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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//