ID   A0A2A9DT00_9MICO        Unreviewed;       509 AA.
AC   A0A2A9DT00;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Choline dehydrogenase-like flavoprotein {ECO:0000313|EMBL:PFG29917.1};
GN   ORFNames=ATJ78_0836 {ECO:0000313|EMBL:PFG29917.1};
OS   Microbacterium agarici.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=630514 {ECO:0000313|EMBL:PFG29917.1, ECO:0000313|Proteomes:UP000221369};
RN   [1] {ECO:0000313|EMBL:PFG29917.1, ECO:0000313|Proteomes:UP000221369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21798 {ECO:0000313|EMBL:PFG29917.1,
RC   ECO:0000313|Proteomes:UP000221369};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (OCT-2017) 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}.
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:PFG29917.1}.
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DR   EMBL; PDJE01000001; PFG29917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A9DT00; -.
DR   Proteomes; UP000221369; 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; 3.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000221369}.
FT   DOMAIN          234..298
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          391..502
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          44..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   509 AA;  53972 MW;  E5872A8EC984641E CRC64;
     MTRNTVDVVV VGSGPAGTAF ARTLAESAPE TSILMVECGP LVASPPGRHV RRTGDAADRE
     RAQVASQGPL GSRRGLPPPR AISPDAEGRL PIGVRPGTFL ISDGMVASDS KGFPAGAMSS
     NVGGMGAHWS CACPAPGEGE LIPFIPPDEF AHDFAAGYRL LSVTQRAFDD SELAMGVQTA
     IGAKFDSFVK RPVQAMPLAL TPDADGRLGF AGTEKLLERL LASPSERFEL RANTLATSLV
     REGDRVVGVQ LRNLVSGEEY RVSSGHVFVA ADAYRTPQLM YASGIRPQAL GRYVNDHLDA
     RSFVQLDDRF RELARGESEA SAGGLDRDAG VTWIPYDREN FPFSVQVMQL DASPIALDEH
     ASPWPGSYVG VVLFGCKDLD TRDRIGFSDR ETDAYGMPAL RIHYQLNDRD HATVHNMMGA
     HENIRDALGS FVGGGPALLQ DGASYHIMGS VRMGETDDGA SVCDSFGRVW GVDGLSVGGN
     GVIPTPTACN PTATSVALAV RAAAHIAQN
//