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Entry: Q8S592_ABIHL
LinkDB: Q8S592_ABIHL
Original site: Q8S592_ABIHL 
ID   Q8S592_ABIHL            Unreviewed;       221 AA.
AC   Q8S592;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=cinnamyl-alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013171};
DE            EC=1.1.1.195 {ECO:0000256|ARBA:ARBA00013171};
DE   Flags: Fragment;
GN   Name=CAD {ECO:0000313|EMBL:AAM10533.1};
OS   Abies holophylla (Neddle fir) (Manchurian fir).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Abies.
OX   NCBI_TaxID=97168 {ECO:0000313|EMBL:AAM10533.1};
RN   [1] {ECO:0000313|EMBL:AAM10533.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wang X.Q., Tank D.C., Sang T.;
RT   "Marked difference of evolutionary rates among members of cinnamyl alcohol
RT   dehydrogenase gene family in Pinaceae.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-coumaroyl alcohol + NADP(+) = (E)-4-coumaraldehyde +
CC         H(+) + NADPH; Xref=Rhea:RHEA:45724, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28353, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:64555; EC=1.1.1.195;
CC         Evidence={ECO:0000256|ARBA:ARBA00036200};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45726;
CC         Evidence={ECO:0000256|ARBA:ARBA00036200};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-cinnamyl alcohol + NADP(+) = (E)-cinnamaldehyde + H(+) +
CC         NADPH; Xref=Rhea:RHEA:10392, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC         ChEBI:CHEBI:33227, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.195; Evidence={ECO:0000256|ARBA:ARBA00036166};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10394;
CC         Evidence={ECO:0000256|ARBA:ARBA00036166};
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=1.1.1.195; Evidence={ECO:0000256|ARBA:ARBA00036509};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22446;
CC         Evidence={ECO:0000256|ARBA:ARBA00036509};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-sinapyl alcohol + NADP(+) = (E)-sinapaldehyde + H(+) +
CC         NADPH; Xref=Rhea:RHEA:45704, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64557;
CC         EC=1.1.1.195; Evidence={ECO:0000256|ARBA:ARBA00035824};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45706;
CC         Evidence={ECO:0000256|ARBA:ARBA00035824};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004928}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072, ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; AF146011; AAM10533.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8S592; -.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd05283; CAD1; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR047109; CAD-like.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF1; CINNAMYL ALCOHOL DEHYDROGENASE 5; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          10..124
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          167..217
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAM10533.1"
FT   NON_TER         221
FT                   /evidence="ECO:0000313|EMBL:AAM10533.1"
SQ   SEQUENCE   221 AA;  23956 MW;  BDB4C4B404568F19 CRC64;
     YTYNLRNKGP EDVILRVIYC GICHSDLVQM RNEMGMSNYP MVPGHEVVGI VTEIGSEVKK
     FKVGEQVGVG CIVGSCRKCG NCNESMEQYC SKRIWTYNDV NHDGTPTQGG FASTMVVDQM
     FVVRIPDNLP LEQAAPLLCA GVTVYSPLKH FGMTESGKRC GILGLGGVGH MGVKIAKAFG
     LHVTVISSSD KKKEEALEVL GADAYLVSKD AEKMQEAAES L
//
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