ID   SLDA2_GLUOX             Reviewed;         740 AA.
AC   Q8KIL1;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Glycerol dehydrogenase large subunit;
DE            EC=1.1.99.22;
DE   AltName: Full=Gluconate/polyol dehydrogenase large subunit;
DE   AltName: Full=D-sorbitol dehydrogenase subunit sldA;
DE            Short=SLDH;
DE   AltName: Full=D-arabitol dehydrogenase large subunit;
DE            Short=ARDH;
DE   Flags: Precursor;
GN   Name=sldA;
OS   Gluconobacter oxydans (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IFO 3255 / IAM 12306 / LMG 1487;
RX   MEDLINE=22572686; 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
RT   IFO 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=IFO 3257 / LMG 1489;
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
CC       acts, more slowly, on a number of other polyols including D-
CC       sorbitol, D-arabinitol, D-mannitol, meso-erythritol, adonitol and
CC       propylene glycol.
CC   -!- CATALYTIC ACTIVITY: Glycerol + acceptor = glycerone + reduced
CC       acceptor.
CC   -!- COFACTOR: PQQ.
CC   -!- SUBCELLULAR LOCATION: Secreted (Probable).
CC   -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC02909.1; Type=Frameshift; Positions=317, 325, 339, 354;
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DR   EMBL; AB065091; BAC02909.1; ALT_FRAME; Genomic_DNA.
DR   BioCyc; MetaCyc:MON-13708; -.
DR   BRENDA; 1.1.1.14; 275912.
DR   BRENDA; 1.1.99.22; 3050.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0047955; F:glycerol dehydrogenase (acceptor) activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR019556; PQQ-dependent_C.
DR   InterPro; IPR019551; PQQ-dependent_N.
DR   InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR   InterPro; IPR002372; PQQ_repeat.
DR   InterPro; IPR011047; Quino_AlcDH-like.
DR   InterPro; IPR001479; Quinoprotein_DH_CS.
DR   Gene3D; G3DSA:2.140.10.10; Quinoprotein_alc_DH-like; 1.
DR   Pfam; PF01011; PQQ; 2.
DR   Pfam; PF10535; PQQ_C; 1.
DR   Pfam; PF10527; PQQ_N; 1.
DR   SMART; SM00564; PQQ; 4.
DR   PROSITE; PS00363; BACTERIAL_PQQ_1; FALSE_NEG.
DR   PROSITE; PS00364; BACTERIAL_PQQ_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Oxidoreductase; Secreted; Signal.
FT   SIGNAL        1     29
FT   CHAIN        30    740       Glycerol dehydrogenase large subunit.
FT                                /FTId=PRO_0000045858.
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
//