ID   A0A1G9TRT0_9EURY        Unreviewed;       538 AA.
AC   A0A1G9TRT0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:SDM50427.1};
GN   ORFNames=SAMN05192554_10393 {ECO:0000313|EMBL:SDM50427.1};
OS   Haloarchaeobius iranensis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halorubellaceae; Haloarchaeobius.
OX   NCBI_TaxID=996166 {ECO:0000313|EMBL:SDM50427.1, ECO:0000313|Proteomes:UP000199370};
RN   [1] {ECO:0000313|EMBL:SDM50427.1, ECO:0000313|Proteomes:UP000199370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB21,IBRC-M 10013,KCTC 4048
RC   {ECO:0000313|Proteomes:UP000199370};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNIA01000003; SDM50427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9TRT0; -.
DR   STRING; 996166.SAMN05192554_10393; -.
DR   OrthoDB; 346033at2157; -.
DR   Proteomes; UP000199370; 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; 2.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199370}.
FT   DOMAIN          15..48
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          94..319
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          408..530
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   538 AA;  58237 MW;  CF997AC3315FF6B9 CRC64;
     MSRGDVDRTP SPRTDVCIVG AGPAGALVAH RLASEGYDVV VLEAGPRFDP ANRLERMERH
     IRPSHGPEDV WDMGGPRDAY TNAGEEHYPL NAARVKGVGG TTLHWQGMVF RLHESDFERR
     SRHGVERDWP IGYDDLQPYY AEAEAELGVA GADDNPFAPP RSEPFPMPAF RPSYSDSLFA
     DACEELGIAM HSAPNARNSE AHDGRSACQG YGTCKPVCPS GAKYDATVHV SKAEEEEGAR
     VIDRAPVQRI EHDRSGETVE AVVYATPDGA EHRQEARQFV LAAGGIEIPR LLLLSRSTQH
     PDGLANSSGA VGRYFMDHLF AGMGGELDAP TRQKHVGFIT SESHQFYDEV DGSVGPYKLE
     FLNYAGPSPV DVALSTESEA AWGDALAEEI RDTYGNRIAM GGLCGQPPRA ENRVTLNPDV
     TDDHGNPVPD IHWSLGERER RTIEAANETQ AAIMDELGVD VDWTTGPEAT GPAFHHMGTT
     RMGTDPDESV VNPRLRTHDL DNCWIASSST FVTGGALNPT LTIAALALRA ADAVSEAL
//