ID CADH6_ORYSJ Reviewed; 360 AA.
AC Q7XWU3; A0A0P0W820;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Probable cinnamyl alcohol dehydrogenase 6 {ECO:0000305};
DE Short=OsCAD6 {ECO:0000303|PubMed:15452707};
DE EC=1.1.1.195 {ECO:0000250|UniProtKB:O49482};
GN Name=CAD6 {ECO:0000303|PubMed:15452707};
GN OrderedLocusNames=Os04g0229100, LOC_Os04g15920; ORFNames=OSJNBa0065B15.8;
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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
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; Evidence={ECO:0000250|UniProtKB:O49482};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10394;
CC Evidence={ECO:0000250|UniProtKB:O49482};
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:0000250|UniProtKB:O49482};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22446;
CC Evidence={ECO:0000250|UniProtKB:O49482};
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:0000250|UniProtKB:O49482};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45706;
CC Evidence={ECO:0000250|UniProtKB:O49482};
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:0000250|UniProtKB:O49482};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45726;
CC Evidence={ECO:0000250|UniProtKB:O49482};
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:0000250|UniProtKB:O49482};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45730;
CC Evidence={ECO:0000250|UniProtKB:O49482};
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 {ECO:0000250|UniProtKB:O49482}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O49482}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AL731598; CAD39904.2; -; Genomic_DNA.
DR EMBL; AP008210; BAF14204.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS88222.1; -; Genomic_DNA.
DR EMBL; AK071484; BAG92519.1; -; mRNA.
DR EMBL; AK099270; BAG94032.1; -; mRNA.
DR RefSeq; XP_015634191.1; XM_015778705.1.
DR AlphaFoldDB; Q7XWU3; -.
DR SMR; Q7XWU3; -.
DR STRING; 39947.Q7XWU3; -.
DR PaxDb; 39947-Q7XWU3; -.
DR EnsemblPlants; Os04t0229100-01; Os04t0229100-01; Os04g0229100.
DR GeneID; 4335223; -.
DR Gramene; Os04t0229100-01; Os04t0229100-01; Os04g0229100.
DR KEGG; osa:4335223; -.
DR eggNOG; KOG0023; Eukaryota.
DR HOGENOM; CLU_026673_20_2_1; -.
DR InParanoid; Q7XWU3; -.
DR OMA; CDDYIAT; -.
DR OrthoDB; 1550at2759; -.
DR BRENDA; 1.1.1.195; 8948.
DR UniPathway; UPA00711; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q7XWU3; OS.
DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050268; F:coniferyl-alcohol dehydrogenase activity; IEA:RHEA.
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 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:SF37; CINNAMYL ALCOHOL DEHYDROGENASE 6-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 2: Evidence at transcript level;
KW Lignin biosynthesis; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..360
FT /note="Probable cinnamyl alcohol dehydrogenase 6"
FT /id="PRO_0000382645"
FT BINDING 48
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 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 70
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 71
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 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 164
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 168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 192..197
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 215..220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 255
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 279
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 302..304
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
SQ SEQUENCE 360 AA; 39086 MW; 0DEA56D0DBB425CA CRC64;
MEVTPNHTQT VSGWAAMDES GKIVPFVFKR RENGVDDVTI KVKYCGMCHT DLHFIHNDWG
ITMYPVVPGH EITGVVTKVG TNVAGFKVGD RVGVGCIAAS CLDCEHCRRS EENYCDKVAL
TYNGIFWDGS ITYGGYSGML VAHKRFVVRI PDTLPLDAAA PLLCAGITVY SPMKQHGMLQ
ADAAGRRLGV VGLGGLGHVA VKFGKAFGLH VTVISTSPAK EREARENLKA DNFVVSTDQK
QMQAMTRSLD YIIDTVAATH SLGPILELLK VNGKLVLVGA PEKPVELPSF PLIFGKRTVS
GSMTGGMKET QEMMDICGEH NITCDIEIVS TDRINDALAR LARNDVRYRF VINVGGDSKL
//
