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CALA_PSEUH
ID   CALA_PSEUH              Reviewed;         255 AA.
AC   P0DMP5;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Coniferyl-alcohol dehydrogenase;
DE            EC=1.1.1.194;
GN   Name=calA;
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], FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA   Shearer A.G., Altman T., Rhee C.D.;
RT   "Finding sequences for over 270 orphan enzymes.";
RL   PLoS ONE 9:E97250-E97250(2014).
CC   -!- FUNCTION: Catalyzes the conversion of coniferyl alcohol into coniferyl
CC       aldehyde in the eugenol degradation pathway. Specific for coniferyl
CC       alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or
CC       sinapyl alcohol. {ECO:0000269|PubMed:12200281}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-coniferol + NADP(+) = (E)-coniferaldehyde + H(+) + NADPH;
CC         Xref=Rhea:RHEA:22444, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547,
CC         ChEBI:CHEBI:17745, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.194; Evidence={ECO:0000269|PubMed:12200281};
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; A92130; CAB69495.1; -; Genomic_RNA.
DR   AlphaFoldDB; P0DMP5; -.
DR   SMR; P0DMP5; -.
DR   GO; GO:0050268; F:coniferyl-alcohol dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0042856; P:eugenol catabolic process; IDA:UniProtKB.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   NAD; NADP; Oxidoreductase.
FT   CHAIN           1..255
FT                   /note="Coniferyl-alcohol dehydrogenase"
FT                   /id="PRO_0000430457"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         12..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         51..52
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   255 AA;  27637 MW;  621C36A19708EF3D CRC64;
     MQLTNKKIVV TGVSSGIGAE TARVLRSHGA TVIGVDRNMP SLTLDAFVQA DLSHPEGIDK
     AISQLPEKID GLCNIAGVPG TADPQLVANV NYLGLKYLTE AVLSRIQPGG SIVNVSSVLG
     AEWPARLQLH KELGSVVGFS EGQAWLKQNP VAPEFCYQYF KEALIVWSQV QAQEWFMRTS
     VRMNCIAPGP VFTPILNEFV TMLGQERTQA DAHRIKRPAY ADEVAAVIAF MCAEESRWIN
     GINIPVDGGL ASTYV
 
 
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