ID A0A1G3E8W8_9GAMM Unreviewed; 673 AA.
AC A0A1G3E8W8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
DE Flags: Fragment;
GN ORFNames=A2Y50_05190 {ECO:0000313|EMBL:OHC28433.1};
OS Pseudomonadales bacterium RIFCSPLOWO2_12_59_9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales.
OX NCBI_TaxID=1802009 {ECO:0000313|EMBL:OHC28433.1, ECO:0000313|Proteomes:UP000179365};
RN [1] {ECO:0000313|EMBL:OHC28433.1, ECO:0000313|Proteomes:UP000179365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OHC28433.1}.
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DR EMBL; MHZN01000163; OHC28433.1; -; Genomic_DNA.
DR STRING; 1802009.A2Y50_05190; -.
DR Proteomes; UP000179365; 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; 4.
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; 2.
DR Pfam; PF00732; GMC_oxred_N; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR PROSITE; PS00624; GMC_OXRED_2; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 75..89
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT DOMAIN 399..413
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OHC28433.1"
SQ SEQUENCE 673 AA; 72863 MW; 74C970C45EE5316B CRC64;
YQVTQFFHGP KNGERCSAAA AYLHPAMHRP NLTVLTNTQA LRVMLADKRA TGVEVQRAGQ
RQIIHADKEV ILCGGAFNSP QLLMLSGIGD PAELTRHGIQ VQHELPGVGK NLQDHLHFIL
TFQSKDSDLL GISPTAAIRL PAAINEWRKT GKGLLASPCA ESGGFVKSDP QLERADLQLN
FVIAMLDDHG RKLHYGNGFS AHVCVLRPKS LGEVGLYDNN PLSAPRIDPK FLSHADDVTA
MLRGARLLQK IMQAPALAEF REEEVRAAEG DSDEALLKHI RAHADTIYHP VGSCKMGTDP
LAVVDPQLRV HGISGLRVVD ASIMPTLIGG NTNAPTIMIA ERAXXXLHPA MHRPNLTVLT
NTQALRVMLA DKRATGVEVQ RAGQRQIIHA DKEVILCGGA FNSPQLLMLS GIGDPAELTR
HGIQVQHELP GVGKNLQDHL DFILTFKSKD SDLLGISPTA AIRLPAAINE WRKTGKGLLA
SPCAESGGFV KSDPQLERAD LQLNFVIAML DDHGRKLHYG NGFSAHVCVL RPKSLGEVGL
YDNNPLSAPR IDPKFLSHAD DVTAMLRGAR LLQKIMQAPA LAEFREEEVR AAEGDSDEAL
LKHIRAHADT IYHPVGSCKM GTDPLAVVDP QLRVHGISGL RVVDASIMPT LIGGNTNAPT
IMIAERAAAF IRA
//
