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| Annotation rule MF_00011 |
General rule information
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| Accession | MF_00011 |
| Dates | 1-JUN-2001 (Created) 10-JUN-2021 (Last updated, Version 51) |
| Name | Adenylosucc_synth |
| Scope | Bacteria
Archaea |
| Template | P0A7D4 (PURA_ECOLI) |
case <OC:Bacteria> or <OC:Archaea>
| Triggered by |
end case
Propagated annotation
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Identifier, protein and gene names
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| Identifier |
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| Protein name |
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| Gene name |
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Comments
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| 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 | RHEA:15753: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
EC 6.3.4.4 |
| Cofactor | Mg(2+) Note: Binds 1 Mg(2+) ion per subunit. |
| Pathway | Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. |
| Subunit | Homodimer. |
| Subcellular location | Cytoplasm. |
| Similarity | Belongs to the adenylosuccinate synthetase family. |
Keywords
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Gene Ontology
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GO:0004019; Molecular function: adenylosuccinate synthase activity.
GO:0005525; Molecular function: GTP binding.
GO:0000287; Molecular function: magnesium ion binding.
GO:0006164; Biological process: purine nucleotide biosynthetic process.
GO:0005737; Cellular component: cytoplasm.
GO:0005525; Molecular function: GTP binding.
GO:0000287; Molecular function: magnesium ion binding.
GO:0006164; Biological process: purine nucleotide biosynthetic process.
GO:0005737; Cellular component: cytoplasm.
Cross-references
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| Pfam | PF00709; Adenylsucc_synt; 1; |
| TIGRFAMs | TIGR00184; purA; 1; |
| PROSITE | PS01266; ADENYLOSUCCIN_SYN_1; 1; |
| PS00513; ADENYLOSUCCIN_SYN_2; 1; |
Features
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| From: PURA_ECOLI (P0A7D4) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| NP_BIND | 13 | 19 | GTP | G-D-E-[GA]-K-[GA]-x | ||||||||
| NP_BIND | 41 | 43 | GTP | G-H-x | ||||||||
| NP_BIND | 332 | 334 | GTP | x-x-D | ||||||||
| NP_BIND | 415 | 417 | GTP | x-x-[GS] | ||||||||
| REGION | 14 | 17 | IMP binding | D-E-[GA]-K | ||||||||
| REGION | 39 | 42 | IMP binding | N-[AS]-G-H | ||||||||
| REGION | 300 | 306 | Substrate binding | x-x-[ST]-x-[KR]-x-R | ||||||||
| ACT_SITE | 14 | 14 | Proton acceptor | D | ||||||||
| ACT_SITE | 42 | 42 | Proton donor | H | ||||||||
| METAL | 14 | 14 | Magnesium | D | ||||||||
| METAL | 41 | 41 | Magnesium; via carbonyl oxygen | G | ||||||||
| BINDING | 130 | 130 | IMP | T | ||||||||
| BINDING | 144 | 144 | IMP; shared with dimeric partner | [KR] | ||||||||
| BINDING | 225 | 225 | IMP | [QN] | ||||||||
| BINDING | 240 | 240 | IMP | T | ||||||||
| BINDING | 304 | 304 | IMP | [KR] | ||||||||
| BINDING | 306 | 306 | GTP | R | ||||||||
Additional information
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| Size range | 336-459 amino acids |
| Related rules | MF_03126 (PURA1 supersedes the current rule); MF_03127 (PURA2 supersedes the current rule); MF_04166 (PURZ supersedes the current rule) |
| Fusion | None |