8HGO_CATRO
ID 8HGO_CATRO Reviewed; 378 AA.
AC W8JWV8;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=8-hydroxygeraniol oxidoreductase {ECO:0000303|PubMed:24710322};
DE Short=8-HGO {ECO:0000303|PubMed:24710322};
DE Short=Cr8HGO {ECO:0000303|PubMed:24710322};
DE EC=1.1.1.- {ECO:0000269|PubMed:24710322};
DE AltName: Full=Alcohol dehydrogenase 10 {ECO:0000303|PubMed:24710322};
GN Name=8HGO {ECO:0000303|PubMed:24710322};
GN Synonyms=ADH10 {ECO:0000303|PubMed:24710322};
GN ORFNames=Caros003452 {ECO:0000303|PubMed:24710322};
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, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION BY JASMONIC ACID, AND PATHWAY.
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 -!- FUNCTION: Component of the seco-iridoid and derivatives monoterpenoid
CC indole alkaloids (MIAs, e.g. vincristine, quinine, and strychnine)
CC biosynthesis pathway. Catalyzes two successive and reversible oxidation
CC steps for the formation of 8-oxogeranial from 8-hydroxygeraniol. Active
CC with 8-OH-geraniol, 8-OH-geranial and 8-oxogeraniol in the presence of
CC NAD(+). {ECO:0000269|PubMed:24710322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6E)-8-hydroxygeranial + NAD(+) = (6E)-8-oxogeranial + H(+) +
CC NADH; Xref=Rhea:RHEA:58844, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:64238, ChEBI:CHEBI:64239;
CC Evidence={ECO:0000269|PubMed:24710322};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58845;
CC Evidence={ECO:0000269|PubMed:24710322};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58846;
CC Evidence={ECO:0000269|PubMed:24710322};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6E)-8-hydroxygeraniol + NAD(+) = (6E)-8-hydroxygeranial +
CC H(+) + NADH; Xref=Rhea:RHEA:58848, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:64235,
CC ChEBI:CHEBI:64238; Evidence={ECO:0000269|PubMed:24710322};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58849;
CC Evidence={ECO:0000269|PubMed:24710322};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58850;
CC Evidence={ECO:0000269|PubMed:24710322};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6E)-8-oxogeraniol + NAD(+) = (6E)-8-oxogeranial + H(+) +
CC NADH; Xref=Rhea:RHEA:58852, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:64236, ChEBI:CHEBI:64239;
CC Evidence={ECO:0000269|PubMed:24710322};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58853;
CC Evidence={ECO:0000269|PubMed:24710322};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58854;
CC Evidence={ECO:0000269|PubMed:24710322};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6E)-8-hydroxygeraniol + NAD(+) = (6E)-8-oxogeraniol + H(+) +
CC NADH; Xref=Rhea:RHEA:58856, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:64235, ChEBI:CHEBI:64236;
CC Evidence={ECO:0000269|PubMed:24710322};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58857;
CC Evidence={ECO:0000269|PubMed:24710322};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:58858;
CC Evidence={ECO:0000269|PubMed:24710322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P40394};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P40394};
CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:24710322}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P40394}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24710322}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:24710322}.
CC -!- TISSUE SPECIFICITY: Expressed in the leaf internal phloem-associated
CC parenchyma (IPAP) inside the mesophyll. {ECO:0000269|PubMed:24710322}.
CC -!- INDUCTION: By jasmonic acid (MeJA). {ECO:0000269|PubMed:24710322}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Class-IV 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; KF302069; AHK60836.1; -; mRNA.
DR AlphaFoldDB; W8JWV8; -.
DR SMR; W8JWV8; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0102311; F:8-hydroxygeraniol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0035834; P:indole alkaloid metabolic process; IDA:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IEP: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; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; Cytoplasm; Metal-binding; NAD; Nucleus;
KW Oxidoreductase; Zinc.
FT CHAIN 1..378
FT /note="8-hydroxygeraniol oxidoreductase"
FT /id="PRO_0000446402"
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:P40394"
FT BINDING 52..56
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
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|UniProtKB:P40394"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 203..208
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 274..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 297..299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
FT BINDING 321..323
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P40394"
SQ SEQUENCE 378 AA; 40412 MW; DCCAD5A0AAB5C2D2 CRC64;
MTKTNSPAPS VITCKAAVVW KSGEPPKVEE IQVDPPKASE VRIKMLCASL CHTDFLACNG
LPVPLFPRIP GHEGVGMIES VGENVTNLKE GDIVMPLYLG ECGECLNCKS GRTNLCHKYP
LGFSGLLLDG TSRMSIGEQK VYHHFSCSTW SEYIVIEAAY AVKVDPRVSL PHASFLCCGF
TTGFGATWRD VNVVKGSTVA VLGLGAVGLG AVQGAKSQGA SRIIGLDIND KKREKGEAFG
MTEFINPKGS NKSISELINE ATGGLGLDYV YECTGVPALL NEAIESSKVG LGTAVLIGAG
LETSGEIKFI PLLCGRTVKG SIYGGVRPKS DLPTLIEKCI NKEIPMDELM THEVSLSEIN
KGFEYLKHPD CVKVVIKF