CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
130IDSIQETKKLKEGKQacetylation[1]
131DSIQETKKLKEGKQIacetylation[1]
133IQETKKLKEGKQIGTacetylation[1]
136TKKLKEGKQIGTTKRacetylation[1]
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. 
Interpro
 IPR018220; Adenylosuccinate_synthase_AS.
 IPR001114; Adenylosuccinate_synthetase.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00709; Adenylsucc_synt 
SMART
 SM00788; Adenylsucc_synt 
PROSITE
 PS01266; ADENYLOSUCCIN_SYN_1
 PS00513; ADENYLOSUCCIN_SYN_2 
PRINTS