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Database: UniProt
Entry: I1QNT2_ORYGL
LinkDB: I1QNT2_ORYGL
Original site: I1QNT2_ORYGL 
ID   I1QNT2_ORYGL            Unreviewed;       362 AA.
AC   I1QNT2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=cinnamyl-alcohol dehydrogenase {ECO:0000256|ARBA:ARBA00013171};
DE            EC=1.1.1.195 {ECO:0000256|ARBA:ARBA00013171};
OS   Oryza glaberrima (African rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA09G0071100.1, ECO:0000313|Proteomes:UP000007306};
RN   [1] {ECO:0000313|Proteomes:UP000007306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA   Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA   Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA   Zuccolo A.;
RT   "The complete genome of Oryza glaberrima.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORGLA09G0071100.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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)-caffeyl alcohol + NADP(+) = (E)-caffeyl aldehyde + H(+) +
CC         NADPH; Xref=Rhea:RHEA:45728, ChEBI:CHEBI:15378, ChEBI:CHEBI:28323,
CC         ChEBI:CHEBI:31334, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         Evidence={ECO:0000256|ARBA:ARBA00035979};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45730;
CC         Evidence={ECO:0000256|ARBA:ARBA00035979};
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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   AlphaFoldDB; I1QNT2; -.
DR   STRING; 4538.I1QNT2; -.
DR   EnsemblPlants; ORGLA09G0071100.1; ORGLA09G0071100.1; ORGLA09G0071100.
DR   Gramene; ORGLA09G0071100.1; ORGLA09G0071100.1; ORGLA09G0071100.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_2_1; -.
DR   OMA; HDAAQMK; -.
DR   UniPathway; UPA00711; -.
DR   Proteomes; UP000007306; Unassembled WGS sequence.
DR   GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052747; F:sinapyl alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
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   InterPro; IPR020843; PKS_ER.
DR   PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR   PANTHER; PTHR42683:SF15; CINNAMYL ALCOHOL DEHYDROGENASE 8D-RELATED; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 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   Lignin biosynthesis {ECO:0000256|ARBA:ARBA00022733};
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          18..346
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   362 AA;  37216 MW;  2A8092B5049A38A2 CRC64;
     MEHNGTAALG WAARDTSGHL SPFSFTRRVQ QEDDVTIKVF YCGICHTDLH IIKNEWGNAM
     YPVVPGHEIV GVVTGVGAGV TKFKAGDTVG VGYFVDSCRA CDSCGKGYEN YCPTMVITSN
     GTDYGGATTQ GGFSDVMVVR QDYVLRVPAS LPPDGAAPLL CAGVTVYSPM VEYGLNGPGK
     HLGVVGLGGL GHLGVKFGKA FGMKVTVISS SPAKRGEALG RLGADAFLSS RDGEGMAAAA
     ATMDGIIDTV SAGHPLVPLL SLLKPKGQMV VVGAPATPLQ LPAYAIIEGG KRVAGNGVGS
     VAECQAMLDF AGEHGIAADV EVVAMDAVNA ALGRLERNDV RYRFVVDVAG TMHAAAAAAV
     SS
//
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