UniProt Accession

 PUR8_ECOLI; P0AB89; P25739 

Genbank Protein ID

 M74924; X59307; U00096; AP009048 

Genbank Nucleotide ID

 AAA92731.1; CAA41996.1; AAC74215.1; BAA35953.1 

Protein Name

 Adenylosuccinate lyase 

Protein Synonyms/Alias

 ASL; Adenylosuccinase; ASase 

Gene Name

 purB 

Gene Synonyms/Alias

 b1131; JW1117 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
19	VDGRYGDKVSALRGI	acetylation	[1]
34	FSEYGLLKFRVQVEV	acetylation	[1]
46	VEVRWLQKLAAHAAI	acetylation	[1]
94	RTTNHDVKAVEYFLK	acetylation	[1, 2]
101	KAVEYFLKEKVAEIP	acetylation	[1]
155	RQLIDGIKDLAVQYR	acetylation	[1]
182	ATPSTIGKEMANVAY	acetylation	[1]
285	YIALNHFKQKTIAGE	acetylation	[1]
301	GSSTMPHKVNPIDFE	acetylation	[1]
327	VLQHLASKLPVSRWQ	acetylation	[1]
362	IAYQSTLKGVSKLEV	acetylation	[1]
366	STLKGVSKLEVNRDH	acetylation	[1, 2]
400	MRRYGIEKPYEKLKE	acetylation	[1]
404	GIEKPYEKLKELTRG	acetylation	[1]
406	EKPYEKLKELTRGKR	acetylation	[1]
412	LKELTRGKRVDAEGM	acetylation	[1]
420	RVDAEGMKQFIDGLA	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] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842] 

Functional Description

  

Sequence Annotation

 REGION 15 16 Substrate binding.
 REGION 90 92 Substrate binding.
 REGION 122 123 Substrate binding.
 REGION 301 303 Substrate binding.
 REGION 340 344 Substrate binding.
 ACT_SITE 171 171 Proton donor/acceptor.
 ACT_SITE 295 295 Proton donor/acceptor.
 BINDING 247 247 Substrate.
 BINDING 309 309 Substrate.
 BINDING 335 335 Substrate.
 BINDING 340 340 Substrate (By similarity).
 MOD_RES 94 94 N6-acetyllysine.
 MOD_RES 366 366 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Lyase; Purine biosynthesis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 456 AA 

Protein Sequence

Gene Ontology

 GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity; IEA:EC.
 GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IDA:EcoCyc.
 GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki. 

Interpro

 IPR013539; AdenyloSucc_lyase_C_pln.
 IPR024083; Fumarase/histidase_N.
 IPR000362; Fumarate_lyase.
 IPR020557; Fumarate_lyase_CS.
 IPR022761; Fumarate_lyase_N.
 IPR008948; L-Aspartase-like.
 IPR004769; Pur_lyase. 

Pfam

 PF08328; ASL_C
 PF00206; Lyase_1 

SMART

  

PROSITE

 PS00163; FUMARATE_LYASES 

PRINTS

 PR00149; FUMRATELYASE.