EzCatDB: S00101
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DB codeS00101
CATH domainDomain 12.40.40.20 : Barwin-like endoglucanasesCatalytic domain
E.C.4.1.1.11
CSA1aw8

CATH domainRelated DB codes (homologues)
2.40.40.20 : Barwin-like endoglucanasesM00007

Enzyme Name
UniProtKBKEGG

P0A790
Protein nameAspartate 1-decarboxylaseaspartate 1-decarboxylase
aspartate alpha-decarboxylase
L-aspartate alpha-decarboxylase
aspartic alpha-decarboxylase
L-aspartate 1-carboxy-lyase
SynonymsEC 4.1.1.11
Aspartate alpha-decarboxylase
ContainsAspartate 1-decarboxylase beta chain
Aspartate 1-decarboxylase alpha chain
RefSeqNP_414673.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_488434.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PfamPF02261 (Asp_decarbox)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00252Alanine and aspartate metabolism
MAP00410beta-Alanine metabolism

UniProtKB:Accession NumberP0A790
Entry namePAND_ECOLI
ActivityL-aspartate = beta-alanine + CO(2).
SubunitHeterooctamer of four alpha and four beta subunits.
Subcellular locationCytoplasm.
CofactorPyruvoyl group.

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00049C00011C00099
CompoundL-AspartateCO2beta-Alanine
Typeamino acids,carboxyl groupothersamino acids
ChEBI17053
16526
16958
57966
PubChem5960
44367445
280
4755801
239
           
1aw8AUnboundUnboundUnbound
1aw8DUnboundUnboundUnbound
1aw8BUnboundUnboundUnbound
1aw8EUnboundUnboundUnbound

Active-site residues
resource
PDB;1aw8 & Swiss-prot;P0A790 & literature;[1],[2],[5]
pdbCatalytic residuesModified residues
          
1aw8ALYS 9
 
1aw8DLYS 9
 
1aw8BTYR 58
PYR 25(Pyruvoyl Ser)
1aw8ETYR 58
PYR 25(Pyruvoyl Ser)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Scheme 2, p.3122
[2]Fig.1b, p.290-291
[5]Scheme 1p.1760

references
[1]
PubMed ID9765870
JournalBiochem Soc Trans
Year1998
Volume26
Pages310-5
AuthorsAbell C
TitleEnzymes that exploit imines--one way or the other.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Medline ID98206295
PubMed ID9546220
JournalNat Struct Biol
Year1998
Volume5
Pages289-93
AuthorsAlbert A, Dhanaraj V, Genschel U, Khan G, Ramjee MK, Pulido R, Sibanda BL, von Delft F, Witty M, Blundell TL, Smith AG, Abell C
TitleCrystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing.
Related PDB1aw8
Related UniProtKBP0A790
[3]
PubMed ID10368289
JournalStructure Fold Des
Year1999
Volume7
Pages227-36
AuthorsCastillo RM, Mizuguchi K, Dhanaraj V, Albert A, Blundell TL, Murzin AG
TitleA six-stranded double-psi beta barrel is shared by several protein superfamilies.
[4]
PubMed ID10610264
JournalStructure Fold Des
Year1999
Volume7
PagesR215-6
AuthorsMizuguchi K, Dhanaraj V, Blundell TL, Murzin AG
TitleN-ethylmaleimide-sensitive fusion protein (NSF) and CDC48 confirmed as members of the double-psi beta-barrel aspartate decarboxylase/formate dehydrogenase family.
[5]
PubMed ID12240302
JournalChem Commun (Camb)
Year2001
Volume(18)
Pages1760-1
AuthorsSaldanha SA, Birch LM, Webb ME, Nabbs BK, von Delft F, Smith AG, Abell C
TitleIdentification of Tyr58 as the proton donor in the aspartate-alpha-decarboxylase reaction.
[6]
PubMed ID12182836
JournalProtein Expr Purif
Year2002
Volume25
Pages533-40
AuthorsChopra S, Pai H, Ranganathan A
TitleExpression, purification, and biochemical characterization of Mycobacterium tuberculosis aspartate decarboxylase, PanD.


createdupdated
2004-03-252009-02-26
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Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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