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8-hydroxygeraniol dehydrogenase (Cr10HGO) (EC 1.1.1.324)

 10HGO_CATRO             Reviewed;         360 AA.
Q6V4H0;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
20-JUN-2018, entry version 75.
RecName: Full=8-hydroxygeraniol dehydrogenase;
Short=Cr10HGO;
EC=1.1.1.324;
Name=10HGO;
Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; lamiids; Gentianales; Apocynaceae;
Rauvolfioideae; Vinceae; Catharanthinae; Catharanthus.
NCBI_TaxID=4058;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
SPECIFICITY.
Teoh K.H., Gorman E.B., McKnight T.D.;
"Characterization and cloning of 10-hydroxygeraniol oxidoreductase.";
(In) Proceedings of Plant Biology '2000: The annual meeting of the
American Society of Plant Physiologists, pp.abstract#272:0-0,
San Diego (2000).
-!- FUNCTION: Dehydrogenase involved in the biosynthesis of
oxogeranial from hydroxygeraniol, a precursor of the terpenoid
indole alkaloids such as vinblastine and vincristine.
{ECO:0000269|Ref.1}.
-!- CATALYTIC ACTIVITY: (6E)-8-hydroxygeraniol + 2 NADP(+) = (6E)-8-
oxogeranial + 2 NADPH. {ECO:0000269|Ref.1}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
-!- TISSUE SPECIFICITY: Present in seedlings and vascular tissues (at
protein level). Restricted to the epidermis. {ECO:0000269|Ref.1}.
-!- MISCELLANEOUS: The recommended numbering of geraniol gives (6E)-8-
hydroxygeraniol as the substrate rather than 10-hydroxygeraniol
and (6E)-8-oxogeranial as the product rather than 10-oxogeranial
as used in most publications.
-!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
family. {ECO:0000305}.
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EMBL; AY352047; AAQ55962.1; -; mRNA.
ProteinModelPortal; Q6V4H0; -.
SMR; Q6V4H0; -.
PRIDE; Q6V4H0; -.
BioCyc; MetaCyc:MONOMER-20519; -.
GO; GO:0102311; F:8-hydroxygeraniol dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
InterPro; IPR013149; ADH_C.
InterPro; IPR013154; ADH_N.
InterPro; IPR002328; ADH_Zn_CS.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020843; PKS_ER.
Pfam; PF08240; ADH_N; 1.
Pfam; PF00107; ADH_zinc_N; 1.
SMART; SM00829; PKS_ER; 1.
SUPFAM; SSF50129; SSF50129; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00059; ADH_ZINC; 1.
1: Evidence at protein level;
Metal-binding; NADP; Oxidoreductase; Zinc.
CHAIN 1 360 8-hydroxygeraniol dehydrogenase.
/FTId=PRO_0000418979.
METAL 50 50 Zinc 1; catalytic. {ECO:0000250}.
METAL 72 72 Zinc 1; catalytic. {ECO:0000250}.
METAL 103 103 Zinc 2. {ECO:0000250}.
METAL 106 106 Zinc 2. {ECO:0000250}.
METAL 109 109 Zinc 2. {ECO:0000250}.
METAL 117 117 Zinc 2. {ECO:0000250}.
METAL 166 166 Zinc 1; catalytic. {ECO:0000250}.
SEQUENCE 360 AA; 38937 MW; AB701A2D8921005E CRC64;
MAKSPEVEHP VKAFGWAARD TSGHLSPFHF SRRATGEHDV QFKVLYCGIC HSDLHMIKNE
WGFTKYPIVP GHEIVGIVTE VGSKVEKFKV GDKVGVGCLV GSCRKCDMCT KDLENYCPGQ
ILTYSATYTD GTTTYGGYSD LMVADEHFVI RWPENLPMDI GAPLLCAGIT TYSPLRYFGL
DKPGTHVGVV GLGGLGHVAV KFAKAFGAKV TVISTSESKK QEALEKLGAD SFLVSRDPEQ
MKAAAASLDG IIDTVSAIHP IMPLLSILKS HGKLILVGAP EKPLELPSFP LIAGRKIIAG
SAIGGLKETQ EMIDFAAKHN VLPDVELVSM DYVNTAMERL LKADVKYRFV IDVANTLKSA


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