GEDH_CARLC
ID GEDH_CARLC Reviewed; 378 AA.
AC B2NI93;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Geraniol dehydrogenase {ECO:0000305};
DE Short=GeDH {ECO:0000305};
DE EC=1.1.1.347 {ECO:0000269|PubMed:18422649};
DE AltName: Full=Farnesol dehydrogenase {ECO:0000305};
DE EC=1.1.1.354 {ECO:0000269|PubMed:18422649};
DE AltName: Full=NAD(+)-farnesol dehydrogenase {ECO:0000305};
GN Name=gedh {ECO:0000303|PubMed:18422649};
OS Carpoglyphus lactis (Dried fruit mite) (Acarus lactis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Hemisarcoptoidea; Carpoglyphidae;
OC Carpoglyphus.
OX NCBI_TaxID=223459 {ECO:0000312|EMBL:BAG32342.1};
RN [1]
RP PROTEIN SEQUENCE OF 1-42, NUCLEOTIDE SEQUENCE [MRNA] OF 18-378, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18422649; DOI=10.1111/j.1742-4658.2008.06421.x;
RA Noge K., Kato M., Mori N., Kataoka M., Tanaka C., Yamasue Y., Nishida R.,
RA Kuwahara Y.;
RT "Geraniol dehydrogenase, the key enzyme in biosynthesis of the alarm
RT pheromone, from the astigmatid mite Carpoglyphus lactis (Acari:
RT Carpoglyphidae).";
RL FEBS J. 275:2807-2817(2008).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of geraniol to
CC geranial, playing an important role in the biosynthesis of neral, an
CC alarm pheromone. Cannot use NADP(+). Also acts as a farnesol
CC dehydrogenase by catalyzing the oxidation of (2E,6E)-farnesol to
CC (2E,6E)-farnesal, with lower activity compared to geraniol
CC dehydrogenase activity. {ECO:0000269|PubMed:18422649}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geraniol + NAD(+) = (2E)-geranial + H(+) + NADH;
CC Xref=Rhea:RHEA:34347, ChEBI:CHEBI:15378, ChEBI:CHEBI:16980,
CC ChEBI:CHEBI:17447, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.347; Evidence={ECO:0000269|PubMed:18422649};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesol + NAD(+) = (2E,6E)-farnesal + H(+) + NADH;
CC Xref=Rhea:RHEA:37167, ChEBI:CHEBI:15378, ChEBI:CHEBI:15894,
CC ChEBI:CHEBI:16619, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.354; Evidence={ECO:0000269|PubMed:18422649};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P11766};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P11766};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=51.0 uM for geraniol {ECO:0000269|PubMed:18422649};
CC KM=59.5 uM for NAD(+) {ECO:0000269|PubMed:18422649};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:18422649};
CC Temperature dependence:
CC Optimum temperature is 25 degrees Celsius.
CC {ECO:0000269|PubMed:18422649};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18422649}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AB305641; BAG32342.1; -; mRNA.
DR AlphaFoldDB; B2NI93; -.
DR SMR; B2NI93; -.
DR BioCyc; MetaCyc:MON-18374; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..378
FT /note="Geraniol dehydrogenase"
FT /id="PRO_0000430710"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P11766"
SQ SEQUENCE 378 AA; 40630 MW; 9D86CA8AC86615F9 CRC64;
VQNPGASAIQ CRAAVLRKEG QPMKIEQVLI QAPGPNQVRV KMVSSGLCAT DAHLVWGEQK
ISDLGGIGCP AIAGHEGAGI VESVGENVTE FVPGDSVLTS FQPQCGQCES CLRPSTNICK
KYDLIKSTTD VSTARTLDGQ PITSLFGLGV YSEYITTTEH HVFKVNKAAN LEHASIISCS
VGTGFYSATN LAAVYEGSTC AVWGLGGIGI NTLFGCKYNK AKHIIGIDVN EDKREIAAEF
GCTEFINPKT LGQPVEQYLM DKFGGVDFAF DCVGYKPILD QAAVSLAIDG TMVIIGAAAK
EVKFEMPAFN FLFNRKVVGG LLGSKKTKVA YQELCDMYVD GTYDVDRLVS NKFSLDQINE
AFQTLKDGNC IRSIVVFK
