LIMC_RHOER
ID LIMC_RHOER Reviewed; 277 AA.
AC Q9RA05;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=(-)-trans-carveol dehydrogenase;
DE EC=1.1.1.n4;
DE AltName: Full=(4R,6S)-carveol dehydrogenase;
DE Short=CDH;
DE Short=Carveol dehydrogenase;
GN Name=limC;
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus;
OC Rhodococcus erythropolis group.
OX NCBI_TaxID=1833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-30, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, STEREOSPECIFICITY, ACTIVITY
RP REGULATION, INDUCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=DCL 14;
RX PubMed=10473585; DOI=10.1074/jbc.274.37.26296;
RA van der Werf M.J., van der Ven C., Barbirato F., Eppink M.H.M.,
RA de Bont J.A.M., van Berkel W.J.H.;
RT "Stereoselective carveol dehydrogenase from Rhodococcus erythropolis DCL14.
RT A novel nicotinoprotein belonging to the short-chain
RT dehydrogenase/reductase superfamily.";
RL J. Biol. Chem. 274:26296-26304(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DCL 14;
RA Van der Vlugt-Bergmans C.J.B., van der Werf M.J.;
RT "Genetic analysis of the lim operon of Rhodococcus erythropolis DCL14.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidation of carveol to carvone, with a strong
CC stereoselectivity since it efficiently converts only the (6S)-
CC stereoisomers, of which (-)-(4R,6S)-trans-carveol is the better
CC substrate. Displays a broad substrate specificity with a preference for
CC substituted cyclohexanols, and does not catalyze the oxidation of
CC primary or short chain aliphatic secondary alcohols. Is also able,
CC albeit more slowly, to oxidize limonene-1,2-diol into 1-hydroxy-2-
CC oxolimonene. {ECO:0000269|PubMed:10473585}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,5R)-carveol + NAD(+) = (R)-carvone + H(+) + NADH;
CC Xref=Rhea:RHEA:25844, ChEBI:CHEBI:15378, ChEBI:CHEBI:15389,
CC ChEBI:CHEBI:15400, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.n4;
CC Evidence={ECO:0000269|PubMed:10473585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(1S,5S)-carveol + NAD(+) = (S)-carvone + H(+) + NADH;
CC Xref=Rhea:RHEA:25848, ChEBI:CHEBI:232, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15399, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.n4;
CC Evidence={ECO:0000269|PubMed:10473585};
CC -!- ACTIVITY REGULATION: Competitively inhibited by the product (S)- or
CC (R)-carvone. {ECO:0000269|PubMed:10473585}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.041 mM for (4R,6S)-carveol {ECO:0000269|PubMed:10473585};
CC KM=0.39 mM for (4S,6S)-carveol {ECO:0000269|PubMed:10473585};
CC KM=0.35 mM for (4R,6R)-carveol {ECO:0000269|PubMed:10473585};
CC KM=2.0 mM for (4S,6R)-carveol {ECO:0000269|PubMed:10473585};
CC Vmax=4200 nmol/min/mg enzyme with (4R,6S)-carveol as substrate
CC {ECO:0000269|PubMed:10473585};
CC Vmax=3870 nmol/min/mg enzyme with (4S,6S)-carveol as substrate
CC {ECO:0000269|PubMed:10473585};
CC Vmax=1450 nmol/min/mg enzyme with (4R,6R)-carveol as substrate
CC {ECO:0000269|PubMed:10473585};
CC Vmax=1320 nmol/min/mg enzyme with (4S,6R)-carveol as substrate
CC {ECO:0000269|PubMed:10473585};
CC pH dependence:
CC Optimum pH is 5.5. Shows 25% of the optimal activity at pH 4.6 and
CC 7.0. {ECO:0000269|PubMed:10473585};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:10473585};
CC -!- PATHWAY: Terpene metabolism; limonene degradation.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10473585}.
CC -!- INDUCTION: By limonene and carveol. {ECO:0000269|PubMed:10473585}.
CC -!- MISCELLANEOUS: In vitro, is only active in the presence of the
CC artificial electron acceptor dichlorophenolindophenol (DCPIP). The
CC physiological electron acceptor that is used to regenerate NAD(+) in
CC vivo is unknown.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AJ006869; CAB54559.1; -; Genomic_DNA.
DR EMBL; AJ272366; CAC20856.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RA05; -.
DR SMR; Q9RA05; -.
DR KEGG; ag:CAB54559; -.
DR BioCyc; MetaCyc:MON-13961; -.
DR UniPathway; UPA00888; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0046251; P:limonene catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR023985; SDR_subfam_1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03971; SDR_subfam_1; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10473585"
FT CHAIN 2..277
FT /note="(-)-trans-carveol dehydrogenase"
FT /id="PRO_0000054718"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 10..32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 277 AA; 29531 MW; 6C4F261788FC971A CRC64;
MARVEGQVAL ITGAARGQGR SHAIKLAEEG ADVILVDVPN DVVDIGYPLG TADELDQTAK
DVENLGRKAI VIHADVRDLE SLTAEVDRAV STLGRLDIVS ANAGIASVPF LSHDIPDNTW
RQMIDINLTG VWHTAKVAVP HILAGERGGS IVLTSSAAGL KGYAQISHYS AAKHGVVGLM
RSLALELAPH RVRVNSLHPT QVNTPMIQNE GTYRIFSPDL ENPTREDFEI ASTTTNALPI
PWVESVDVSN ALLFLVSEDA RYITGAAIPV DAGTTLK
