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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
 
 
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