ID A0A094LAT3_9GAMM Unreviewed; 536 AA.
AC A0A094LAT3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN ORFNames=IDSA_04630 {ECO:0000313|EMBL:KFZ31968.1};
OS Pseudidiomarina salinarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=435908 {ECO:0000313|EMBL:KFZ31968.1, ECO:0000313|Proteomes:UP000054363};
RN [1] {ECO:0000313|EMBL:KFZ31968.1, ECO:0000313|Proteomes:UP000054363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISL-52 {ECO:0000313|EMBL:KFZ31968.1,
RC ECO:0000313|Proteomes:UP000054363};
RA Du J., Shao Z.;
RT "The draft genome sequence of Idiomarina salinarum ISL-52.";
RL Submitted (JUN-2014) 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, ECO:0000256|RuleBase:RU003968}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFZ31968.1}.
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DR EMBL; JPER01000001; KFZ31968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094LAT3; -.
DR STRING; 435908.IDSA_04630; -.
DR eggNOG; COG2303; Bacteria.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000054363; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 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: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; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 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,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000054363}.
FT DOMAIN 86..109
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 258..272
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 536 AA; 58608 MW; B93150A2AEA2712E CRC64;
MAGHRYEYDY IIIGGGSAGC VLAERLSADG RFSIGLFEAG GSGQSPFSTM PGGVARFMHS
RKFNWRYRSQ DKAPLRDGNG LYTPRGKGLG GSSAINAMIY TRGAPSDYDE WARLSSEDWN
WRNMLQRFRK LEANQRGADG YHGDSGPIHV SDCPPHFPVA RQFLKAAESA GIPLNPDFNG
AELYGAGPYQ FTIYNQQRWS ARKAFLEPAL KRSNLEVHTN CLVRKITSTE GLITGIEVQR
GRDSFLARAK REVILSAGAF NSPHLLKLSG IGPAAELSSF GIPLVADRPE VGENLQEHVD
ILLQYRNRKR DGISLNFRGL LKLAAGCWQY ARHRTGPMAQ PPVEVGAFLK SSAAVTTPDI
QLHLIAACFN DSGYDLTPAL RDRFGCHVCV LRPKARGKVY LRSADPNQPP GFSYDFLQHR
EDREVLLAGV KQAQGIMQQQ PLAAHNGGEV FPGSCESDEE LLAKLQQQAG LIYHPTSTCR
MGNDADSVVD PQLRVRGVKG LRVVDASVMP RVVSGNTNAP TIAIADQGAD FILADA
//
