DB code: D00031
CATH domain | 3.40.50.1770 : Rossmann fold | Catalytic domain |
---|---|---|
3.40.50.720 : Rossmann fold | Catalytic domain | |
E.C. | 1.4.1.1 | |
CSA | 1pjb | |
M-CSA | 1pjb | |
MACiE | M0067 |
CATH domain | Related DB codes (homologues) |
---|---|
3.40.50.1770 : Rossmann fold | M00161 |
3.40.50.720 : Rossmann fold | S00543 S00551 S00552 S00553 S00602 S00604 S00605 S00608 S00610 S00625 S00319 S00328 S00329 S00330 S00331 S00332 D00456 D00457 D00458 S00324 S00320 S00325 S00326 S00327 D00459 S00335 S00336 S00334 T00219 S00339 D00513 D00001 D00002 D00003 D00005 D00007 D00008 D00010 D00012 D00017 D00018 D00023 D00027 D00028 D00032 D00033 D00034 D00035 D00037 D00048 D00071 D00476 D00481 D00482 D00490 D00492 D00494 D00545 D00601 D00603 D00604 D00605 D00615 D00845 D00857 D00858 M00161 M00171 M00210 T00002 T00010 T00011 T00015 T00227 T00247 T00408 T00414 D00827 D00262 D00274 D00275 M00035 T00109 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
---|---|---|---|
O52942 |
|
Alanine dehydrogenase
EC 1.4.1.1 |
PF01262
(AlaDh_PNT_C)
PF05222 (AlaDh_PNT_N) [Graphical View] |
KEGG enzyme name |
---|
alanine dehydrogenase
AlaDH L-alanine dehydrogenase NAD+-linked alanine dehydrogenase alpha-alanine dehydrogenase NAD+-dependent alanine dehydrogenase alanine oxidoreductase NADH-dependent alanine dehydrogenase |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
O52942 | O52942_PHOLP |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00430 | Taurine and hypotaurine metabolism | |
MAP00720 | Reductive carboxylate cycle (CO2 fixation) |
Compound table | |||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | |||||||||||
KEGG-id | C00041 | C00001 | C00003 | C00022 | C00014 | C00004 | C00080 | ||||||
E.C. | |||||||||||||
Compound | L-Alanine | H2O | NAD+ | Pyruvate | NH3 | NADH | H+ | ||||||
Type | amino acids | H2O | amide group,amine group,nucleotide | carbohydrate,carboxyl group | amine group,organic ion | amide group,amine group,nucleotide | others | ||||||
ChEBI |
16977 57972 16977 57972 |
15377 15377 |
15846 15846 |
32816 32816 |
16134 16134 |
16908 16908 |
15378 15378 |
||||||
PubChem |
5950 7311724 5950 7311724 |
22247451 962 22247451 962 |
5893 5893 |
1060 1060 |
222 222 |
439153 439153 |
1038 1038 |
||||||
1pjbA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1pjcA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1sayA01 | Unbound | Unbound | Bound:PYR | Unbound | Unbound | ||||||||
1pjbA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1pjcA02 | Unbound | Bound:NAD | Unbound | Unbound | Unbound | ||||||||
1sayA02 | Unbound | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
literature [2] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1pjbA01 | LYS 74;HIS 95;GLU 117 | |||||||||
1pjcA01 | LYS 74;HIS 95;GLU 117 | |||||||||
1sayA01 | LYS 74;HIS 95;GLU 117 | |||||||||
1pjbA02 | ASP 269 | |||||||||
1pjcA02 | ASP 269 | |||||||||
1sayA02 | ASP 269 |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[2]
|
p.563-564, Fig.3 | 3 |
References | |
---|---|
[1] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 7896761 |
Journal | J Biochem (Tokyo) |
Year | 1994 |
Volume | 116 |
Pages | 995-1000 |
Authors | Sawa Y, Tani M, Murata K, Shibata H, Ochiai H |
Title |
Purification and characterization of alanine dehydrogenase from a cyanobacterium, |
Related PDB | 1pjc |
Related UniProtKB | |
[2] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 9665169 |
Journal | Nat Struct Biol |
Year | 1998 |
Volume | 5 |
Pages | 561-7 |
Authors | Baker PJ, Sawa Y, Shibata H, Sedelnikova SE, Rice DW |
Title | Analysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase. |
Related PDB | 1say 1pjb |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10611473 |
Journal | FEBS Lett |
Year | 1999 |
Volume | 464 |
Pages | 1-8 |
Authors | Jackson JB, Peake SJ, White SA |
Title | Structure and mechanism of proton-translocating transhydrogenase. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10385325 |
Journal | Nat Biotechnol |
Year | 1999 |
Volume | 17 |
Pages | 588-92 |
Authors | Hols P, Kleerebezem M, Schanck AN, Ferain T, Hugenholtz J, Delcour J, de Vos WM |
Title | Conversion of Lactococcus lactis from homolactic to homoalanine fermentation through metabolic engineering. |
Related PDB | |
Related UniProtKB | |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11041346 |
Journal | Arch Microbiol |
Year | 2000 |
Volume | 174 |
Pages | 162-7 |
Authors | Laue H, Cook AM |
Title |
Purification, |
Related PDB | |
Related UniProtKB |
Comments |
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Created | Updated |
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2004-03-16 | 2009-09-28 |