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CADH5_ORYSJ
ID   CADH5_ORYSJ             Reviewed;         354 AA.
AC   Q0J6T3; A0A0P0XED6; A3BRE1; C7J6B6;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable cinnamyl alcohol dehydrogenase 5 {ECO:0000305};
DE            Short=OsCAD5 {ECO:0000303|PubMed:15452707};
DE            EC=1.1.1.195 {ECO:0000305};
GN   Name=CAD5 {ECO:0000303|PubMed:15452707};
GN   OrderedLocusNames=Os08g0270400, Os08g0270433, Os08g0270466, LOC_Os08g16910;
GN   ORFNames=OsJ_26689;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15452707; DOI=10.1007/s00425-004-1385-4;
RA   Tobias C.M., Chow E.K.;
RT   "Structure of the cinnamyl-alcohol dehydrogenase gene family in rice and
RT   promoter activity of a member associated with lignification.";
RL   Planta 220:678-688(2005).
CC   -!- FUNCTION: Involved in lignin biosynthesis. Catalyzes the final step
CC       specific for the production of lignin monomers. Catalyzes the NADPH-
CC       dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde,
CC       sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their
CC       respective alcohols. {ECO:0000250|UniProtKB:O49482}.
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O49482};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O49482};
CC   -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O49482}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAH94216.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAT04648.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP005731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP008214; BAH94216.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014964; BAT04648.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM000145; EAZ42130.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0J6T3; -.
DR   SMR; Q0J6T3; -.
DR   STRING; 4530.OS08T0270400-00; -.
DR   PRIDE; Q0J6T3; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   InParanoid; Q0J6T3; -.
DR   UniPathway; UPA00711; -.
DR   Proteomes; UP000000763; Chromosome 8.
DR   Proteomes; UP000007752; Chromosome 8.
DR   Proteomes; UP000059680; Chromosome 8.
DR   GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
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; IBA:GO_Central.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Lignin biosynthesis; Metal-binding; NADP; Oxidoreductase;
KW   Reference proteome; Zinc.
FT   CHAIN           1..354
FT                   /note="Probable cinnamyl alcohol dehydrogenase 5"
FT                   /id="PRO_0000382644"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         45
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         102
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         163
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         184..189
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         207..212
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         247
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         271
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   BINDING         294..296
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:O49482"
FT   CONFLICT        13
FT                   /note="D -> E (in Ref. 4; EAZ42130)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  37196 MW;  3A0713624BDB6884 CRC64;
     MAPTAAAGLA ARDASGHLSP LTISRRSTGD DDVVIKILYC GICHSDLHSI KNEWKNATYP
     LVPGHEIAGV VTEAGKNVTK FKGGDKVGVG CMVNSCHSCD SCNQGLENHC PGVIFTYNSV
     DKDGTVTYGG YSSMVVVHER FVVRFPEAMP LDKGAPLLCA GITVYSPMKY HGLNVPSKHV
     GVLGLGGLGH VAVKFAKAFG MTVTVISSSP GKRQEALERL GADAFVVSKN ADEMNAATGT
     MDGIINTVSA NIPIAPLLGL LKPNGKMILV GLPEKPMEIP PFALVASNKT LAGSCIGGMA
     DTEMIDLAAK HGVTAEIEVI GADYVNTAME RLAKADVRYR FVIDIGNTLK DAIE
 
 
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