| Tag | Content |
|---|
| CPLM ID | CPLM-010444 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Adenylosuccinate synthetase |
Protein Synonyms/Alias | AMPSase; AS-synthetase; AdSS; IMP--aspartate ligase |
Gene Name | ADE12 |
Gene Synonyms/Alias | YNL220W; N1290 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 25 | LVDLLVGKYDIVARC | acetylation | [1] | | 392 | QDITKITKYEDLPEN | acetylation | [1] |
|
Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | 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. |
Sequence Annotation | NP_BIND 11 17 GTP (By similarity).
NP_BIND 39 41 GTP (By similarity).
NP_BIND 337 339 GTP (By similarity).
NP_BIND 419 421 GTP (By similarity).
REGION 12 15 IMP binding (By similarity).
REGION 37 40 IMP binding (By similarity).
REGION 305 311 Substrate binding (By similarity).
ACT_SITE 12 12 Proton acceptor (By similarity).
ACT_SITE 40 40 Proton donor (By similarity).
METAL 12 12 Magnesium (By similarity).
METAL 39 39 Magnesium; via carbonyl oxygen (By
BINDING 134 134 IMP (By similarity).
BINDING 148 148 IMP; shared with dimeric partner (By
BINDING 230 230 IMP (By similarity).
BINDING 245 245 IMP (By similarity).
BINDING 309 309 IMP (By similarity).
BINDING 311 311 GTP (By similarity). |
Keyword | Complete proteome; Cytoplasm; Direct protein sequencing; GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 433 AA |
Protein Sequence | MVNVVLGSQW GDEGKGKLVD LLVGKYDIVA RCAGGNNAGH TIVVDGVKYD FHMLPSGLVN 60
PNCQNLLGNG VVIHVPSFFK ELETLEAKGL KNARSRLFVS SRAHLVFDFH QVTDKLRELE 120
LSGRSKDGKN IGTTGKGIGP TYSTKASRSG LRVHHLVNDQ PGAWEEFVAR YKRLLETRRQ 180
RYGDFEYDFE AKLAEYKKLR EQLKPFVVDS VVFMHNAIEA KKKILVEGAN ALMLDIDFGT 240
YPYVTSSNTG IGGVLTGLGI PPRTIDEIYG VVKAYTTRVG EGPFPTEQLN ENGEKLQTIG 300
AEFGVTTGRK RRCGWLDLVV LKYSTLINGY TSLNITKLDV LDTFKEIPVG ISYSIQGKKL 360
DLFPEDLNIL GKVEVEYKVL PGWDQDITKI TKYEDLPENA KKYLKYIEDF VGVPVEWVGT 420
GPARESMLHK EIK 433 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:SGD. GO:0004019; F:adenylosuccinate synthase activity; IDA:SGD. GO:0003688; F:DNA replication origin binding; IDA:SGD. GO:0005525; F:GTP binding; IEA:HAMAP. GO:0000287; F:magnesium ion binding; IEA:HAMAP. GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway. GO:0006164; P:purine nucleotide biosynthetic process; IMP:SGD. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |