VDH_PSEFL
ID VDH_PSEFL Reviewed; 482 AA.
AC O69763;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Vanillin dehydrogenase;
DE EC=1.2.1.67;
GN Name=vdh;
OS Pseudomonas fluorescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=294;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=AN103;
RX PubMed=9461612; DOI=10.1074/jbc.273.7.4163;
RA Gasson M.J., Kitamura Y., McLauchlan W.R., Narbad A., Parr A.J.,
RA Parsons E.L., Payne J., Rhodes M.J., Walton N.J.;
RT "Metabolism of ferulic acid to vanillin. A bacterial gene of the enoyl-SCoA
RT hydratase/isomerase superfamily encodes an enzyme for the hydration and
RT cleavage of a hydroxycinnamic acid SCoA thioester.";
RL J. Biol. Chem. 273:4163-4170(1998).
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation of vanillin to vanillic
CC acid. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + vanillin = 2 H(+) + NADH + vanillate;
CC Xref=Rhea:RHEA:13309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16632, ChEBI:CHEBI:18346, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.67;
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; Y13067; CAA73503.1; -; Genomic_DNA.
DR AlphaFoldDB; O69763; -.
DR SMR; O69763; -.
DR STRING; 690597.JH730982_gene2033; -.
DR eggNOG; COG1012; Bacteria.
DR GO; GO:0050608; F:vanillin dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase.
FT CHAIN 1..482
FT /note="Vanillin dehydrogenase"
FT /id="PRO_0000418953"
FT ACT_SITE 250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT BINDING 228..233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 482 AA; 50440 MW; C803EE29ECC9571B CRC64;
MLDVPLLIGG QSCPARDGRT FERRNPVTGE LVSRVAAATL EDADAAVAAA QQAFPAWAAL
APNERRSRLL KAAEQLQARS GEFIEAAGET GAMANWYGFN VRLAANMLRE AASMTTQVNG
EVIPSDVPGS FAMALRQPCG VVLGIAPWNA PVILATRAIA MPLACGNTVV LKASELSPAV
HRLIGQVLQD AGLGDGVVNV ISNAPADAAQ IVERLIANPA VRRVNFTGST HVGRIVGELS
ARHLKPALLE LGGKAPLLVL DDADLEAAVQ AAAFGAYFNQ GQICMSTERL IVDAKVADAF
VAQLAAKVET LRAGDPADPE SVLGSLVDAS AGTRIKALID DAVAKGARLV IGGQLEGSIL
QPTLLDGVDA SMRLYREESF GPVAVVLRGE GEEALLQLAN DSEFGLSAAI FSRDTGRALA
LAQRVESGIC HINGPTVHDE AQMPFGGVKS SGYGSFGGKA SIEHFTQLRW VTLQNGPRHY
PI