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Database: UniProt
Entry: A0A176Y7Y9_9BRAD
LinkDB: A0A176Y7Y9_9BRAD
Original site: A0A176Y7Y9_9BRAD 
ID   A0A176Y7Y9_9BRAD        Unreviewed;       623 AA.
AC   A0A176Y7Y9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:OAE99699.1};
GN   ORFNames=AYJ54_33005 {ECO:0000313|EMBL:OAE99699.1};
OS   Bradyrhizobium centrolobii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1505087 {ECO:0000313|EMBL:OAE99699.1, ECO:0000313|Proteomes:UP000076959};
RN   [1] {ECO:0000313|EMBL:OAE99699.1, ECO:0000313|Proteomes:UP000076959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR 10245 {ECO:0000313|EMBL:OAE99699.1,
RC   ECO:0000313|Proteomes:UP000076959};
RA   Simoes-Araujo J.L.Sr., Barauna A.C., Silva K., Zilli J.E.;
RT   "Draft Genome Sequence of the Strain BR 10245 (Bradyrhizobium sp.) isolated
RT   from nodules of Centrolobium paraense.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
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:OAE99699.1}.
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DR   EMBL; LUUB01000118; OAE99699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176Y7Y9; -.
DR   STRING; 1505087.AYJ54_33005; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000076959; 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:SF213; DEHYDROGENASE, PUTATIVE-RELATED; 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|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   DOMAIN          336..350
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         285
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   623 AA;  70666 MW;  F44C9D35FE630F34 CRC64;
     MTEVESYDYV VVGAGAGGGV LAARLAEAGR RVLVLDAGDD PVRSADAVSP ESRPVGPDYQ
     VPAFHPFASE NPGLRWNFWV RHYADTAQQQ KDWRYRANWE GEAVDGVVYP RASGLGGCTS
     HNAMIIVRPN NADWNHIWEI TGDASWRASN MQRYFLRLER CRYRWLRWLD RLFGWNPTGH
     GWRGWLTTQR ALPLRAVLDW RLRRTMRRAL LTTASLLPDA AEGWGWLMRS LGDPNDERLL
     DVEASTICLT PMSSARHTRT GPREFLLDVQ RRFPNNLTIR LNALVTRIKI DPVSRTASGV
     IYREGRRIYR AAAQPRGEAG RERFVGASRE VILAGGAFNT PQLLMLSGIG DREHLAGCRI
     VAVKDLPGVG RNLQDRYEIG VVNRVRQPWD ALRGATYTTK DRLYRQWRRW GTGAYTSNGL
     LFSAKFRSRT DQERPDLFCF CLLADFRGYY PGYSERINKL DYLTWAVLKA YTHNTAGTVR
     LRSNDPLDRP LINFRHFAEG NFAPDADLDA MITGIRFGRK VADALGKLIV EEEVPGRHLY
     TDDQLRRHVE DNAWGHHACG TCAMKPEDQG GVVDSEFRVY GMRNLRIVDA SIFPRIPGYF
     IVTAVYMIAE KAADVLLGDR EPV
//
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