SPM_004760
  | Uniprot: A0A037UN58
Description: adenylosuccinate synthetase EC number: 6.3.4.4 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520}. Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_00011}; ; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00011} Enzyme regulation: Function [CC]: 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. {ECO:0000256|HAMAP-Rule:MF_00011}. Pathway: PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520}. Active site: ACT_SITE 18 18 Proton acceptor. {ECO:0000256|HAMAP-Rule:MF_00011}.; ACT_SITE 46 46 Proton donor. {ECO:0000256|HAMAP-Rule:MF_00011}. Binding site: BINDING 133 133 IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.; BINDING 147 147 IMP; shared with dimeric partner. {ECO:0000256|HAMAP-Rule:MF_00011}.; BINDING 228 228 IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.; BINDING 243 243 IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.; BINDING 307 307 IMP. {ECO:0000256|HAMAP-Rule:MF_00011}.; BINDING 309 309 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}. Calcium binding: DNA binding: Metal binding: METAL 18 18 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00011}.; METAL 45 45 Magnesium; via carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_00011}. Nucleotide binding: NP_BIND 17 23 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.; NP_BIND 45 47 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.; NP_BIND 335 337 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}.; NP_BIND 417 419 GTP. {ECO:0000256|HAMAP-Rule:MF_00011}. Site: Gene names (primary): purA Gene names (synonym): Mass: 48,589 Subunit structure [CC]: SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00011}. Gene ontology (GO): cytoplasm [GO:0005737]; adenylosuccinate synthase activity [GO:0004019]; GTP binding [GO:0005525]; magnesium ion binding [GO:0000287]; 'de novo' AMP biosynthetic process [GO:0044208] Gene ontology IDs: GO:0000287; GO:0004019; GO:0005525; GO:0005737; GO:0044208 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the adenylosuccinate synthetase family. {ECO:0000256|HAMAP-Rule:MF_00011, ECO:0000256|RuleBase:RU000520}. Protein families: Adenylosuccinate synthetase family Coiled coil: Domain [FT]: Motif: Region: REGION 18 21 IMP binding. {ECO:0000256|HAMAP-Rule:MF_00011}.; REGION 43 46 IMP binding. {ECO:0000256|HAMAP-Rule:MF_00011}.; REGION 303 309 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_00011}. EMBL: AGBZ02000004 ProteinModelPortal: MEROPS: EnsemblBacteria KO: KAI92051 UniPathway: CDD: Gene3D: HAMAP: InterPro: MF_00011 PANTHER: IPR018220;IPR033128;IPR001114;IPR027417 PIRSF: PTHR11846 PRINTS: PROSITE: Pfam: PS01266;PS00513 ProDom: PF00709 SMART: SUPFAM: SM00788 TIGRFAMs: SSF52540 |
21252-22554(+) >nucleotide sequence AAGGGCAAAATTACCGATTATTTTGCTCAACAAGCAGATGTTATTGTTCGTTGAGCTGGT GGTGATAATGCTGGACATACAATTGTCATTAAAGGAACAAAATATAAGTTAAGTATTGTT CCTTCTGGTGTTTTTAATAAAAAATCAATGAATGTAATTGGGAATGGTTGCGTTGTTAAT TTACGTAAATTAGTTAGTGAAATTAGTTATTTACAAGAACATGGTTTTGATTGTAAAAAT TTACGAATTAGTGATCGTGCCCATTTAATTTTTCCATATCATATGAAAATTGATGAGTTG CAAGAAGAGTATCGTCAAAAAGACTCAATTGGAACAACAAAAAAAGGAATTGGTCCTTGT TATCAAGATAAAGCCGAACGAATTGGCATTAGACTAGGTGATTTGTTTGATGAAAAAGGA TTTTTACAAAAATTAGAAAATAATTTAAAATTTAAAAATGAAGTTTTAACAAAAGTTTTT AATAGTAAAGGATTTGACCCAAAATTAATTTGAAAAGAATATTTGGCATTATTTCAACAA ATTAAATCTTTAGTAACTGATACTTCAATTTTAGTTGATAATGCAATTCATACTCACCAA AAGGTTTTATTTGAAGGAGCACAAGGTGTAATGTTAGACTTAGATCACGGTACTTATCCT TTTGTTACTTCATCAAATCCAACAGCATCTTCAATTCCTGTTGGTGTTGGGATTGCACCT CGTTATATTAACAATGTTTTAGGAATCGTTAAAGCATATAATACCCGTGTTGGGACAGGA CCATTTCCATCCGAAATTTTTGGGGAAGTTGAAACGTATATTCGTGAAGCAGGACATGAA TATGGAACTGTATCTGGGCGAGCACGACGAATTGGGTGATTTGATGGTATTTTAATGAAA CATTCGCTACGAATTAGTGGTTATACTAGTATGGCAATTATGTTATTAGATGTTTTAACT ACTATTAAGGAATTAAAAATTTGTGTTGGATATGAATATCAGGGGCAACAAATTGATTAT GTTCCAAGTACAATTAAAGAATATGAGATGTGTAAACCAATTTTAATAACAATGCCGGGA TGAGATGAAGACATTAGTAATGTTACAACATTTGAAGGTTTACCACATAATGCCCAACAA TATTTAATGAAATTAGAAGAAATTGTTGGTGTTCCAATTAGTTTATTTTCTGTTGGTCCT GATCGTGAACAAACTATTTTAATGAATAAGGAGATTTTTTAA >protein sequence PSGVFNKKSMNVIGNGCVVNLRKLVSEISYLQEHGFDCKNLRISDRAHLIFPYHMKIDEL QEEYRQKDSIGTTKKGIGPCYQDKAERIGIRLGDLFDEKGFLQKLENNLKFKNEVLTKVF NSKGFDPKLIWKEYLALFQQIKSLVTDTSILVDNAIHTHQKVLFEGAQGVMLDLDHGTYP FVTSSNPTASSIPVGVGIAPRYINNVLGIVKAYNTRVGTGPFPSEIFGEVETYIREAGHE YGTVSGRARRIGWFDGILMKHSLRISGYTSMAIMLLDVLTTIKELKICVGYEYQGQQIDY VPSTIKEYEMCKPILITMPGWDEDISNVTTFEGLPHNAQQYLMKLEEIVGVPISLFSVGP DREQTILMNKEIF |
© Fisunov Lab of Proteomics, 2016.