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 |
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| 1f0xA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1f0xB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1f0xA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1f0xB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1f0xA03 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | |
| 1f0xB03 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | |
| 1f0xA04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1f0xB04 |
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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 |
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| 1f0xB01 |
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| 1f0xA02 |
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| 1f0xB02 |
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| 1f0xA03 |
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| 1f0xB03 |
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| 1f0xA04 |
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| 1f0xB04 |
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| 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 |
|---|
| Created | Updated |
|---|---|
| 2004-03-25 | 2009-02-26 |