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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
 
 
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