ID   ADH13_CATRO             Reviewed;         362 AA.
AC   W8JCF0;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Alcohol dehydrogenase 13 {ECO:0000303|PubMed:24710322};
DE            Short=CrADH13 {ECO:0000303|PubMed:24710322};
DE            EC=1.3.1.- {ECO:0000305};
GN   Name=ADH13 {ECO:0000303|PubMed:24710322}; Synonyms=CAD4 {ECO:0000305};
GN   ORFNames=Caros016974 {ECO:0000305};
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthinae; Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Little Bright Eyes;
RX   PubMed=24710322; DOI=10.1038/ncomms4606;
RA   Miettinen K., Dong L., Navrot N., Schneider T., Burlat V., Pollier J.,
RA   Woittiez L., van der Krol S., Lugan R., Ilc T., Verpoorte R.,
RA   Oksman-Caldentey K.M., Martinoia E., Bouwmeester H., Goossens A.,
RA   Memelink J., Werck-Reichhart D.;
RT   "The seco-iridoid pathway from Catharanthus roseus.";
RL   Nat. Commun. 5:3606-3606(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P06525};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P06525};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06525}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=ORCAE database;
CC       URL="https://bioinformatics.psb.ugent.be/orcae/overview/Catro";
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DR   EMBL; KF302078; AHK60845.1; -; mRNA.
DR   AlphaFoldDB; W8JCF0; -.
DR   SMR; W8JCF0; -.
DR   KEGG; ag:AHK60845; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..362
FT                   /note="Alcohol dehydrogenase 13"
FT                   /id="PRO_0000446404"
FT   BINDING         51
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P06525"
FT   BINDING         73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P00327"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P06525"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06525"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06525"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06525"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06525"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P06525"
FT   BINDING         193..198
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P06525"
FT   BINDING         280..282
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00327"
SQ   SEQUENCE   362 AA;  39641 MW;  FA90B36EAA7A9E69 CRC64;
     MAGETTKLDL SVKAIGWGAA DASGVLQPIR FYRRAPGERD VKIRVLYCGV CNFDMEMVRN
     KWGFTRYPYV FGHETAGEVV EVGKKVEKFK VGDKVGVGCM VGSCGKCFHC QNEMENYCPE
     PNLADGSTYR EEGERSYGGC SNVMVVDEKF VLRWPENLPQ DKGVPLLCAG VVVYSPMKYM
     GFDKPGKHIG VFGLGGLGSI AVKFIKAFGG KATVISTSRR KEKEAIEEHG ADAFVVNTDS
     EQLKALEGTM DGVVDTTPGG RTPMPLMLNL VKFDGAVILV GAPETLFELP LEPMGRKKII
     GSSTGGLKEY QEVLDIAAKH NIVCDTEVIG IDYLSTAMER IKNLDVKYRF AIDIGNTLKF
     EE