EzCatDB: D00031
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DB codeD00031
CATH domainDomain 13.40.50.1770 : Rossmann foldCatalytic domain
Domain 23.40.50.720 : Rossmann foldCatalytic domain
E.C.1.4.1.1
CSA1pjb
MACiEM0067

CATH domainRelated DB codes (homologues)
3.40.50.1770 : Rossmann foldM00161
3.40.50.720 : Rossmann foldS00543,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

Enzyme Name
UniProtKBKEGG

O52942
Protein name
alanine dehydrogenase
AlaDH
L-alanine dehydrogenase
NAD+-linked alanine dehydrogenase
alpha-alanine dehydrogenase
NAD+-dependent alanine dehydrogenase
alanine oxidoreductase
NADH-dependent alanine dehydrogenase
SynonymsAlanine dehydrogenase
EC 1.4.1.1
PfamPF01262 (AlaDh_PNT_C)
PF05222 (AlaDh_PNT_N)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00430Taurine and hypotaurine metabolism
MAP00720Reductive carboxylate cycle (CO2 fixation)

UniProtKB:Accession NumberO52942
Entry nameO52942_PHOLP
Activity
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00041C00001C00003C00022C00014C00004C00080
CompoundL-AlanineH2ONAD+PyruvateNH3NADHH+
Typeamino acidsH2Oamide group,amine group,nucleotidecarbohydrate,carboxyl groupamine group,organic ionamide group,amine group,nucleotideothers
ChEBI16977
57972
15377
15846
32816
16134
16908
15378
PubChem7311724
5950
962
22247451
5893
1060
222
439153
1038
               
1pjbA01Unbound UnboundUnboundUnboundUnbound 
1pjcA01Unbound UnboundUnboundUnboundUnbound 
1sayA01Unbound UnboundBound:PYRUnboundUnbound 
1pjbA02Unbound UnboundUnboundUnboundUnbound 
1pjcA02Unbound Bound:NADUnboundUnboundUnbound 
1sayA02Unbound UnboundUnboundUnboundUnbound 

Active-site residues
resource
literature [2]
pdbCatalytic residues
         
1pjbA01LYS 74;HIS 95;GLU 117
1pjcA01LYS 74;HIS 95;GLU 117
1sayA01LYS 74;HIS 95;GLU 117
1pjbA02ASP 269
1pjcA02ASP 269
1sayA02ASP 269

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.563-564, Fig.33

references
[1]
CommentsX-ray crystallography
PubMed ID7896761
JournalJ Biochem (Tokyo)
Year1994
Volume116
Pages995-1000
AuthorsSawa Y, Tani M, Murata K, Shibata H, Ochiai H
TitlePurification and characterization of alanine dehydrogenase from a cyanobacterium, Phormidium lapideum.
Related PDB1pjc
[2]
CommentsX-ray crystallography
PubMed ID9665169
JournalNat Struct Biol
Year1998
Volume5
Pages561-7
AuthorsBaker PJ, Sawa Y, Shibata H, Sedelnikova SE, Rice DW
TitleAnalysis of the structure and substrate binding of Phormidium lapideum alanine dehydrogenase.
Related PDB1say,1pjb
[3]
PubMed ID10611473
JournalFEBS Lett
Year1999
Volume464
Pages1-8
AuthorsJackson JB, Peake SJ, White SA
TitleStructure and mechanism of proton-translocating transhydrogenase.
[4]
PubMed ID10385325
JournalNat Biotechnol
Year1999
Volume17
Pages588-92
AuthorsHols P, Kleerebezem M, Schanck AN, Ferain T, Hugenholtz J, Delcour J, de Vos WM
TitleConversion of Lactococcus lactis from homolactic to homoalanine fermentation through metabolic engineering.
[5]
PubMed ID11041346
JournalArch Microbiol
Year2000
Volume174
Pages162-7
AuthorsLaue H, Cook AM
TitlePurification, properties and primary structure of alanine dehydrogenase involved in taurine metabolism in the anaerobe Bilophila wadsworthia.


createdupdated
2004-03-162009-09-28


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