ID A8TRT6_9PROT Unreviewed; 537 AA.
AC A8TRT6;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:EDP64618.1};
GN ORFNames=BAL199_27711 {ECO:0000313|EMBL:EDP64618.1};
OS alpha proteobacterium BAL199.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP64618.1, ECO:0000313|Proteomes:UP000003417};
RN [1] {ECO:0000313|EMBL:EDP64618.1, ECO:0000313|Proteomes:UP000003417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP64618.1,
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 -!- 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:EDP64618.1}.
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; ABHC01000008; EDP64618.1; -; Genomic_DNA.
DR AlphaFoldDB; A8TRT6; -.
DR STRING; 331869.BAL199_27711; -.
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|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000003417}.
FT DOMAIN 84..107
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 256..270
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 537 AA; 57698 MW; 83C942A48D506274 CRC64;
MAADATWDYI IVGAGSAGCV LANRLTENGR YKVLLLEAGP KDRSLWIPMP VGFYKLLTSK
TYNWGFVTEP EAGTGNRPIA TPRGKTLGGS SAINGVLYVR GQPLDYDTWS QLGNRGWSYD
SVLPYFRKSE TYTNGGDDSR GTDGPLGVTE TTERHELLDA FVDAAESQGF PRNSDYNNGD
QEGFGYYQLT ARGGRRVSTA KAFLHPAKGR ANLTIETGAF ATGLLFDGTR AAGVAYTVNG
QKREARAGRE VILAAGAVQS PQLLELSGIG APEILKRQGI EVRHALPGVG ENYRDHYGTR
MRWRVTKPIT LNELTRGPNL VREVIRWGLT GQGVLGYGAG IIFGFVKTRP ELETPDVQFH
LAHASYADAA TRKLEKEPGM TLAVCPLRSE SRGSIHIKSA DPAAPPAIRG NFLSDPVDVA
AIVEGMKIGR QIAEAAPLDP YRAFEMTPGP DCATDADFEA YARQTGQTLY HIVGTAKMGP
ATDGQAVVDD RLRVHGVPGL RVVDASIMPT LVSGNTNAAA IMIGEKGSAM ILEDAQV
//
