EzCatDB: D00475
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DB codeD00475
CATH domainDomain 13.40.605.10 : Aldehyde Dehydrogenase; Chain A, domain 1Catalytic domain
Domain 23.40.309.10 : Aldehyde Dehydrogenase; Chain A, domain 2Catalytic domain
E.C.1.2.1.4

CATH domainRelated DB codes (homologues)
3.40.309.10 : Aldehyde Dehydrogenase; Chain A, domain 2D00020,D00021,D00022,D00614
3.40.605.10 : Aldehyde Dehydrogenase; Chain A, domain 1D00020,D00021,D00022,D00614

Enzyme Name
UniProtKBKEGG

Q56694
Protein nameNADP-dependent fatty aldehyde dehydrogenasealdehyde dehydrogenase (NADP+)
NADP+-acetaldehyde dehydrogenase
NADP+-dependent aldehyde dehydrogenase
aldehyde dehydrogenase (NADP+)
SynonymsEC 1.2.1.4
PfamPF00171 (Aldedh)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00930Caprolactam degradation

UniProtKB:Accession NumberQ56694
Entry nameALDH_VIBHA
ActivityAn aldehyde + NADP(+) + H(2)O = an acid + NADPH.
SubunitHomodimer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00071C00006C00001C00174C00005C00080
CompoundAldehydeNADP+H2OAcidNADPHH+
Typecarbohydrateamide group,amine group,nucleotideH2Oothersamide group,amine group,nucleotideothers
ChEBI
18009
15377

16474
15378
PubChem
5886
962
22247451

5884
1038
              
1cbzA01UnboundAnalogue:NAP UnboundUnbound 
1cbzB01UnboundAnalogue:NAP UnboundUnbound 
1cbzC01UnboundAnalogue:NAP UnboundUnbound 
1cbzD01UnboundAnalogue:NAP UnboundUnbound 
1co3A01UnboundBound:NAP UnboundUnbound 
1co3B01UnboundBound:NAP UnboundUnbound 
1co3C01UnboundBound:NAP UnboundUnbound 
1co3D01UnboundBound:NAP UnboundUnbound 
1eyyA01UnboundAnalogue:NAP UnboundUnbound 
1eyyB01UnboundAnalogue:NAP UnboundUnbound 
1eyyC01UnboundAnalogue:NAP UnboundUnbound 
1eyyD01UnboundAnalogue:NAP UnboundUnbound 
1ez0A01UnboundBound:NAP UnboundUnbound 
1ez0B01UnboundBound:NAP UnboundUnbound 
1ez0C01UnboundBound:NAP UnboundUnbound 
1ez0D01UnboundBound:NAP UnboundUnbound 
1cbzA02UnboundUnbound UnboundUnbound 
1cbzB02UnboundUnbound UnboundUnbound 
1cbzC02UnboundUnbound UnboundUnbound 
1cbzD02UnboundUnbound UnboundUnbound 
1co3A02UnboundUnbound UnboundUnbound 
1co3B02UnboundUnbound UnboundUnbound 
1co3C02UnboundUnbound UnboundUnbound 
1co3D02UnboundUnbound UnboundUnbound 
1eyyA02UnboundUnbound UnboundUnbound 
1eyyB02UnboundUnbound UnboundUnbound 
1eyyC02UnboundUnbound UnboundUnbound 
1eyyD02UnboundUnbound UnboundUnbound 
1ez0A02UnboundUnbound UnboundUnbound 
1ez0B02UnboundUnbound UnboundUnbound 
1ez0C02UnboundUnbound UnboundUnbound 
1ez0D02UnboundUnbound UnboundUnbound 

Active-site residues
resource
Swiss-prot;Q56694 & literature [7]
pdbCatalytic residues
         
1cbzA01ASN 147;GLU 253;HIS 450
1cbzB01ASN 147;GLU 253;HIS 450
1cbzC01ASN 147;GLU 253;HIS 450
1cbzD01ASN 147;GLU 253;HIS 450
1co3A01ASN 147;GLU 253;HIS 450
1co3B01ASN 147;GLU 253;HIS 450
1co3C01ASN 147;GLU 253;HIS 450
1co3D01ASN 147;GLU 253;HIS 450
1eyyA01ASN 147;GLU 253;HIS 450
1eyyB01ASN 147;GLU 253;HIS 450
1eyyC01ASN 147;GLU 253;HIS 450
1eyyD01ASN 147;GLU 253;HIS 450
1ez0A01ASN 147;GLU 253;HIS 450
1ez0B01ASN 147;GLU 253;HIS 450
1ez0C01ASN 147;GLU 253;HIS 450
1ez0D01ASN 147;GLU 253;HIS 450
1cbzA02CYS 289
1cbzB02CYS 289
1cbzC02CYS 289
1cbzD02CYS 289
1co3A02CYS 289
1co3B02CYS 289
1co3C02CYS 289
1co3D02CYS 289
1eyyA02CYS 289
1eyyB02CYS 289
1eyyC02CYS 289
1eyyD02CYS 289
1ez0A02CYS 289
1ez0B02CYS 289
1ez0C02CYS 289
1ez0D02CYS 289

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]p.859-860
[6]p.14411-14413, p.14414-14418
[7]p.34-36

references
[1]
PubMed ID8527447
JournalBiochemistry
Year1995
Volume34
Pages16725-32
AuthorsVedadi M, Szittner R, Smillie L, Meighen E
TitleInvolvement of cysteine 289 in the catalytic activity of an NADP(+)-specific fatty aldehyde dehydrogenase from Vibrio harveyi.
[2]
PubMed ID8897616
JournalProtein Sci
Year1996
Volume5
Pages2130-2
AuthorsCroteau N, Vedadi M, Delarge M, Meighen E, Abu-Abed M, Howell PL, Vrielink A
TitleCrystallization and preliminary X-ray analysis of aldehyde dehydrogenase from Vibrio harveyi.
[3]
PubMed ID9059630
JournalAdv Exp Med Biol
Year1997
Volume414
Pages269-75
AuthorsVedadi M, Croteau N, Delarge M, Vrielink A, Meighen E
TitleStructural and functional studies of a NADP(+)-specific aldehyde dehydrogenase from the luminescent marine bacterium Vibrio harveyi.
[4]
PubMed ID10471295
JournalBiochemistry
Year1999
Volume38
Pages11440-7
AuthorsZhang L, Ahvazi B, Szittner R, Vrielink A, Meighen E
TitleChange of nucleotide specificity and enhancement of catalytic efficiency in single point mutants of Vibrio harveyi aldehyde dehydrogenase.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
Medline ID20363527
PubMed ID10903148
JournalBiochem J
Year2000
Volume349 Pt 3
Pages853-61
AuthorsAhvazi B, Coulombe R, Delarge M, Vedadi M, Zhang L, Meighen E, Vrielink A
TitleCrystal structure of the NADP+-dependent aldehyde dehydrogenase from Vibrio harveyi: structural implications for cofactor specificity and affinity.
Related PDB1ez0,1eyy,1co3,1cbz
Related UniProtKBQ56694
[6]
PubMed ID11087393
JournalBiochemistry
Year2000
Volume39
Pages14409-18
AuthorsZhang L, Ahvazi B, Szittner R, Vrielink A, Meighen E
TitleA histidine residue in the catalytic mechanism distinguishes Vibrio harveyi aldehyde dehydrogenase from other members of the aldehyde dehydrogenase superfamily.
[7]
PubMed ID11306028
JournalChem Biol Interact
Year2001
Volume130-132
Pages29-38
AuthorsZhang L, Ahvazi B, Szittner R, Vrielink A, Meighen E
TitleDifferences in nucleotide specificity and catalytic mechanism between Vibrio harveyi aldehyde dehydrogenase and other members of the aldehyde dehydrogenase superfamily.

comments
This enzyme belongs to aldehyde dehydrogenase superfamily.

createdupdated
2005-01-192009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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