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Database: UniProt
Entry: A0A142M3K5_AMIAI
LinkDB: A0A142M3K5_AMIAI
Original site: A0A142M3K5_AMIAI 
ID   A0A142M3K5_AMIAI        Unreviewed;       551 AA.
AC   A0A142M3K5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Choline dehydrogenase-like flavoprotein {ECO:0000313|EMBL:MBB3709258.1};
GN   ORFNames=FHS67_005607 {ECO:0000313|EMBL:MBB3709258.1};
OS   Aminobacter aminovorans (Chelatobacter heintzii).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Aminobacter.
OX   NCBI_TaxID=83263 {ECO:0000313|EMBL:MBB3709258.1, ECO:0000313|Proteomes:UP000577697};
RN   [1] {ECO:0000313|EMBL:MBB3709258.1, ECO:0000313|Proteomes:UP000577697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10368 {ECO:0000313|EMBL:MBB3709258.1,
RC   ECO:0000313|Proteomes:UP000577697};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|RuleBase:RU003968}.
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:MBB3709258.1}.
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DR   EMBL; JACICB010000027; MBB3709258.1; -; Genomic_DNA.
DR   RefSeq; WP_067958286.1; NZ_JACICB010000027.1.
DR   AlphaFoldDB; A0A142M3K5; -.
DR   STRING; 83263.AA2016_1995; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000577697; 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; 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, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968}.
FT   DOMAIN          79..102
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          252..266
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         81
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         217
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   551 AA;  60013 MW;  B683626AA9ADDC40 CRC64;
     MTYDYIITGA GPAGCVLANR LSEDSDVRVL LLEAGGGDWN PLFHMPAGFA KMTKGVASWG
     WETVPQKHMK GRVLRYTQAK VIGGGSSINA QLYTRGNAAD YDLWASEDGC TGWDYRSVLP
     YFKRSEDNQR FADDYHGYGG PLGVSMPSAA LPICDAYIRA GQELGIPYNH DFNGKQQAGV
     GFYQLTQRNK RRSSASMAYL APIKDRRNLT VRLGARVTRI VVQKGRAVGV EVASGNGSEI
     IRAEREVLVS SGAIGSPKLL LQSGIGPADH LKSVGVPVVH DLKGVGENMQ DHLDLFVISE
     CTGDHTYDNV AKLHRTLWAG LQYVLFRTGP VTSSLFETGG FWYADPDARS PDIQFHLGLG
     SGIEAGVARL KNAGVTLNSA YLHPRSRGTV RLASSDPAAA PLIDPNYWAD PHDRKMSIEG
     LRVAREIMQQ AALKPFVLAE RLPGPDKVTE EQLFDYGCAN AKTDHHPVGT CKMGTDDMAV
     VDLELKVHGM EGLRVCDSSV MPRVPSCNTN GPTVMMGEKG ADIIRNRDPL PPAIFTYERN
     DTRPRARAEI S
//
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