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
ATGAGTGGTACAAATTATCGAACATTAGCAATTGTTGGGAGCCAGTGAGGTGATGAAGGA
AAGGGCAAAATTACCGATTATTTTGCTCAACAAGCAGATGTTATTGTTCGTTGAGCTGGT
GGTGATAATGCTGGACATACAATTGTCATTAAAGGAACAAAATATAAGTTAAGTATTGTT
CCTTCTGGTGTTTTTAATAAAAAATCAATGAATGTAATTGGGAATGGTTGCGTTGTTAAT
TTACGTAAATTAGTTAGTGAAATTAGTTATTTACAAGAACATGGTTTTGATTGTAAAAAT
TTACGAATTAGTGATCGTGCCCATTTAATTTTTCCATATCATATGAAAATTGATGAGTTG
CAAGAAGAGTATCGTCAAAAAGACTCAATTGGAACAACAAAAAAAGGAATTGGTCCTTGT
TATCAAGATAAAGCCGAACGAATTGGCATTAGACTAGGTGATTTGTTTGATGAAAAAGGA
TTTTTACAAAAATTAGAAAATAATTTAAAATTTAAAAATGAAGTTTTAACAAAAGTTTTT
AATAGTAAAGGATTTGACCCAAAATTAATTTGAAAAGAATATTTGGCATTATTTCAACAA
ATTAAATCTTTAGTAACTGATACTTCAATTTTAGTTGATAATGCAATTCATACTCACCAA
AAGGTTTTATTTGAAGGAGCACAAGGTGTAATGTTAGACTTAGATCACGGTACTTATCCT
TTTGTTACTTCATCAAATCCAACAGCATCTTCAATTCCTGTTGGTGTTGGGATTGCACCT
CGTTATATTAACAATGTTTTAGGAATCGTTAAAGCATATAATACCCGTGTTGGGACAGGA
CCATTTCCATCCGAAATTTTTGGGGAAGTTGAAACGTATATTCGTGAAGCAGGACATGAA
TATGGAACTGTATCTGGGCGAGCACGACGAATTGGGTGATTTGATGGTATTTTAATGAAA
CATTCGCTACGAATTAGTGGTTATACTAGTATGGCAATTATGTTATTAGATGTTTTAACT
ACTATTAAGGAATTAAAAATTTGTGTTGGATATGAATATCAGGGGCAACAAATTGATTAT
GTTCCAAGTACAATTAAAGAATATGAGATGTGTAAACCAATTTTAATAACAATGCCGGGA
TGAGATGAAGACATTAGTAATGTTACAACATTTGAAGGTTTACCACATAATGCCCAACAA
TATTTAATGAAATTAGAAGAAATTGTTGGTGTTCCAATTAGTTTATTTTCTGTTGGTCCT
GATCGTGAACAAACTATTTTAATGAATAAGGAGATTTTTTAA


>protein sequence
MSGTNYRTLAIVGSQWGDEGKGKITDYFAQQADVIVRWAGGDNAGHTIVIKGTKYKLSIV
PSGVFNKKSMNVIGNGCVVNLRKLVSEISYLQEHGFDCKNLRISDRAHLIFPYHMKIDEL
QEEYRQKDSIGTTKKGIGPCYQDKAERIGIRLGDLFDEKGFLQKLENNLKFKNEVLTKVF
NSKGFDPKLIWKEYLALFQQIKSLVTDTSILVDNAIHTHQKVLFEGAQGVMLDLDHGTYP
FVTSSNPTASSIPVGVGIAPRYINNVLGIVKAYNTRVGTGPFPSEIFGEVETYIREAGHE
YGTVSGRARRIGWFDGILMKHSLRISGYTSMAIMLLDVLTTIKELKICVGYEYQGQQIDY
VPSTIKEYEMCKPILITMPGWDEDISNVTTFEGLPHNAQQYLMKLEEIVGVPISLFSVGP
DREQTILMNKEIF






















© Fisunov Lab of Proteomics, 2016.