GEOA_CASDE
ID GEOA_CASDE Reviewed; 373 AA.
AC H1ZV38;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Geraniol dehydrogenase;
DE Short=GeDH;
DE EC=1.1.1.347;
DE AltName: Full=Geraniol oxidation pathway protein A;
DE AltName: Full=Perillyl-alcohol dehydrogenase;
DE EC=1.1.1.144;
GN Name=geoA;
OS Castellaniella defragrans (Alcaligenes defragrans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Castellaniella.
OX NCBI_TaxID=75697;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-29, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, INDUCTION, GENE NAME, PATHWAY, AND SUBUNIT.
RC STRAIN=DSM 12143 / 65Phen;
RX PubMed=22286981; DOI=10.1128/aem.07226-11;
RA Luddeke F., Wulfing A., Timke M., Germer F., Weber J., Dikfidan A.,
RA Rahnfeld T., Linder D., Meyerdierks A., Harder J.;
RT "Geraniol and geranial dehydrogenases induced in anaerobic monoterpene
RT degradation by Castellaniella defragrans.";
RL Appl. Environ. Microbiol. 78:2128-2136(2012).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of geraniol to
CC geranial. Is involved in the anaerobic degradation of the monoterpene
CC beta-myrcene. Can also catalyze the oxidation of (S)-perillyl alcohol
CC to perillyl aldehyde, and to a lesser extent, the oxidation of nerol,
CC citronellol, cumic alcohol, and benzyl alcohol. Cannot use NADP(+)
CC instead of NAD(+) as cosubstrate. {ECO:0000269|PubMed:22286981}.
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:22286981};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + perillyl alcohol = H(+) + NADH + perillyl aldehyde;
CC Xref=Rhea:RHEA:10664, ChEBI:CHEBI:15378, ChEBI:CHEBI:15420,
CC ChEBI:CHEBI:15421, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.144; Evidence={ECO:0000269|PubMed:22286981};
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 -!- ACTIVITY REGULATION: Is inhibited by EDTA, N-ethylmaleimide,
CC diethylpyrocarbonate, and 1-cyclohexyl-N-(2-
CC morpholinoethyl)carbodiimide in vitro. {ECO:0000269|PubMed:22286981}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for geraniol {ECO:0000269|PubMed:22286981};
CC KM=7 uM for (S)-perillyl alcohol {ECO:0000269|PubMed:22286981};
CC KM=45 uM for nerol {ECO:0000269|PubMed:22286981};
CC KM=86 uM for citronellol {ECO:0000269|PubMed:22286981};
CC KM=21 uM for cumic alcohol {ECO:0000269|PubMed:22286981};
CC KM=170 uM for benzyl alcohol {ECO:0000269|PubMed:22286981};
CC Vmax=10 umol/min/mg enzyme with geraniol as substrate
CC {ECO:0000269|PubMed:22286981};
CC Vmax=18 umol/min/mg enzyme with (S)-perillyl alcohol as substrate
CC {ECO:0000269|PubMed:22286981};
CC Vmax=18 umol/min/mg enzyme with nerol as substrate
CC {ECO:0000269|PubMed:22286981};
CC Vmax=11 umol/min/mg enzyme with citronellol as substrate
CC {ECO:0000269|PubMed:22286981};
CC Vmax=14 umol/min/mg enzyme with cumic alcohol as substrate
CC {ECO:0000269|PubMed:22286981};
CC Vmax=47 umol/min/mg enzyme with benzyl alcohol as substrate
CC {ECO:0000269|PubMed:22286981};
CC Note=The values given here are for the native GeDH, the values for
CC the recombinant protein can be found in another article
CC (PubMed:22286981).;
CC pH dependence:
CC Optimum pH is 9.4. {ECO:0000269|PubMed:22286981};
CC -!- PATHWAY: Terpene metabolism; monoterpene degradation.
CC {ECO:0000269|PubMed:22286981}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22286981}.
CC -!- INDUCTION: By the monoterpene limonene. {ECO:0000269|PubMed:22286981}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; FR669447; CCF55024.1; -; Genomic_DNA.
DR AlphaFoldDB; H1ZV38; -.
DR SMR; H1ZV38; -.
DR KEGG; ag:CCF55024; -.
DR BioCyc; MetaCyc:MON-17740; -.
DR BRENDA; 1.1.1.347; 229.
DR UniPathway; UPA00137; -.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0018457; F:perillyl-alcohol dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:UniProtKB.
DR GO; GO:0043694; P:monoterpene catabolic process; TAS:UniProtKB.
DR GO; GO:0016098; P:monoterpenoid metabolic process; IDA:UniProtKB.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
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 Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
FT CHAIN 1..373
FT /note="Geraniol dehydrogenase"
FT /id="PRO_0000418648"
FT BINDING 47
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 67
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 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P11766"
FT BINDING 175
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 373 AA; 38274 MW; ADFDD2A270CCB121 CRC64;
MNDTQDFISA QAAVLRQVGG PLAVEPVRIS MPKGDEVLIR IAGVGVCHTD LVCRDGFPVP
LPIVLGHEGS GTVEAVGEQV RTLKPGDRVV LSFNSCGHCG NCHDGHPSNC LQMLPLNFGG
AQRVDGGQVL DGAGHPVQSM FFGQSSFGTH AVAREINAVK VGDDLPLELL GPLGCGIQTG
AGAAINSLGI GPGQSLAIFG GGGVGLSALL GARAVGADRV VVIEPNAARR ALALELGASH
ALDPHAEGDL VAAIKAATGG GATHSLDTTG LPPVIGSAIA CTLPGGTVGM VGLPAPDAPV
PATLLDLLSK SVTLRPITEG DADPQRFIPR MLDFHRAGKF PFDRLITRYR FDQINEALHA
TEKGEAIKPV LVF
