UniProt Accession

 PURA_ECOLI; P0A7D4; P12283; Q2M6C8 

Genbank Protein ID

 J04199; U14003; U00096; AP009048 

Genbank Nucleotide ID

 AAA24446.1; AAA97073.1; AAC77134.1; BAE78178.1 

Protein Name

 Adenylosuccinate synthetase 

Protein Synonyms/Alias

 AMPSase; AdSS; IMP--aspartate ligase 

Gene Name

 purA 

Gene Synonyms/Alias

 adeK; b4177; JW4135 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
19	WGDEGKGKIVDLLTE	acetylation	[1]
50	TLVINGEKTVLHLIP	acetylation	[1]
82	LSPAALMKEMKELED	acetylation	[1, 2]
85	AALMKEMKELEDRGI	acetylation	[1]
141	IGPAYEDKVARRGLR	acetylation	[1]
155	RVGDLFDKETFAEKL	acetylation	[1]
161	DKETFAEKLKEVMEY	acetylation	[1]
163	ETFAEKLKEVMEYHN	acetylation	[1]
178	FQLVNYYKAEAVDYQ	acetylation	[1]
268	DYVLGILKAYSTRVG	acetylation	[1]
293	ETGEFLCKQGNEFGA	acetylation	[1]
332	LSGFCLTKLDVLDGL	acetylation	[1]
340	LDVLDGLKEVKLCVA	acetylation	[1, 2]
343	LDGLKEVKLCVAYRM	acetylation	[1]
367	PLAADDWKGVEPIYE	acetylation	[1]
387	SESTFGVKDRSGLPQ	acetylation	[1]
401	QAALNYIKRIEELTG	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 

Functional Description

 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 (By similarity). 

Sequence Annotation

 NP_BIND 13 19 GTP.
 NP_BIND 41 43 GTP.
 NP_BIND 332 334 GTP.
 NP_BIND 415 417 GTP.
 REGION 14 17 IMP binding.
 REGION 39 42 IMP binding.
 REGION 300 306 Substrate binding.
 ACT_SITE 14 14 Proton acceptor.
 ACT_SITE 42 42 Proton donor.
 METAL 14 14 Magnesium.
 METAL 41 41 Magnesium; via carbonyl oxygen.
 BINDING 130 130 IMP.
 BINDING 144 144 IMP; shared with dimeric partner.
 BINDING 225 225 IMP.
 BINDING 240 240 IMP.
 BINDING 304 304 IMP.
 BINDING 306 306 GTP.  

Keyword

 3D-structure; 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

 432 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0004019; F:adenylosuccinate synthase activity; IDA:EcoCyc.
 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:0046086; P:adenosine biosynthetic process; IMP:EcoliWiki.
 GO:0015949; P:nucleobase-containing small molecule interconversion; IDA:EcoliWiki.
 GO:0006164; P:purine nucleotide biosynthetic process; IMP:EcoCyc.
 GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki. 

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