ID D2S2V0_HALTV Unreviewed; 529 AA.
AC D2S2V0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:ADB63697.1};
GN OrderedLocusNames=Htur_4961 {ECO:0000313|EMBL:ADB63697.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OG Plasmid pHTUR03 {ECO:0000313|EMBL:ADB63697.1,
OG ECO:0000313|Proteomes:UP000001903}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB63697.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB63697.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RC PLASMID=pHTUR03 {ECO:0000313|EMBL:ADB63697.1,
RC ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
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}.
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DR EMBL; CP001863; ADB63697.1; -; Genomic_DNA.
DR AlphaFoldDB; D2S2V0; -.
DR KEGG; htu:Htur_4961; -.
DR HOGENOM; CLU_002865_7_2_2; -.
DR OrthoDB; 212451at2157; -.
DR Proteomes; UP000001903; Plasmid pHTUR03.
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};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Plasmid {ECO:0000313|EMBL:ADB63697.1}.
FT DOMAIN 83..106
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 255..269
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 529 AA; 58224 MW; E754EA6B1495AF35 CRC64;
MSAEATYDYI VVGAGSAGCV LANRLSEDED TSVLLLEAGE PNEKPEIDIP AAFPDLLKSS
VDWEYHTEPQ TELNGRELYW PRGRTLGGSS AINAMIYIRG HQVDYDHWAS LGNDEWSYDD
VLPYFKRSEN FEPGDSAYHD QNGPLNVCSP RTPRSLSQTF IEAAVEAGHI RNNDFNSERQ
EGVGFYHINQ KDGQRHSAAD AFLKPVLDRT NLIARTNAQV TRIVFDGSRT TGVEYEVDGD
HVRANVDCEV VLSAGAINSP QLLMLSGIGE AEHLREHDIE VQQDLPGVGH NLQDHLVTHV
VCEATGVDTL DDANSPQYFD TYSQHQRGPL TSNIAESGGF VRTESDLPAP DLQYHFGPSY
FMRHGFDNPA EGQGFSIGVT QLRPESRGRI SLASGDPSAT PTIDPQYLAE STDLEILAKG
LRTAREIARA DALDKYRERE IWPGEDVQTD EELKAHVRKT AETIYHPVGT CKMGNDSQSV
VDDRLRVHGV EGLRVVDASI MPTIVGGNTN APTIMIAEQA ADFMTEGSQ
//
