CADH7_ORYSJ
ID CADH7_ORYSJ Reviewed; 379 AA.
AC Q0JA75; A0A0N7KJP2; Q7F9B4;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Cinnamyl alcohol dehydrogenase 7 {ECO:0000305};
DE Short=OsCAD7 {ECO:0000303|PubMed:15452707};
DE EC=1.1.1.195 {ECO:0000269|PubMed:19116760};
DE AltName: Full=Protein FLEXIBLE CULM 1 {ECO:0000303|PubMed:19116760};
GN Name=CAD7 {ECO:0000303|PubMed:15452707};
GN Synonyms=FC1 {ECO:0000303|PubMed:19116760};
GN OrderedLocusNames=Os04g0612700, LOC_Os04g52280; ORFNames=OSJNBa0070C17.13;
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).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19116760; DOI=10.1007/s11103-008-9448-8;
RA Li X., Yang Y., Yao J., Chen G., Li X., Zhang Q., Wu C.;
RT "FLEXIBLE CULM 1 encoding a cinnamyl-alcohol dehydrogenase controls culm
RT mechanical strength in rice.";
RL Plant Mol. Biol. 69:685-697(2009).
CC -!- FUNCTION: Involved in lignin biosynthesis. May catalyze the final step
CC specific for the production of lignin monomers, like coniferyl alcohol,
CC sinapyl alcohol and 4-coumaryl alcohol. {ECO:0000269|PubMed:19116760}.
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:0000269|PubMed:19116760};
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 -!- TISSUE SPECIFICITY: Expressed in roots, first internodes and panicles.
CC Expressed in the vascular bundles and sclerenchyma cells below the
CC epidermis in leaves and stems. {ECO:0000269|PubMed:19116760}.
CC -!- DISRUPTION PHENOTYPE: Reduced lignin content, late heading time, semi-
CC dwarf and flexible culm. {ECO:0000269|PubMed:19116760}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE05206.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL731610; CAE05206.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF15762.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS90969.1; -; Genomic_DNA.
DR EMBL; AK102452; BAG95561.1; -; mRNA.
DR RefSeq; XP_015635610.1; XM_015780124.1.
DR AlphaFoldDB; Q0JA75; -.
DR SMR; Q0JA75; -.
DR STRING; 4530.OS04T0612700-01; -.
DR PaxDb; Q0JA75; -.
DR PRIDE; Q0JA75; -.
DR EnsemblPlants; Os04t0612700-01; Os04t0612700-01; Os04g0612700.
DR GeneID; 4336968; -.
DR Gramene; Os04t0612700-01; Os04t0612700-01; Os04g0612700.
DR KEGG; osa:4336968; -.
DR eggNOG; KOG0023; Eukaryota.
DR HOGENOM; CLU_026673_20_2_1; -.
DR InParanoid; Q0JA75; -.
DR OMA; YSDIHTL; -.
DR OrthoDB; 625659at2759; -.
DR BRENDA; 1.1.1.195; 8948.
DR UniPathway; UPA00711; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q0JA75; OS.
DR GO; GO:0045551; F:cinnamyl-alcohol dehydrogenase activity; IMP:UniProtKB.
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; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Lignin biosynthesis; Metal-binding; NADP; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..379
FT /note="Cinnamyl alcohol dehydrogenase 7"
FT /id="PRO_0000382646"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60
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 62
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 82
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 83
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 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 185
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 189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 210..215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 233..238
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 297
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 320..322
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
SQ SEQUENCE 379 AA; 39566 MW; 28A2B28B13FA7866 CRC64;
MAPTTTATAA AEQAPPPQHT RKAVGLAAHD DSGHLTPIRI SRRKTGDDDV AIKVLYCGIC
HSDLHTIKNE WRNAVYPVVA GHEITGVVTE VGKNVARFKA GDEVGVGCMV NTCGGCESCR
DGCENYCSGG VVFTYNSVDR DGTRTYGGYS DAVVVSQRFV VRFPSSAGGG AGAALPLDSG
APLLCAGVTV YAPMRQHGLC EAGKHVGVVG LGGLGHVAVK FARAFGMRVT VISTSPVKRQ
EALERLGADG FIVSTNASEM KAAMGTMHGI INTASASTSM HSYLALLKPK GKMILVGLPE
KPLQIPTFAL VGGGKILAGS CMGSISETQE MIDFAAEHGV AADIELIGAD EVNTAMERLA
KGDVRYRFVV DIGNTLRSD
