CPNA_COMS9
ID CPNA_COMS9 Reviewed; 250 AA.
AC Q8GAV9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Cyclopentanol dehydrogenase {ECO:0000303|PubMed:12406764};
DE EC=1.1.1.163 {ECO:0000269|PubMed:12406764};
DE AltName: Full=Cyclohexanol dehydrogenase {ECO:0000303|PubMed:12406764};
DE EC=1.1.1.245 {ECO:0000269|PubMed:12406764};
GN Name=cpnA {ECO:0000303|PubMed:12406764};
OS Comamonas sp. (strain NCIMB 9872).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas; unclassified Comamonas.
OX NCBI_TaxID=213664;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12406764; DOI=10.1128/aem.68.11.5671-5684.2002;
RA Iwaki H., Hasegawa Y., Wang S., Kayser M.M., Lau P.C.K.;
RT "Cloning and characterization of a gene cluster involved in cyclopentanol
RT metabolism in Comamonas sp. strain NCIMB 9872 and biotransformations
RT effected by Escherichia coli-expressed cyclopentanone 1,2-monooxygenase.";
RL Appl. Environ. Microbiol. 68:5671-5684(2002).
RN [2]
RP ERRATUM OF PUBMED:12406764.
RA Iwaki H., Hasegawa Y., Wang S., Kayser M.M., Lau P.C.K.;
RL Appl. Environ. Microbiol. 69:2414-2414(2003).
CC -!- FUNCTION: Catalyzes the oxidation of cyclopentanol to cyclopentanone
CC and cyclohexanol to cyclohexanone. The activity toward cyclohexanol is
CC 60% that of cyclopentanol. {ECO:0000269|PubMed:12406764}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclopentanol + NAD(+) = cyclopentanone + H(+) + NADH;
CC Xref=Rhea:RHEA:11728, ChEBI:CHEBI:15378, ChEBI:CHEBI:16133,
CC ChEBI:CHEBI:16486, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.163; Evidence={ECO:0000269|PubMed:12406764};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclohexanol + NAD(+) = cyclohexanone + H(+) + NADH;
CC Xref=Rhea:RHEA:10044, ChEBI:CHEBI:15378, ChEBI:CHEBI:17854,
CC ChEBI:CHEBI:18099, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.245; Evidence={ECO:0000269|PubMed:12406764};
CC -!- PATHWAY: Alcohol metabolism; cyclopentanol degradation; 5-valerolactone
CC from cyclopentanol: step 1/2.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AB073151; BAC22653.1; -; Genomic_DNA.
DR EMBL; AB022102; BAC01270.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GAV9; -.
DR SMR; Q8GAV9; -.
DR KEGG; ag:BAC22653; -.
DR BioCyc; MetaCyc:MON-7722; -.
DR UniPathway; UPA00764; UER00749.
DR GO; GO:0018460; F:cyclohexanol dehydrogenase activity; IEA:RHEA.
DR GO; GO:0055041; F:cyclopentanol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0033022; P:cyclopentanol catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase.
FT CHAIN 1..250
FT /note="Cyclopentanol dehydrogenase"
FT /id="PRO_0000054551"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 16..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 63..64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 155
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT BINDING 185..193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P9WGT1"
SQ SEQUENCE 250 AA; 26626 MW; 7C42C3CBAEBB858E CRC64;
MGRVNDKVVL VTGGAMGMGL THCTLLAREG ATVYLSDMNE ELGHQAVAEI RRQGGKAHFL
HLDVTNENHW TGAVDTILAE SDRLDALVNN AGILTLKPVQ DTSNEEWDRI FEINVRSVFL
GTRAVIEPMR KAHKGCIVNV SSIYGLVGAP GAAAYEASKG AVRLFTKACA VDLAPFNIRV
NSVHPGVIAT PMTQQILDAP QSARALLGPT LLGRAAQPME VSQAVLFLVS DEASFVHGSE
LVVDGGYTAN
