ID   SDH_GLUOY               Reviewed;         531 AA.
AC   Q47944;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=L-sorbose 1-dehydrogenase;
DE            Short=SDH;
DE            EC=1.1.99.32;
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=T-100;
RX   PubMed=9023923; DOI=10.1128/aem.63.2.454-460.1997;
RA   Saito Y., Ishii Y., Hayashi H., Imao Y., Akashi T., Yoshikawa K.,
RA   Noguchi Y., Soeda S., Yoshida M., Niwa M., Hosoda J., Shimomura K.;
RT   "Cloning of genes coding for L-sorbose and L-sorbosone dehydrogenases from
RT   Gluconobacter oxydans and microbial production of 2-keto-L-gulonate, a
RT   precursor of L-ascorbic acid, in a recombinant G. oxydans strain.";
RL   Appl. Environ. Microbiol. 63:454-460(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + L-sorbopyranose = 1-dehydro-L-sorbose + AH2;
CC         Xref=Rhea:RHEA:24878, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:48649, ChEBI:CHEBI:48657; EC=1.1.99.32;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   EMBL; D86622; BAA13145.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47944; -.
DR   SMR; Q47944; -.
DR   BioCyc; MetaCyc:MON-13711; -.
DR   BRENDA; 1.1.99.32; 38.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; PTHR11552; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..531
FT                   /note="L-sorbose 1-dehydrogenase"
FT                   /id="PRO_0000338412"
FT   ACT_SITE        469
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
SQ   SEQUENCE   531 AA;  57624 MW;  D5E0429ECF0C437E CRC64;
     MTSGFDYIVV GGGSAGCVLA ARLSENPSVR VCLIEAGRRD THPLIHMPVG FAKMTTGPHT
     WDLLTEPQKH ANNRQIPYVQ GRILGGGSSI NAEVFTRGHP SDFDRWAAEG ADGWSFRDVQ
     KYFIRSEGNA VFSGTWHGTN GPLGVSNLAE PNPTSRAFVQ SCQEMGLPYN PDFNGASQEG
     AGIYQMTIRN NRRCSTAVGY LRPALGRKNL TVVTRALVLK IVFNGTRATG VQYIANGTLN
     TAEASQEIVV TAGAIGTPKL MMLSGVGPAA HLRENGIPVV QDLPGVGENL QDHFGVDIVA
     ELKTDESFDK YRKLHWMLWA GLEYTMFRSG PVASNVVEGG AFWYSDPSSG VPDLQFHFLA
     EAGAEAGVTS VPKGASGITL NSYVLRPKSR GTVRLRSADP RVNPMVDPNF LGDPADLETS
     AEGVRLSYEM FSQPSLEKHI RKTCFFSGKQ PTMQMYRDYA REHGRTSYHP TCTCKMGRDD
     MSVVDPRLKV HGLEGIRICD SSVMPSLLGS NTNAATIMIS ERAADFIQGN A