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Database: UniProt
Entry: A0A158CSC0_9BURK
LinkDB: A0A158CSC0_9BURK
Original site: A0A158CSC0_9BURK 
ID   A0A158CSC0_9BURK        Unreviewed;       578 AA.
AC   A0A158CSC0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Sorbose dehydrogenase {ECO:0000313|EMBL:SAK85272.1};
GN   ORFNames=AWB75_05664 {ECO:0000313|EMBL:SAK85272.1};
OS   Caballeronia catudaia.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1777136 {ECO:0000313|EMBL:SAK85272.1, ECO:0000313|Proteomes:UP000054870};
RN   [1] {ECO:0000313|EMBL:SAK85272.1, ECO:0000313|Proteomes:UP000054870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29318 {ECO:0000313|EMBL:SAK85272.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; FCOF02000039; SAK85272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158CSC0; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000054870; Unassembled WGS sequence.
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; 3.30.410.40; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT   DOMAIN          262..276
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         89
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         227
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   578 AA;  61720 MW;  A8F5A70453B81BD0 CRC64;
     MHIEKAYDYL IVGAGSAGCV LASRLTEDGR RSVLLLEAGE DYLPGEEPAD IVDPYPLSSY
     NPSYMWDGLK AFWHNSTHGA PAGFPQAKVM GGGSAVAGMV AFRGTPDDYN EWQAMGAAGW
     SWDSVLPYFS KLETDQDFSD SLHGRRGPVP IRRVPRNMWP PLTSAIEQYA KASGYPFIAD
     MNGDFRDGFG ATPISNTANS RVTTAAAYLT SSVRQRPNLT ILSRACVRSV RFSDKRATGV
     LAEVDGRLIE FAARAEVIVT AGAIHSPALL MRSGIGEGGA LQKLGISVVA DLDGVGKNLR
     NHAAVFICAM LHRNSRQSSS LRTHPTACMR MSSNLLGAPK SDLYINIQSK TSWNAMGTRV
     ASLNAVLLKP AGSGQVSLNV HDANQSPRVE FGFGDNARDI ERLSKAVLRI LNILKSPVVA
     PLVGAPFVVR VGDRIRRWNT HTASSAVNAR AFATLLDAMP SALGDRVLAA LTGHRLDSER
     LISDPTFLLN FVTREITGVY HPVGTCRMGN HTDPAAVVDS AGRVLGVANL RVADASIMPT
     IPRGNTNIPT IMVAEKLSDA IVKGETTAIS GASIGSAT
//
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