DB code: M00001

CATH domain 3.30.70.610 : Alpha-Beta Plaits
3.30.43.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2
3.30.465.20 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 Catalytic domain
3.30.1370.20 : Ribosomal Protein S8; Chain
E.C. 1.1.1.28
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.30.43.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2 M00004 M00039 M00179 T00003
3.30.465.20 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 M00004 M00179

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P06149 D-lactate dehydrogenase
EC 1.1.1.28
Respiratory D-lactate dehydrogenase
NP_416637.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_490372.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF01565 (FAD_binding_4)
PF09330 (Lact-deh-memb)
[Graphical View]

KEGG enzyme name
D-lactate dehydrogenase
lactic acid dehydrogenase
lactic acid dehydrogenase
D-specific lactic dehydrogenase
D-(-)-lactate dehydrogenase (NAD+)
D-lactic acid dehydrogenase
D-lactic dehydrogenase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P06149 DLD_ECOLI (R)-lactate + NAD(+) = pyruvate + NADH. Cell membrane, Peripheral membrane protein, Cytoplasmic side. FAD.

KEGG Pathways
Map code Pathways E.C.
MAP00620 Pyruvate metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00016 C00256 C00003 C00022 C00004
E.C.
Compound FAD (R)-Lactate NAD+ Pyruvate NADH
Type amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide carbohydrate,carboxyl group amide group,amine group,nucleotide carbohydrate,carboxyl group amide group,amine group,nucleotide
ChEBI 16238
42111
15846
32816
16908
PubChem 643975
61503
5893
1060
439153
1f0xA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1f0xB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1f0xA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1f0xB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1f0xA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1f0xB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:FAD Unbound Unbound Unbound Unbound
1f0xA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1f0xB04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1f0xA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f0xB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f0xA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f0xB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f0xA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f0xB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f0xA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1f0xB04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[9]
p.9415

References
[1]
Resource
Comments
Medline ID
PubMed ID 4565667
Journal J Biol Chem
Year 1972
Volume 247
Pages 7858-63
Authors Walsh CT, Abeles RH, Kaback HR
Title Mechanisms of active transport in isolated bacterial membrane vesicles. X. Inactivation of D-lactate dehydrogenase and D-lactate dehydrogenase-coupled transport in Escherichia coli membrane vesicles by an acetylenic substrate.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 4582730
Journal J Biol Chem
Year 1973
Volume 248
Pages 7012-7
Authors Kohn LD, Kaback HR
Title Mechanisms of active transport in isolated bacterial membrane vesicles. XV. Purification and properties of the membrane-bound D-lactate dehydrogenase from.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 7026558
Journal J Biol Chem
Year 1981
Volume 256
Pages 10369-74
Authors Kovatchev S, Vaz WL, Eibl H
Title Lipid dependence of the membrane-bound D-lactate dehydrogenase of Escherichia coli.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 3548821
Journal Biochemistry
Year 1987
Volume 26
Pages 549-56
Authors Rule GS, Pratt EA, Simplaceanu V, Ho C
Title Nuclear magnetic resonance and molecular genetic studies of the membrane-bound D-lactate dehydrogenase of Escherichia coli.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 2185834
Journal Biochemistry
Year 1990
Volume 29
Pages 3256-62
Authors Peersen OB, Pratt EA, Truong HT, Ho C, Rule GS
Title Site-specific incorporation of 5-fluorotryptophan as a probe of the structure and function of the membrane-bound D-lactate dehydrogenase of Escherichia coli: a 19F nuclear magnetic resonance study.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 1850292
Journal Biochemistry
Year 1991
Volume 30
Pages 3893-8
Authors Truong HT, Pratt EA, Ho C
Title Interaction of the membrane-bound D-lactate dehydrogenase of Escherichia coli with phospholipid vesicles and reconstitution of activity using a spin-labeled fatty acid as an electron acceptor: a magnetic resonance and biochemical study.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 1931992
Journal Biochemistry
Year 1991
Volume 30
Pages 10722-9
Authors Truong HT, Pratt EA, Rule GS, Hsue PY, Ho C
Title Inactive and temperature-sensitive folding mutants generated by tryptophan substitutions in the membrane-bound d-lactate dehydrogenase of Escherichia coli.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 8987983
Journal Biochemistry
Year 1996
Volume 35
Pages 16502-9
Authors Sun ZY, Pratt EA, Simplaceanu V, Ho C
Title A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydrogenase of Escherichia coli.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID 20402548
PubMed ID 10944213
Journal Proc Natl Acad Sci U S A
Year 2000
Volume 97
Pages 9413-8
Authors Dym O, Pratt EA, Ho C, Eisenberg D
Title The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme.
Related PDB 1f0x
Related UniProtKB P06149

Comments

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