ID   CALB_PSEUH              Reviewed;         481 AA.
AC   O86447;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Coniferyl aldehyde dehydrogenase;
DE            Short=CALDH;
DE            EC=1.2.1.68;
GN   Name=calB;
OS   Pseudomonas sp. (strain HR199 / DSM 7063).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=86003;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, FUNCTION,
RP   SUBUNIT, AND CATALYTIC ACTIVITY.
RX   PubMed=9721273; DOI=10.1128/jb.180.17.4387-4391.1998;
RA   Achterholt S., Priefert H., Steinbuechel A.;
RT   "Purification and characterization of the coniferyl aldehyde dehydrogenase
RT   from Pseudomonas sp. strain HR199 and molecular characterization of the
RT   gene.";
RL   J. Bacteriol. 180:4387-4391(1998).
RN   [2]
RP   FUNCTION.
RX   PubMed=12200281; DOI=10.1128/aem.68.9.4315-4321.2002;
RA   Overhage J., Steinbuechel A., Priefert H.;
RT   "Biotransformation of eugenol to ferulic acid by a recombinant strain of
RT   Ralstonia eutropha H16.";
RL   Appl. Environ. Microbiol. 68:4315-4321(2002).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of coniferyl
CC       aldehyde to ferulic acid and which is induced during growth with
CC       eugenol as the carbon source. {ECO:0000269|PubMed:12200281,
CC       ECO:0000269|PubMed:9721273}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-coniferaldehyde + H2O + NADP(+) = (E)-ferulate + 2 H(+) +
CC         NADPH; Xref=Rhea:RHEA:23964, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16547, ChEBI:CHEBI:29749, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.2.1.68;
CC         Evidence={ECO:0000269|PubMed:9721273};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-coniferaldehyde + H2O + NAD(+) = (E)-ferulate + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:23968, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16547, ChEBI:CHEBI:29749, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.68;
CC         Evidence={ECO:0000269|PubMed:9721273};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9721273}.
CC   -!- MISCELLANEOUS: The enzyme activity with NADP(+) is 4.3% of that with
CC       NAD(+).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ006231; CAA06926.1; -; Genomic_DNA.
DR   AlphaFoldDB; O86447; -.
DR   SMR; O86447; -.
DR   KEGG; ag:CAA06926; -.
DR   BRENDA; 1.2.1.68; 5085.
DR   GO; GO:0050269; F:coniferyl-aldehyde dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   GO; GO:0042856; P:eugenol catabolic process; IDA:UniProtKB.
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   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43570; PTHR43570; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9721273"
FT   CHAIN           2..481
FT                   /note="Coniferyl aldehyde dehydrogenase"
FT                   /id="PRO_0000056585"
FT   ACT_SITE        221
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   481 AA;  51987 MW;  A1AC6CC1CB1D55B1 CRC64;
     MSILGLNGAP VGAEQLGSAL DRMKKAHLEQ GPANLELRLS RLDRAIAMLL ENREAIADAV
     SADFGNRSRE QTLLCDIAGS VASLKDSREH VAKWMEPEHH KAMFPGAEAR VEFQPLGVVG
     VISPWNFPIV LAFGPLAGIF AAGNRAMLKP SELTPRTSAL LAELIARYFD ETELTTVLGD
     AEVGALFSAQ PFDHLIFTGG TAVAKHIMRA AADNLVPVTL ELGGKSPVIV SRSADMADVA
     QRVLTVKTFN AGQICLAPDY VLLPEESLDS FVAEATRFVA AMYPSLLDNP DYTSIINARN
     FDRLHRYLTD AQAKGGRVIE INPAAEELGD SGIRKIAPTL IVNVSDEMLV LNEEIFGPLL
     PIKTYRDFDS AIDYVNSKQR PLASYFFGED AVEREQVLKR TVSGAVVVND VMSHVMMDTL
     PFGGVGHSGM GAYHGIYGFR TFSHAKPVLV QSPVGESNLA MRAPYGEAIH GLLSVLLSTE
     C