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Database: UniProt
Entry: F7QRJ3_9BRAD
LinkDB: F7QRJ3_9BRAD
Original site: F7QRJ3_9BRAD 
ID   F7QRJ3_9BRAD            Unreviewed;       546 AA.
AC   F7QRJ3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:EGP06204.1};
DE            EC=1.1.99.1 {ECO:0000313|EMBL:EGP06204.1};
GN   ORFNames=CSIRO_4214 {ECO:0000313|EMBL:EGP06204.1};
OS   Bradyrhizobiaceae bacterium SG-6C.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae.
OX   NCBI_TaxID=709797 {ECO:0000313|EMBL:EGP06204.1, ECO:0000313|Proteomes:UP000003148};
RN   [1] {ECO:0000313|EMBL:EGP06204.1, ECO:0000313|Proteomes:UP000003148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG-6C {ECO:0000313|EMBL:EGP06204.1,
RC   ECO:0000313|Proteomes:UP000003148};
RX   PubMed=21742875; DOI=10.1128/JB.05647-11;
RA   Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G.,
RA   Pandey G.;
RT   "Genome Sequence of the Newly Isolated Chemolithoautotrophic
RT   Bradyrhizobiaceae Strain SG-6C.";
RL   J. Bacteriol. 193:5057-5057(2011).
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:EGP06204.1}.
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DR   EMBL; AFOF01000037; EGP06204.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7QRJ3; -.
DR   STRING; 709797.CSIRO_4214; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_5; -.
DR   Proteomes; UP000003148; Chromosome.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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};
KW   Oxidoreductase {ECO:0000313|EMBL:EGP06204.1}.
FT   DOMAIN          83..106
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          257..271
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         85
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"
FT   BINDING         501
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   546 AA;  59132 MW;  C70CE8E09B956602 CRC64;
     MKLSGYDYII VGAGSAGCVL ASRLSEDPNV NVLLIEAGAP SASIFVHMPA GIRVLYTSPK
     YNWQFWTEPQ ANLNNRKIYI PRGRVVGGSS SINSMIAIRG NAWDYDSWAA QGLPSWSYEN
     LRPYLRKIED ATLVTGERDQ DRGYSGPIRL SYGTLQHPIS KAFIESAVSA GLPENNGFNG
     PSQVGAGFYE LTIAEGKRSG AFKYLDRAKG RRNLTLMANC RVRRIAMEGT RARGVVIEKG
     GREVTIPAER EVLLTSGAIG SPQLLMLSGI GPADHLQSLG IKPVLDSAGV GDNLQDHLDC
     AIRMEASQPV TLTPYLGLIK GGLAGAQYIL RGTGPATSQG VEAGAFWGPD QGSSLPEWQA
     HLIVALRNPP PNERIAHGFA IRVCQLRPKS RGTLRLRSAN PSDTPAIDPR FLSDESDFVS
     MQEGVRQLCG IIDQPGLKKF VKRKIDIDAF TSVDSRKKWI RARAETIYHP VGTCRMGEDS
     NAVVDGQLRV RGIDNLRVID GSIMPTVISG NTNLPIMAMA EKAAELIAGN NKTSQFQAHN
     SKARSA
//
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