10HGO_CATRO
ID 10HGO_CATRO Reviewed; 360 AA.
AC Q6V4H0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=8-hydroxygeraniol dehydrogenase;
DE Short=Cr10HGO;
DE EC=1.1.1.324;
GN Name=10HGO;
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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RA Teoh K.H., Gorman E.B., McKnight T.D.;
RT "Characterization and cloning of 10-hydroxygeraniol oxidoreductase.";
RL (In) Proceedings of Plant Biology '2000: The annual meeting of the American
RL Society of Plant Physiologists, pp.abstract#272:0-0, San Diego (2000).
CC -!- FUNCTION: Dehydrogenase involved in the biosynthesis of oxogeranial
CC from hydroxygeraniol, a precursor of the terpenoid indole alkaloids
CC such as vinblastine and vincristine. {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6E)-8-hydroxygeraniol + 2 NADP(+) = (6E)-8-oxogeranial + 2
CC H(+) + 2 NADPH; Xref=Rhea:RHEA:32659, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64235,
CC ChEBI:CHEBI:64239; EC=1.1.1.324; Evidence={ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- TISSUE SPECIFICITY: Present in seedlings and vascular tissues (at
CC protein level). Restricted to the epidermis. {ECO:0000269|Ref.1}.
CC -!- MISCELLANEOUS: The recommended numbering of geraniol gives (6E)-8-
CC hydroxygeraniol as the substrate rather than 10-hydroxygeraniol and
CC (6E)-8-oxogeranial as the product rather than 10-oxogeranial as used in
CC most publications.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AY352047; AAQ55962.1; -; mRNA.
DR PDB; 6K3G; X-ray; 2.41 A; B=1-360.
DR PDB; 6KJ5; X-ray; 3.75 A; A=4-359.
DR PDBsum; 6K3G; -.
DR PDBsum; 6KJ5; -.
DR AlphaFoldDB; Q6V4H0; -.
DR SMR; Q6V4H0; -.
DR BioCyc; MetaCyc:MON-20519; -.
DR GO; GO:0102311; F:8-hydroxygeraniol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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 3D-structure; Metal-binding; NADP; Oxidoreductase; Zinc.
FT CHAIN 1..360
FT /note="8-hydroxygeraniol dehydrogenase"
FT /id="PRO_0000418979"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT TURN 5..7
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 8..18
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 39..48
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:6K3G"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:6K3G"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 306..318
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 333..341
FT /evidence="ECO:0007829|PDB:6K3G"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:6K3G"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:6K3G"
SQ 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