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CADH1_PSEMZ
ID   CADH1_PSEMZ             Reviewed;          20 AA.
AC   P85913;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Probable cinnamyl alcohol dehydrogenase 1;
DE            Short=CAD 1 {ECO:0000250|UniProtKB:Q08350};
DE            EC=1.1.1.195;
DE   Flags: Fragments;
OS   Pseudotsuga menziesii (Douglas-fir) (Abies menziesii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC   Pseudotsuga.
OX   NCBI_TaxID=3357;
RN   [1]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004;
RA   Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.;
RT   "A proteomics approach to identify proteins differentially expressed in
RT   Douglas-fir seedlings infected by Phellinus sulphurascens.";
RL   J. Proteomics 71:425-438(2008).
CC   -!- FUNCTION: Involved in lignin biosynthesis. Catalyzes the final step
CC       specific for the production of lignin monomers, like coniferyl alcohol,
CC       sinapyl alcohol and 4-coumaryl alcohol (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:Q08350};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q08350};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q08350};
CC   -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC       {ECO:0000250|UniProtKB:Q08350}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000255}.
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DR   AlphaFoldDB; P85913; -.
DR   UniPathway; UPA00711; -.
DR   GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0052747; F:sinapyl alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Lignin biosynthesis; Metal-binding; NADP; Oxidoreductase; Zinc.
FT   CHAIN           <1..>20
FT                   /note="Probable cinnamyl alcohol dehydrogenase 1"
FT                   /id="PRO_0000371717"
FT   NON_CONS        8..9
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         20
FT                   /evidence="ECO:0000303|PubMed:18602030"
SQ   SEQUENCE   20 AA;  2167 MW;  BC9F5ECE2D428A48 CRC64;
     MGSLESERFV VDVAASNLDK
 
 
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