ID   SLDA_GLUOX              Reviewed;         743 AA.
AC   Q70JN9; Q5FSL8;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
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; Synonyms=ga5dhB; OrderedLocusNames=GOX0854;
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   -!- COFACTOR:
CC       Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC         Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ577472; CAE12058.1; -; Genomic_DNA.
DR   EMBL; CP000009; AAW60628.1; -; Genomic_DNA.
DR   RefSeq; WP_011252424.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q70JN9; -.
DR   SMR; Q70JN9; -.
DR   STRING; 290633.GOX0854; -.
DR   EnsemblBacteria; AAW60628; AAW60628; GOX0854.
DR   KEGG; gox:GOX0854; -.
DR   eggNOG; COG4993; Bacteria.
DR   HOGENOM; CLU_018478_1_0_5; -.
DR   OMA; GGHHFME; -.
DR   BRENDA; 1.1.1.69; 38.
DR   BRENDA; 1.1.99.21; 38.
DR   Proteomes; UP000006375; Chromosome.
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   3: Inferred from homology;
KW   Oxidoreductase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..743
FT                   /note="Glycerol dehydrogenase large subunit"
FT                   /id="PRO_0000045857"
FT   REGION          27..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..463
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   743 AA;  79562 MW;  FCD88F07B68BAD87 CRC64;
     MRRSHLLATV ACATLACAPL AANAQFAPAG SGGSPTSSVP GPGNGSGNSF EPTENTPAAK
     SRFSGPSPYA PQAPGVNAAN LPDIGSMDPN DVPQMAPQQS ASPASGDWAA YGHDDSQMRY
     SPLSEITPQN ADQLKVAFVY HTGSYPRPGQ TNKWAAETTP IKVGDGLYMC SAQNDIMKID
     PATGKEIWRH NINEKYEAIP YTAACKGVTY FTSSQVPEGQ PCHNRILEGT LDMRLIAVDA
     ATGNLCEGFG NGGQVNLMQG LGESVPGFVS MTTPPPVVNG VVVVNHEVLD GQRRWAPSGV
     IRGYDAESGK FLWAWDVNRP NDHSQPTGNN HYSRGTPNSW AAMTGDNALG LVYVPTGNSA
     SDYYSALRSP EENKVSSAVV ALDVKTGSPR WVFQTVHKDV WDYDIGSQAT LMDMPGQDGQ
     PVPALIMPTK RGQTFVLDRR DGKPILPVEE RPAPSPGVIP GDPRSPTQPW STGMPALRVP
     DLKETDMWGM SPIDQLFCRI KFRRANYTGE FTPPSVDKPW IEYPGYNGGS DWGSVSYDPQ
     SGILIANWNI TPMYDQLVTR KKADELGLMP IDDPNYKPGG GGAEGNGAMD GTPYGIVVTP
     FWDQYTGMMC NRPPYGMITA IDMKHGQKVL WQHPLGTARA NGPWGLPTGL PWEIGTPNNG
     GSVVTAGGVV FIAAATDNQI RAIDEHTGKV VWSAVLPGGG QANPMTYEAN GHQYVAIMAG
     GHHFMMTPVS DQLVVYALPD HKG