ID   F7XHD8_SINMM            Unreviewed;       536 AA.
AC   F7XHD8;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:AEH83964.1};
GN   OrderedLocusNames=SM11_pD1132 {ECO:0000313|EMBL:AEH83964.1};
OS   Sinorhizobium meliloti (strain SM11).
OG   Plasmid pSmeSM11d {ECO:0000313|EMBL:AEH83964.1,
OG   ECO:0000313|Proteomes:UP000009045}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH83964.1, ECO:0000313|Proteomes:UP000009045};
RN   [1] {ECO:0000313|EMBL:AEH83964.1, ECO:0000313|Proteomes:UP000009045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM11 {ECO:0000313|EMBL:AEH83964.1,
RC   ECO:0000313|Proteomes:UP000009045};
RC   PLASMID=pSmeSM11d {ECO:0000313|Proteomes:UP000009045};
RX   PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA   Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA   Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT   "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT   isolate SM11 extends the S. meliloti pan-genome.";
RL   J. Biotechnol. 155:20-33(2011).
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; CP001832; AEH83964.1; -; Genomic_DNA.
DR   RefSeq; WP_014530690.1; NZ_JAJJBH010000002.1.
DR   AlphaFoldDB; F7XHD8; -.
DR   KEGG; smx:SM11_pD1132; -.
DR   PATRIC; fig|707241.3.peg.6819; -.
DR   HOGENOM; CLU_002865_7_1_5; -.
DR   Proteomes; UP000009045; Plasmid pSmeSM11d.
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; 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:AEH83964.1}.
FT   DOMAIN          260..274
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   536 AA;  58450 MW;  34B3688ACFE6A1F3 CRC64;
     MNETIADAGS YDFIVIGAGS AGCVLANRLS ADPKNRVLLL EAGGSDRYHW VHVPIGYLYC
     MGNPRTDWMM RTAAEPGLNG RSLPYPRGKL LGGCSSINGM IYMRGQAADY DGWRQAGNTG
     WGWDDVLPYF LKSEDNFRGK SPMHGAGGEW RVERQRLSWP ILDAFRDAAE ELGIPKAEDF
     NTGDNEGSGY FEVNQRGGVR WNTSKAFLRP AMKRPNLRVL TGAETERLIF DGRRTKGVRF
     RLNGRIQVAR ATREVILSAG AINSPKILEL SGVGRPDVVS AAGAEVVHDL PGVGENLQDH
     LQIRTVFRIE GAKTLNQLYH SIFSRIGMGA EYMLRRSGPL SMAPSQLGIF AKSSPSVATA
     DLEYHVQPLS TDRLGEPLHR YPAVTVSVCN LRPESRGSVH VTTAESSAAP DIRPNYLSTP
     GDRLLAAHAI RHARNLMATK AIARFRPAEM LPGSEFQSED ELIRRAGDIA TTIFHPVGTC
     KMGSDPMAVV DPSLKVHGLD GLRVVDASIM PSIVSGNTNS PVIMIAEKAA EAILHR
//