Tag | Content |
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CPLM ID | CPLM-016932 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Adenylosuccinate synthetase |
Protein Synonyms/Alias | AMPSase; AdSS; IMP--aspartate ligase |
Gene Name | Adss |
Gene Synonyms/Alias | PF13_0287 |
Created Date | July 27, 2013 |
Organism | Plasmodium falciparum (isolate 3D7) |
NCBI Taxa ID | 36329 |
Lysine Modification | Position | Peptide | Type | References |
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130 | IDSIQETKKLKEGKQ | acetylation | [1] | 131 | DSIQETKKLKEGKQI | acetylation | [1] | 133 | IQETKKLKEGKQIGT | acetylation | [1] | 136 | TKKLKEGKQIGTTKR | acetylation | [1] |
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Reference | [1] Extensive lysine acetylation occurs in evolutionarily conserved metabolic pathways and parasite-specific functions during Plasmodium falciparum intraerythrocytic development. Miao J, Lawrence M, Jeffers V, Zhao F, Parker D, Ge Y, Sullivan WJ Jr, Cui L. Mol Microbiol. 2013 Aug;89(4):660-75. [ PMID: 23796209] |
Functional Description | Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity). |
Sequence Annotation | NP_BIND 25 31 GTP (By similarity). NP_BIND 53 55 GTP (By similarity). NP_BIND 339 341 GTP (By similarity). NP_BIND 425 427 GTP (By similarity). REGION 26 29 IMP binding (By similarity). REGION 51 54 IMP binding (By similarity). REGION 307 313 Substrate binding (By similarity). ACT_SITE 26 26 Proton acceptor (By similarity). ACT_SITE 54 54 Proton donor (By similarity). METAL 26 26 Magnesium (By similarity). METAL 53 53 Magnesium; via carbonyl oxygen (By BINDING 62 62 GTP (By similarity). BINDING 141 141 IMP (By similarity). BINDING 155 155 IMP; shared with dimeric partner (By BINDING 232 232 IMP (By similarity). BINDING 247 247 IMP (By similarity). BINDING 307 307 GTP (By similarity). BINDING 311 311 IMP (By similarity). BINDING 313 313 GTP (By similarity). |
Keyword | Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 442 AA |
Protein Sequence | MNIFDHQIKN VDKGNVVAIL GAQWGDEGKG KIIDMLSEYS DITCRFNGGA NAGHTISVND 60 KKYALHLLPC GVLYDNNISV LGNGMVIHVK SLMEEIESVG GKLLDRLYLS NKAHILFDIH 120 QIIDSIQETK KLKEGKQIGT TKRGIGPCYS TKASRIGIRL GTLKNFENFK NMYSKLIDHL 180 MDLYNITEYD KEKELNLFYN YHLKLRDRIV DVISFMNTNL ENNKKVLIEG ANAAMLDIDF 240 GTYPYVTSSC TTVGGVFSGL GIHHKKLNLV VGVVKSYLTR VGCGPFLTEL NNDVGQYLRE 300 KGHEYGTTTK RPRRCGWLDI PMLLYVKCIN SIDMINLTKL DVLSGLEEIL LCVNFKNKKT 360 GELLEKGCYP VEEEISEEYE PVYEKFSGWK EDISTCNEFD ELPENAKKYI LAIEKYLKTP 420 IVWIGVGPNR KNMIVKKNFN LN 442 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0004019; F:adenylosuccinate synthase activity; IEA:HAMAP. 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:0006167; P:AMP biosynthetic process; ISS:GeneDB_Pfalciparum. |
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Pfam | |
SMART | |
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