CADH_MAIZE
ID CADH_MAIZE Reviewed; 367 AA.
AC O24562; O64408;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Probable cinnamyl alcohol dehydrogenase {ECO:0000303|PubMed:9675900, ECO:0000303|Ref.1};
DE Short=CAD {ECO:0000303|PubMed:9675900, ECO:0000303|Ref.1};
DE EC=1.1.1.195 {ECO:0000269|PubMed:9675900};
DE AltName: Full=Brown-midrib 1 protein {ECO:0000303|PubMed:9675900};
GN Name=CAD {ECO:0000303|PubMed:9675900, ECO:0000303|Ref.1};
GN Synonyms=BM1 {ECO:0000303|PubMed:9675900};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Wisconsin 64A;
RA Civardi L., Tatout P., Murigneux A., Puigdomenech P., Rigau J.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RC STRAIN=cv. UE95;
RX PubMed=9675900; DOI=10.1046/j.1365-313x.1998.00153.x;
RA Halpin C., Holt K., Chojecki J., Oliver D., Chabbert B., Monties B.,
RA Edwards K., Barakate A., Foxon G.A.;
RT "Brown-midrib maize (bm1) -- a mutation affecting the cinnamyl alcohol
RT dehydrogenase gene.";
RL Plant J. 14:545-553(1998).
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:9675900}.
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:9675900};
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:0000269|PubMed:9675900}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O49482}.
CC -!- DISRUPTION PHENOTYPE: Reduced lignin content, and modified lignin of
CC reddish-brown color. {ECO:0000269|PubMed:9675900}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y13733; CAA74070.1; -; mRNA.
DR EMBL; AJ005702; CAA06687.1; -; mRNA.
DR PIR; T02767; T02767.
DR PIR; T02990; T02990.
DR RefSeq; NP_001105654.1; NM_001112184.1.
DR AlphaFoldDB; O24562; -.
DR SMR; O24562; -.
DR STRING; 4577.GRMZM5G844562_P01; -.
DR PaxDb; O24562; -.
DR PRIDE; O24562; -.
DR GeneID; 542663; -.
DR KEGG; zma:542663; -.
DR MaizeGDB; 13856; -.
DR eggNOG; KOG0023; Eukaryota.
DR OrthoDB; 625659at2759; -.
DR UniPathway; UPA00711; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; O24562; baseline and differential.
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..367
FT /note="Probable cinnamyl alcohol dehydrogenase"
FT /id="PRO_0000160797"
FT BINDING 47
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 49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 69
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 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 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 163
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 167
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 188..193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 211..216
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 251
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 275
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT BINDING 298..300
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O49482"
FT CONFLICT 179
FT /note="N -> T (in Ref. 2; CAA06687)"
FT /evidence="ECO:0000305"
FT CONFLICT 239..240
FT /note="AA -> GP (in Ref. 2; CAA06687)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 38739 MW; 5C9B844673C017C9 CRC64;
MGSLASERKV VGWAARDATG HLSPYSYTLR NTGPEDVVVK VLYCGICHTD IHQAKNHLGA
SKYPMVPGHE VVGEVVEVGP EVAKYGVGDV VGVGVIVGCC RECSPCKANV EQYCNKKIWS
YNDVYTDGRP TQGGFASTMV VDQKFVVKIP AGLAPEQAAP LLCAGVTVYS PLKHFGLTNP
GLRGGILGLG GVGHMGVKVA KAMGHHVTVI SSSSKKRAEA MDHLGADAYL VSSDAAAMAA
AADSLDYIID TVPVHHPLEP YLALLKLDGK LVLLGVIGEP LSFVSPMVML GRKAITGSFI
GSIDETAEVL QFCVDKGLTS QIEVVKMGYV NEALERLERN DVRYRFVVDV AGSNVEAEAA
AADAASN
