DB code: S00197

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 18420	17305 17305	32816 32816	16992 16992
PubChem	888 888	440165 440165	1060 1060	1122 1122

1dxeA	Bound:_MG	Unbound	Unbound	Unbound
1dxeB	Bound:_MG	Unbound	Unbound	Unbound
1dxfA	Bound:_MG	Unbound	Bound:PYR	Unbound
1dxfB	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	HIS 50;ARG 75	GLU 153;ASP 179(Magnesium binding)
1dxeB	HIS 50;ARG 75	GLU 153;ASP 179(Magnesium binding)
1dxfA	HIS 50;ARG 75	GLU 153;ASP 179(Magnesium binding)
1dxfB	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