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CHNA_RHOS6
ID   CHNA_RHOS6              Reviewed;         270 AA.
AC   Q6TMA3;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Cyclohexanol dehydrogenase {ECO:0000303|Ref.2};
DE            EC=1.1.1.245 {ECO:0000269|Ref.1, ECO:0000269|Ref.2};
DE   AltName: Full=Cyclohexanol dehydrogenase II {ECO:0000303|Ref.2};
DE            Short=CHD II {ECO:0000303|Ref.2};
GN   Name=chnA {ECO:0000303|Ref.1};
OS   Rhodococcus sp. (strain TK6).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=249095;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RA   Choi J.-H., Kim T.-K., Kim Y.-M., Kim W.-C., Joo G.-J., Lee K.Y.,
RA   Rhee I.-K.;
RT   "Cloning and characterization of cyclohexanol dehydrogenase gene from
RT   Rhodococcus sp. TK6.";
RL   J. Microbiol. Biotechnol. 15:1189-1196(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 10-24, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION,
RP   AND INDUCTION.
RA   Kim T.-K., Choi J.-H., Rhee I.-K.;
RT   "Purification and characterization of a cyclohexanol dehydrogenase from
RT   Rhodococcus sp. TK6.";
RL   J. Microbiol. Biotechnol. 12:39-45(2002).
CC   -!- FUNCTION: Catalyzes the oxidation of cyclohexanol to cyclohexanone. Can
CC       also use a broad range of other alcohols, including trans-cyclohexane-
CC       1,2-diol, trans-cyclopentane-1,2-diol, cyclopentanol, hexane-1,2-diol,
CC       ethanol, 1-propanol, 1-butanol, 1-pentanol and 1-hexanol.
CC       {ECO:0000269|Ref.1, ECO:0000269|Ref.2}.
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|Ref.1, ECO:0000269|Ref.2};
CC   -!- ACTIVITY REGULATION: Activity is enhanced by the addition of Ba(2+) and
CC       Mg(2+), but inhibited by the addition of Al(3+), Ca(2+), Co(2+),
CC       Cu(2+), Mn(2+) and Zn(2+). {ECO:0000269|Ref.2}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.7 mM for cyclohexanol {ECO:0000269|Ref.2};
CC         KM=2.8 mM for trans-cyclohexane-1,2-diol {ECO:0000269|Ref.2};
CC         KM=14.2 mM for cyclopentanol {ECO:0000269|Ref.2};
CC         KM=13.7 mM for trans-cyclopentane-1,2-diol {ECO:0000269|Ref.2};
CC         KM=13.5 mM for hexane-1,2-diol {ECO:0000269|Ref.2};
CC       pH dependence:
CC         Optimum pH is 8.0 (Ref.1). Stable between pH 7.5 and 8.5 (Ref.2).
CC         {ECO:0000269|Ref.1, ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Rapidly inactivated at temperatures above 40 degrees Celsius.
CC         {ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|Ref.2}.
CC   -!- INDUCTION: Induced by cyclohexanol. {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AY394000; AAR27575.1; -; Genomic_DNA.
DR   SMR; Q6TMA3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN           1..270
FT                   /note="Cyclohexanol dehydrogenase"
FT                   /id="PRO_0000453523"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT   BINDING         19..21
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT   BINDING         40
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT   BINDING         78..79
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT   BINDING         105
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT   BINDING         176
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT   BINDING         180
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P9WGT1"
FT   CONFLICT        10
FT                   /note="K -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        13
FT                   /note="L -> H (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   270 AA;  28376 MW;  862540D116FC718B CRC64;
     MTDNLPLRGK VALVTGAARG IGRAYALRLA KRGADVAVVD FDLHSYKDYQ LEAASMRGDT
     VVDEIREIGM RALGFQADVT DATTLNEAVQ QIVGEWGRLD IAICNAGGGV GSPEETRASI
     VEKDLVDVVV ARNLTGTIHT CQAVAVPMKE QRSGKIVTVG SQAGHRIEDN GGYAHYGAAK
     AAVAKYTQYL ARDLGPFGVT VNCVAPGYIS TGRLAPILSA MGDAQLLDDV PLGRYGTPED
     CAGVIEFLSS DLSDYVTGAI IPVDGGLTYS
 
 
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