ID   SLDB_GLUTH              Reviewed;         126 AA.
AC   Q8L1D5;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 52.
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;
OS   Gluconobacter thailandicus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=257438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 3255 / JCM 20465 / IAM 12306 / LMG 1487;
RX   PubMed=12686146; DOI=10.1016/s1570-9639(03)00071-2;
RA   Hoshino T., Sugisawa T., Shinjoh M., Tomiyama N., Miyazaki T.;
RT   "Membrane-bound D-sorbitol dehydrogenase of Gluconobacter suboxydans IFO
RT   3255 -- enzymatic and genetic characterization.";
RL   Biochim. Biophys. Acta 1647:278-288(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-11, AND CHARACTERIZATION.
RC   STRAIN=NBRC 3255 / JCM 20465 / IAM 12306 / LMG 1487;
RX   PubMed=12676670; DOI=10.1128/aem.69.4.1959-1966.2003;
RA   Matsushita K., Fujii Y., Ano Y., Toyama H., Shinjoh M., Tomiyama N.,
RA   Miyazaki T., Sugisawa T., Hoshino T., Adachi O.;
RT   "5-keto-D-gluconate production is catalyzed by a quinoprotein glycerol
RT   dehydrogenase, major polyol dehydrogenase, in gluconobacter species.";
RL   Appl. Environ. Microbiol. 69:1959-1966(2003).
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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB065091; BAC02908.1; -; Genomic_DNA.
DR   RefSeq; WP_007281753.1; NZ_LHZS01000106.1.
DR   AlphaFoldDB; Q8L1D5; -.
DR   SMR; Q8L1D5; -.
DR   PATRIC; fig|257438.4.peg.3128; -.
DR   BioCyc; MetaCyc:MON-13709; -.
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   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Membrane; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12676670"
FT   CHAIN           2..126
FT                   /note="Glycerol dehydrogenase small subunit"
FT                   /id="PRO_0000076320"
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;  13736 MW;  BB4D1492FB83ED86 CRC64;
     MPNLQGNRTL TEWLTLLLGV IVLLVGLFFV IGGADLAMLG GSTYYVLCGI LLVASGVFML
     MGRTLGAFLY LGALAYTWVW SFWEVGFSPI DLLPRAFGPT ILGILVALTI PVLRRMESRR
     TLRGAV