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Database: UniProt
Entry: V5XCA9_MYCNE
LinkDB: V5XCA9_MYCNE
Original site: V5XCA9_MYCNE 
ID   V5XCA9_MYCNE            Unreviewed;       506 AA.
AC   V5XCA9;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:AHC26050.1};
GN   ORFNames=D174_16310 {ECO:0000313|EMBL:AHC26050.1};
OS   Mycolicibacterium neoaurum VKM Ac-1815D.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC26050.1, ECO:0000313|Proteomes:UP000018763};
RN   [1] {ECO:0000313|EMBL:AHC26050.1, ECO:0000313|Proteomes:UP000018763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC26050.1,
RC   ECO:0000313|Proteomes:UP000018763};
RX   PubMed=24435872;
RA   Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A., Schelkunov M.I.,
RA   Strizhov N., Ivashina T.V., Ashapkin V.V., Donova M.V.;
RT   "Complete Genome Sequence of Sterol-Transforming Mycobacterium neoaurum
RT   Strain VKM Ac-1815D.";
RL   Genome Announc. 2:e01177-13(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; CP006936; AHC26050.1; -; Genomic_DNA.
DR   RefSeq; WP_019509882.1; NC_023036.2.
DR   AlphaFoldDB; V5XCA9; -.
DR   SMR; V5XCA9; -.
DR   KEGG; mne:D174_16310; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_11; -.
DR   Proteomes; UP000018763; Chromosome.
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, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018763}.
FT   DOMAIN          253..267
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         95..98
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   506 AA;  53410 MW;  DE5E6D38DB459ADC CRC64;
     MNAGASDAEV FDHIVVGAGS AGCVIAARLA AAGARVGLLE AGGTDRRPDV RLPLGIASLF
     ATANWRYPML PDPSKHDQPG AFAAGRIIGG SGSINAMVYV RGRAADYRRW ALAGATGWDH
     EDVLPAFRAL ENWCDGADEF RGSGGPIDVS WCGHTHPLDA AFLDAAAESG FDRNPDHNGA
     SQLGAGPAQV NQRRGLRCSA ATGFLRALPA DRRPRVITRA PVDRVVLERG RAIGVMTRGR
     LLRAEHDVIL SAGAIGTPAV LLRSGIGPGG TAADLSGVGQ NLQDHLVVAQ HWSSHVPTIN
     SLTAPQAARA LGSLAARGSG PLTTTPFEAQ LFTDDFQIAI SPIHYQLDPL RGRARIGRAD
     AFTVYTVLLH PRSRGHVELR NGKPVVRHHR LADAQDRADL LSGAALAREL VESTSAMRPM
     AGRYLDDTGD FDADWLGDKE SSIYHAVGTC RMGTDDNAVV GPDLRVHAVD GLRVADASIM
     PNITSGNTNA PSMMIGYRAA DVILHG
//
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