DB code: S00101

CATH domain 2.40.40.20 : Barwin-like endoglucanases Catalytic domain
E.C. 4.1.1.11
CSA 1aw8
M-CSA 1aw8
MACiE

CATH domain Related DB codes (homologues)
2.40.40.20 : Barwin-like endoglucanases M00007

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains RefSeq Pfam
P0A790 Aspartate 1-decarboxylase
EC 4.1.1.11
Aspartate alpha-decarboxylase
Aspartate 1-decarboxylase beta chain
Aspartate 1-decarboxylase alpha chain
NP_414673.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_488434.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF02261 (Asp_decarbox)
[Graphical View]

KEGG enzyme name
aspartate 1-decarboxylase
aspartate alpha-decarboxylase
L-aspartate alpha-decarboxylase
aspartic alpha-decarboxylase
L-aspartate 1-carboxy-lyase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0A790 PAND_ECOLI L-aspartate = beta-alanine + CO(2). Heterooctamer of four alpha and four beta subunits. Cytoplasm. Pyruvoyl group.

KEGG Pathways
Map code Pathways E.C.
MAP00252 Alanine and aspartate metabolism
MAP00410 beta-Alanine metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00049 C00011 C00099
E.C.
Compound L-Aspartate CO2 beta-Alanine
Type amino acids,carboxyl group others amino acids
ChEBI 17053
17053
16526
16526
16958
57966
16958
57966
PubChem 44367445
5960
44367445
5960
280
280
239
4755801
239
4755801
1aw8A Unbound Unbound Unbound
1aw8D Unbound Unbound Unbound
1aw8B Unbound Unbound Unbound
1aw8E Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1aw8 & Swiss-prot;P0A790 & literature;[1],[2],[5]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1aw8A LYS 9
1aw8D LYS 9
1aw8B TYR 58 PYR 25(Pyruvoyl Ser)
1aw8E TYR 58 PYR 25(Pyruvoyl Ser)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
Scheme 2, p.312 2
[2]
Fig.1b, p.290-291
[5]
Scheme 1 p.1760

References
[1]
Resource
Comments
Medline ID
PubMed ID 9765870
Journal Biochem Soc Trans
Year 1998
Volume 26
Pages 310-5
Authors Abell C
Title Enzymes that exploit imines--one way or the other.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Medline ID 98206295
PubMed ID 9546220
Journal Nat Struct Biol
Year 1998
Volume 5
Pages 289-93
Authors Albert A, Dhanaraj V, Genschel U, Khan G, Ramjee MK, Pulido R, Sibanda BL, von Delft F, Witty M, Blundell TL, Smith AG, Abell C
Title Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing.
Related PDB 1aw8
Related UniProtKB P0A790
[3]
Resource
Comments
Medline ID
PubMed ID 10368289
Journal Structure Fold Des
Year 1999
Volume 7
Pages 227-36
Authors Castillo RM, Mizuguchi K, Dhanaraj V, Albert A, Blundell TL, Murzin AG
Title A six-stranded double-psi beta barrel is shared by several protein superfamilies.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 10610264
Journal Structure Fold Des
Year 1999
Volume 7
Pages R215-6
Authors Mizuguchi K, Dhanaraj V, Blundell TL, Murzin AG
Title N-ethylmaleimide-sensitive fusion protein (NSF) and CDC48 confirmed as members of the double-psi beta-barrel aspartate decarboxylase/formate dehydrogenase family.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 12240302
Journal Chem Commun (Camb)
Year 2001
Volume (18)
Pages 1760-1
Authors Saldanha SA, Birch LM, Webb ME, Nabbs BK, von Delft F, Smith AG, Abell C
Title Identification of Tyr58 as the proton donor in the aspartate-alpha-decarboxylase reaction.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 12182836
Journal Protein Expr Purif
Year 2002
Volume 25
Pages 533-40
Authors Chopra S, Pai H, Ranganathan A
Title Expression, purification, and biochemical characterization of Mycobacterium tuberculosis aspartate decarboxylase, PanD.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-03-25 2009-02-26