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SLDB_GLUOX
ID   SLDB_GLUOX              Reviewed;         126 AA.
AC   Q70JP0; Q5FSL7;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Glycerol dehydrogenase small subunit;
DE            EC=1.1.99.22;
DE   AltName: Full=D-arabitol dehydrogenase small subunit;
DE            Short=ARDH;
DE   AltName: Full=D-sorbitol dehydrogenase subunit SldB;
DE            Short=SLDH;
DE   AltName: Full=Gluconate/polyol dehydrogenase small subunit;
GN   Name=sldB; Synonyms=g5dhA; OrderedLocusNames=GOX0855;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 621 / DSM 50049 / NBRC 3172 / NCIMB 7069 / NRRL B-72;
RX   PubMed=15060755; DOI=10.1007/s00253-004-1594-6;
RA   Salusjaervi T., Povelainen M., Hvorslev N., Eneyskaya E.E.,
RA   Kulminskaya A.A., Shabalin K.A., Neustroev K.N., Kalkkinen N.,
RA   Miasnikov A.N.;
RT   "Cloning of a gluconate/polyol dehydrogenase gene from Gluconobacter
RT   suboxydans IFO 12528, characterisation of the enzyme and its use for the
RT   production of 5-ketogluconate in a recombinant Escherichia coli strain.";
RL   Appl. Microbiol. Biotechnol. 65:306-314(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
CC   -!- FUNCTION: Catalyzes the oxidation of glycerol to glycerone. Also acts,
CC       more slowly, on a number of other polyols including D-sorbitol, D-
CC       arabinitol, D-mannitol, meso-erythritol, adonitol and propylene glycol
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + glycerol = AH2 + dihydroxyacetone; Xref=Rhea:RHEA:17493,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:16016, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:17754; EC=1.1.99.22;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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DR   EMBL; AJ577472; CAE12057.1; -; Genomic_DNA.
DR   EMBL; CP000009; AAW60629.1; -; Genomic_DNA.
DR   RefSeq; WP_011252425.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q70JP0; -.
DR   STRING; 290633.GOX0855; -.
DR   EnsemblBacteria; AAW60629; AAW60629; GOX0855.
DR   GeneID; 56905171; -.
DR   KEGG; gox:GOX0855; -.
DR   eggNOG; COG4993; Bacteria.
DR   HOGENOM; CLU_146618_0_0_5; -.
DR   BRENDA; 1.1.1.69; 38.
DR   BRENDA; 1.1.99.21; 38.
DR   Proteomes; UP000006375; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047955; F:glycerol dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..126
FT                   /note="Glycerol dehydrogenase small subunit"
FT                   /id="PRO_0000076319"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   126 AA;  13724 MW;  16DB804354615412 CRC64;
     MPNTYGSRTL TEWLTLVLGV VIILVGLFFV IAGADLAMLG GSVYYVICGI PLVAGGVFML
     MGRTLGAFLY LGALAYTWVW SLWEVGFSPV DLLPRDFGPT LLGILVALTI PVLRRMETRR
     TLRGTV
 
 
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