ID   SLDA_GLUTH              Reviewed;         740 AA.
AC   Q8KIL1;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Glycerol dehydrogenase large subunit;
DE            EC=1.1.99.22;
DE   AltName: Full=D-arabitol dehydrogenase large subunit;
DE            Short=ARDH;
DE   AltName: Full=D-sorbitol dehydrogenase subunit SldA;
DE            Short=SLDH;
DE   AltName: Full=Gluconate/polyol dehydrogenase large subunit;
DE   Flags: Precursor;
GN   Name=sldA;
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 30-39, 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   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC02909.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB065091; BAC02909.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q8KIL1; -.
DR   SMR; Q8KIL1; -.
DR   BioCyc; MetaCyc:MON-13708; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0047955; F:glycerol dehydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   CDD; cd10280; PQQ_mGDH; 1.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR017511; PQQ_mDH.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   PANTHER; PTHR32303:SF4; PTHR32303:SF4; 1.
DR   Pfam; PF13360; PQQ_2; 2.
DR   SMART; SM00564; PQQ; 4.
DR   SUPFAM; SSF50998; SSF50998; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:12676670"
FT   CHAIN           30..740
FT                   /note="Glycerol dehydrogenase large subunit"
FT                   /id="PRO_0000045858"
FT   REGION          28..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..459
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   740 AA;  79499 MW;  E7CD78737CDEDF59 CRC64;
     MRRPYLLATA AGLALACSPL IAHAQFAPAG AGGEPSSSVP GPGNASEPTE NSPKSQSYFA
     GPSPYAPQAP GVNAANLPDI ESIDPSQVPA MAPQQSANPA RGDWVAYGRD DHQTRYSPLS
     EITPENASKL KVAFVYHTGS YPRPGQVNKW AAETTPIKVG DGLYTCSAMN DIIKLDPATG
     KQIWRRNVDV KYHSIPYTAA CKGVTYFTSS VVPEGQPCHN RLIEGTLDMR LIAVDAETGD
     FCPNFGHGGQ VNLMQGLGES VPGFVSMTAP PPVINGVVVV NHEVLDGQRR WAPSGVIRGY
     DAESGKFVWA WDVNNSDDHS QPTGNRHYSR GTPNSWATMT GDNEEGLVYV PTGNSAADYY
     SALRSDAENK VSSAVVAIDV KTGSPRWVFQ TAHKDVWDYD IGSQATLMDM PGPDGQTVPA
     LIMPTKRGQT FVLDRRTGKP ILPVEERPAP SPGVIPGDPR SPTQPWSVGM PALRVPDLKE
     TDMWGMSPID QLFCRIKFRR ANYVGEFTPP SVDKPWIEYP GYNGGSDWGS MSYDPQSGIL
     IANWNITPMY DQLVTRKKAD SLGLMPIDDP NFKPGGGGAE GNGAMDGTPY GIVVTPFWDQ
     YTGMMCNRPP YGMITAIDMK HGQKVLWQHP LGTARANGPW GLPTGLPWEI GTPNNGGSVV
     TGGGLIFIGA ATDNQIRAID EHTGKVVWSA VLPGGGQANP MTYEANGHQY VAIMAGGHHF
     MMTPVSDQLV VYALPDAIKQ