductance . Both in vivo and in vitro, the protein shows wide pH range stability and is resistant to enzymatic proteolysis from gastrointestinal environments . It specifically binds mature enterocytes but does not cause cell disruption on caco-2 (human colorectal adenocarcinoma cells) or rat intestinal cells . After oral administration to mice, it binds enterocytes and induces large dose-dependent morphological changes on their small intestine mucosa, reducing the absorptive surface (By similarity). Additionally, it is detected in the Peyer's patches where it activates lymphoid follicles and triggers apoptosis (By similarity). The toxin can also traverse the intestinal barrier and induce oral adaptive immunity with evidence of circulating antibody response . The toxin also shows hemagglutination properties thanks to the tachylectin subunit, but does not show hemolytic activity . In addition to enterotoxin activity, the toxin also acts as a neurotoxin, since an intraperitoneal injection induces paralysis of the mice rear limbs, followed by death .
PTM: Glycosylated. PV2 contains four O-linked and one N-linked oligosaccharide bonds. The protein contains 2.5% of carbohydrates (high levels of mannose, galactose, and NAcGlucosamine, and small amounts of NacGalactosamine).
Sequence Mass (Da): 31584
Sequence Length: 286
Subcellular Location: Secreted
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A0A060LAL9 | MASNESLQTTAAMAPVTIERRVNPNLDDELPKPFLPRALVAVDTEHPSGTPGHQHGDMSVLQQHVAFSNRNNDGIVYPWETFLGFRAVGFNIIISFFGCLIINIFLSYPTLPGWIPSPFFPIYIDRIHRAKHGSDSEVYDTEGRFVPAKFEEIFTKNAKTHPDKLSFSELWNLTEHNRNALDPLGWIAAKLEWFLLYSLAKDPHGFVPKEAARGVFDGSLFEFCEKSRKVKQATVKSLTFKI | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group.
Function: Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies.
Catalytic Activity: RH + ROOH = ROH + ROH.
Sequence Mass (Da): 27378
Sequence Length: 242
Domain: Transmembrane regions are predicted by sequence analysis tools, but these regions probably constitute hydrophobic domains associated to phospholipids.
Subcellular Location: Lipid droplet
EC: 1.11.2.3
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Q7Z7A4 | MAFMEKPPAGKVLLDDTVPLTAAIEASQSLQSHTEYIIRVQRGISVENSWQIVRRYSDFDLLNNSLQIAGLSLPLPPKKLIGNMDREFIAERQKGLQNYLNVITTNHILSNCELVKKFLDPNNYSANYTEIALQQVSMFFRSEPKWEVVEPLKDIGWRIRKKYFLMKIKNQPKERLVLSWADLGPDKYLSDKDFQCLIKLLPSCLHPYIYRVTFATANESSALLIRMFNEKGTLKDLIYKAKPKDPFLKKYCNPKKIQGLELQQIKTYGRQILEVLKFLHDKGFPYGHLHASNVMLDGDTCRLLDLENSLLGLPSFYRSYFSQFRKINTLESVDVHCFGHLLYEMTYGRPPDSVPVDSFPPAPSMAVVAVLESTLSCEACKNGMPTISRLLQMPLFSDVLLTTSEKPQFKIPTKLKEALRIAKECIEKRLIEEQKQIHQHRRLTRAQSHHGSEEERKKRKILARKKSKRSALENSEEHSAKYSNSNNSAGSGASSPLTSPSSPTPPSTSGISALPPPPPPPPPPAAPLPPASTEAPAQLSSQAVNGMSRGALLSSIQNFQKGTLRKAKTCDHSAPKIG | Function: Binds to and modulates brain Na,K-ATPase subunits ATP1B1 and ATP1B3 and may thereby participate in the regulation of electrical excitability and synaptic transmission. May not display kinase activity.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 64950
Sequence Length: 578
Domain: The protein kinase domain is predicted to be catalytically inactive.
Subcellular Location: Cytoplasm
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Q09476 | MPSDDRFADAVKPALEALLSDLQHTTEVLRRAHISDRRSQSRDDFEQSYDLQGNLNTQSVSNGNITTSPYKRRSSEGKDYSKSQERIYENESRLNPPVYSRPSVQSLLSQVEEPPIRASSSRKSLGPPSQAQSYSDVRSNGRSPSRDPLHSDSMIGTMNGELSSKHGVNTIPKGDCAACGKPIIGQVVIALGKMWHPEHYTCCECGAELGQRPFFERNGRAFCEEDYHNQFSPKCQGCHRAITDRCVSVMNKNFHIECFTCAECNQPFGEDGFHEKNGQTYCKRDFFRLFAPKCNGCSQPITSNFITALGTHWHPDCFVCQHCGVSFNGASFFEHNGAPLCERHYHESRGSICSQCRGAINGRCVAAMGRKFHPEHFRCSYCNHQLTKGTFKEVDRRPFCHKCYNNTYALTPA | Function: Required for myofilament organization of the pharyngeal sarcomeres and for pharyngeal muscle contractions and hence for pharyngeal pumping . Together with lin-8, might be required for myofilament organization in the body wall muscles .
Sequence Mass (Da): 46453
Sequence Length: 413
Domain: LIM zinc-binding domains 1-4 are sufficient for the localization to dense bodies, adhesion plaques and M lines in body wall muscles.
Subcellular Location: Cell junction
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Q58CY6 | MSTVDLARVGACVLKHAVTGEAVELRNLWQEQACVVAGLRRFGCMVCRWIARDLSNLKGLLDQHGVRLVGVGPEALGLQEFLDGGYFAGELYLDESKQFYKELGFKRYNSLSILPAALGKPVREVAAKAKAVGIQGNLSGDLLQSGGLLVVAKGGDKVLLHFVQKSPGDYAPLESILQALGISAEVGPSELPQCDEEACSR | Function: Catalyzes the reduction of prostaglandin-ethanolamide H(2) (prostamide H(2)) to prostamide F(2alpha) with NADPH as proton donor. Also able to reduce prostaglandin H(2) to prostaglandin F(2alpha) (By similarity).
Catalytic Activity: [thioredoxin]-dithiol + prostaglandin H2 = [thioredoxin]-disulfide + prostaglandin F2alpha
Sequence Mass (Da): 21497
Sequence Length: 201
Subcellular Location: Cytoplasm
EC: 1.11.1.20
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Q49Y42 | MKVDLNCDLGEAFGNYSFGGDNQIIPLITSANIACGFHAGDQHVMNDTIKLAKDNGIGIGAHPGLPDLQGFGRRNMDLSPEEVYDIVVYQLGALNGFCRIHDVKINHVKPHGALYQMGARDKVIAHAIAKAVYDFDPTLIYVGLSNTLLISEAQALGLSTASEVFADRRYEDDGQLVSRKEADALITNTDEAIKQVINMVKFQKVITKNNNTIDIKADTICVHGDGAHAIEFVTQIREQLTKEGISITRLGG | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 27408
Sequence Length: 252
EC: 3.5.2.9
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Q9RL45 | MIDLNADLGEGFGRWTLTDDDALLSVVTSANVACGFHAGDPSVMRRVCDLAAERGVRIGAQVSYRDLAGFGRRAMDVPSDELAAEVAYQIGALRVFAEAAGAPVAYVKPHGALYNRTVHDEGQARAVVAGVRLAGGALPVLGLPGSRLLTAAAEAGLTGVPEAFADRAYTAEGSLVPRSEAGSVVTDEDAVVRRALAFAVEGSVEAVDGTAVAVAARSLCVHGDTPNAARIAARVREALETAGVGIGAFA | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 25511
Sequence Length: 250
EC: 3.5.2.9
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Q53WG6 | MKVDLNADAGESYGAFAYGHDREIFPLVSSANLACGFHGGSPGRILEAVRLAKAHGVAVGAHPGFPDLVGFGRREMALSPEEVYADVLYQIGALSAFLKAEGLPLHHVKPHGALYLKACRDRETARAIALAVKAFDPGLPLVVLPGTVYEEEARKAGLRVVLEAFPERAYLRSGQLAPRSMPGSWITDPEEAARRALRMVLEGKVEALDGGEVAVRADTLCIHGDNPNAPEVARAVREALEQAGVEVRAF | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 26725
Sequence Length: 250
EC: 3.5.2.9
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C4LFU8 | MAQVDLNCDMGESFGIYQMGTDTQIMPLVSSANIACGFHAGDPSVMRKTLEAAVAQGVALGAHPGLPDLVGFGRRNMQVSAQEAYDMVVYQVGALAGFAKAAGVSLHHVKPHGALYNMAAKDKALADAIARAVRDIDASLVLYGLAGSQLIQAGKNAGLRVASEVFADRTYQADGSLTSRSQPNALLQSDEEAVQQVLTMVTEKRVKAVTGEWVSLDADTICIHGDGAHALSFATKVRAALLQAGVEIKAM | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 26299
Sequence Length: 251
EC: 3.5.2.9
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A5EZN1 | MSKRTIQLNCDMGESFGVWTMGADEEVMPWIDMANIACGFHASDPHVMSRTIDLALEHEVMIGAHPSYPDLQGFGRRSLAMNEQEVSEIILYQVGALKALCESKNGQLSYVKPHGALYNDMMSDPSIFRAVVDAVSCFNLPLMVLASANNQDYLDIADRFDVPLLFEAFADRTYLANGKLTPRSQPNAVLSSEEAILNQVRQIARYGKVTSSDGFVIPIEADTLCVHGDNPNAVSLIARIRAALDE | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 27057
Sequence Length: 246
EC: 3.5.2.9
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Q7ME92 | MNKQRVTLNCDMGESFGNWKMGSDELVMPWVDMANIACGFHASDPSVMSKTVALAKHYKVKIGAHPGYQDLVGFGRRSIPHTPAQISEIVLYQVGALKAVCQYHDVPLHYVKPHGALYNDMMESEAIFRAICEAVSIFGIPLMILATSDNQRYLDIADIYDVPLLFEAFADRQYQEDGKLTPRSQANAVYHQPEDIYNQALQIATYGSVNTANGTRLSLEADTICVHGDNPESITLVQRISQAIAKM | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Mass (Da): 27412
Sequence Length: 247
EC: 3.5.2.9
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