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