DB code: S00197

CATH domain 3.20.20.60 : TIM Barrel Catalytic domain
E.C. 4.1.2.20
CSA 1dxe
M-CSA 1dxe
MACiE

CATH domain Related DB codes (homologues)
3.20.20.60 : TIM Barrel S00241 T00217 S00242 T00043 D00477

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P23522 5-keto-4-deoxy-D-glucarate aldolase
KDGluc aldolase
KDGlucA
EC 4.1.2.20
2-dehydro-3-deoxy-D-glucarate aldolase
2-keto-3-deoxy-D-glucarate aldolase
5-dehydro-4-deoxy-D-glucarate aldolase
Alpha-keto-beta-deoxy-D-glucarate aldolase
NP_417595.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491314.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF03328 (HpcH_HpaI)
[Graphical View]

KEGG enzyme name
2-dehydro-3-deoxyglucarate aldolase
2-keto-3-deoxyglucarate aldolase
alpha-keto-beta-deoxy-D-glucarate aldolase
2-dehydro-3-deoxy-D-glucarate tartronate-semialdehyde-lyase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P23522 GARL_ECOLI 5-dehydro-4-deoxy-D-glucarate = pyruvate + tartronate semialdehyde. 2-dehydro-3-deoxy-D-glucarate = pyruvate + tartronate semialdehyde. Homohexamer, trimer of dimers. Binds 1 magnesium ion per subunit. Can also use, although less efficiently, Co(2+), Fe(2+) and Mn(2+).

KEGG Pathways
Map code Pathways E.C.
MAP00053 Ascorbate and aldarate metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C03921 C00022 C01146
E.C.
Compound Magnesium 2-Dehydro-3-deoxy-D-glucarate Pyruvate Tartronate semialdehyde
Type divalent metal (Ca2+, Mg2+) carbohydrate,carboxyl group carbohydrate,carboxyl group carbohydrate,carboxyl group
ChEBI 18420
17305
32816
16992
PubChem 888
440165
1060
1122
1dxeA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Unbound Unbound
1dxeB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Unbound Unbound
1dxfA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Bound:PYR Unbound
1dxfB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:_MG Unbound Bound:PYR Unbound

Reference for Active-site residues
resource references E.C.
literature [3]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1dxeA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 50;ARG 75 GLU 153;ASP 179(Magnesium binding)
1dxeB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 50;ARG 75 GLU 153;ASP 179(Magnesium binding)
1dxfA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 50;ARG 75 GLU 153;ASP 179(Magnesium binding)
1dxfB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 50;ARG 75 GLU 153;ASP 179(Magnesium binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.3851-3852

References
[1]
Resource
Comments
Medline ID
PubMed ID 10393309
Journal Acta Crystallogr D Biol Crystallogr
Year 1999
Volume 55
Pages 1368-9
Authors Blackwell NC, Cullis PM, Cooper RA, Izard T
Title Rhombohedral crystals of 2-dehydro-3-deoxygalactarate aldolase from Escherichia coli.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 11053844
Journal Acta Crystallogr D Biol Crystallogr
Year 2000
Volume 56
Pages 1437-9
Authors Hendry EJ, Buchanan CL, Russell RJ, Hough DW, Reeve CD, Danson MJ, Taylor GL
Title Preliminary crystallographic studies of an extremely thermostable KDG aldolase from Sulfolobus solfataricus.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID 20380920
PubMed ID 10921867
Journal EMBO J
Year 2000
Volume 19
Pages 3849-56
Authors Izard T, Blackwell NC
Title Crystal structures of the metal-dependent 2-dehydro-3-deoxy-galactarate aldolase suggest a novel reaction mechanism.
Related PDB 1dxe 1dxf
Related UniProtKB P23522

Comments

Created Updated
2004-03-30 2009-03-19