UniProt Accession

 PAND_ECOLI; P0A790; P31664; Q8KMY8 

Genbank Protein ID

 L17086; U00096; AP009048 

Genbank Nucleotide ID

 AAA24274.1; AAC73242.1; BAB96708.2 

Protein Name

 Aspartate 1-decarboxylase 

Protein Synonyms/Alias

 Aspartate alpha-decarboxylase; Aspartate 1-decarboxylase beta chain; Aspartate 1-decarboxylase alpha chain 

Gene Name

 panD 

Gene Synonyms/Alias

 b0131; JW0127 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
9	IRTMLQGKLHRVKVT	acetylation	[1]
115	FEGDNEMKRTAKAIP	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] 

Functional Description

 Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. 

Sequence Annotation

 REGION 73 75 Substrate binding (By similarity).
 ACT_SITE 25 25 Schiff-base intermediate with substrate;
 ACT_SITE 58 58 Proton donor.
 BINDING 57 57 Substrate (By similarity).
 MOD_RES 25 25 Pyruvic acid (Ser).  

Keyword

 3D-structure; Autocatalytic cleavage; Complete proteome; Cytoplasm; Decarboxylase; Direct protein sequencing; Lyase; Pantothenate biosynthesis; Pyruvate; Reference proteome; Schiff base; Zymogen. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 126 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004068; F:aspartate 1-decarboxylase activity; IEA:HAMAP.
 GO:0006523; P:alanine biosynthetic process; IEA:InterPro.
 GO:0015940; P:pantothenate biosynthetic process; IEA:HAMAP.
 GO:0016540; P:protein autoprocessing; IDA:EcoCyc. 

Interpro

 IPR009010; Asp_de-COase-like_dom.
 IPR003190; Asp_decarbox. 

Pfam

 PF02261; Asp_decarbox 

SMART

  

PROSITE

  

PRINTS