ID A8TJY0_9PROT Unreviewed; 535 AA.
AC A8TJY0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=GMC type oxidoreductase {ECO:0000313|EMBL:EDP66918.1};
GN ORFNames=BAL199_17693 {ECO:0000313|EMBL:EDP66918.1};
OS alpha proteobacterium BAL199.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP66918.1, ECO:0000313|Proteomes:UP000003417};
RN [1] {ECO:0000313|EMBL:EDP66918.1, ECO:0000313|Proteomes:UP000003417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP66918.1,
RC ECO:0000313|Proteomes:UP000003417};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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:EDP66918.1}.
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DR EMBL; ABHC01000001; EDP66918.1; -; Genomic_DNA.
DR AlphaFoldDB; A8TJY0; -.
DR STRING; 331869.BAL199_17693; -.
DR eggNOG; COG2303; Bacteria.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000003417; 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.
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:UP000003417}.
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 88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 535 AA; 57550 MW; D42651EDB2F78E97 CRC64;
MTSSGPDAWD YIIVGAGSAG CVLANRLSAD PGNRVLVLEA GGSDAHPYVR APVGFLKTFQ
DPRFNWCYTT EPGAGVDNRA IFFPRGKVLG GSSSINGHLY VRGQARDFDT WAQLGNRGWS
YDDVLPYFRR AEDRSSGSDA YHGTGGPQHV SDIQERHPIC EAFIAGAAAA GVPRNADYNG
AVQEGVGYYQ RTIRGGRRHS AATGFLHPVR NRRNLRVESH AQVLRVEVDG TRATGVTWRQ
HGKVYRSVAG AEVILSAGAI NTPHLLQVSG IGSGERLRRL GIPVVHDLPG VGEGLQDHYA
IRVVHRVTKP ITLNERARGP RLWWEIARWL ATGGGLLAFS PAHVGAFVRS HPELELPDLQ
FVFTPASYSD GVVGQLQREP GMTIGVWQMR PDSRGYVRAR SADPDAAPAI QPNYLSAESD
REAVVDGLRW ARRLLASSAL EPYRGPETLP GPHVQSNSEL LGYARAKGAT VYHAIGTCRM
GSDPGAVVSP DLRLNGLSGI RVVDASVMPT MVSANTNAAT LMIAEKAADL ILAAG
//
