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 16238 |
42111 42111 |
15846 15846 |
32816 32816 |
16908 16908 |
||||||
PubChem |
643975 643975 |
61503 61503 |
5893 5893 |
1060 1060 |
439153 439153 |
||||||
1f0xA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1f0xB01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1f0xA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1f0xB02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1f0xA03 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||||||
1f0xB03 | Bound:FAD | Unbound | Unbound | Unbound | Unbound | ||||||
1f0xA04 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1f0xB04 | 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 | ||||||||||
1f0xB01 | ||||||||||
1f0xA02 | ||||||||||
1f0xB02 | ||||||||||
1f0xA03 | ||||||||||
1f0xB03 | ||||||||||
1f0xA04 | ||||||||||
1f0xB04 |
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. |
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. |
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, |
Related PDB | 1f0x |
Related UniProtKB | P06149 |
Comments |
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Created | Updated |
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2004-03-25 | 2009-02-26 |