ID Q89CB2_BRADU Unreviewed; 540 AA.
AC Q89CB2;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:BAC53150.1};
GN OrderedLocusNames=blr7885 {ECO:0000313|EMBL:BAC53150.1};
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC53150.1, ECO:0000313|Proteomes:UP000002526};
RN [1] {ECO:0000313|Proteomes:UP000002526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC {ECO:0000313|Proteomes:UP000002526};
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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}.
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DR EMBL; BA000040; BAC53150.1; -; Genomic_DNA.
DR RefSeq; NP_774525.1; NC_004463.1.
DR AlphaFoldDB; Q89CB2; -.
DR STRING; 224911.AAV28_37140; -.
DR EnsemblBacteria; BAC53150; BAC53150; BAC53150.
DR KEGG; bja:blr7885; -.
DR PATRIC; fig|224911.5.peg.8113; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_5; -.
DR InParanoid; Q89CB2; -.
DR OrthoDB; 9785276at2; -.
DR PhylomeDB; Q89CB2; -.
DR Proteomes; UP000002526; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002526}.
FT DOMAIN 88..111
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 261..275
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 98..101
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 540 AA; 59505 MW; 2443580EAE67E150 CRC64;
MTIRGETTLT DTFDFVVVGA GSGGCAVAGR LSEDAATSVA LLDAGGRNDS WRITTPFGLA
LPYRAANWAF DTVPQKGLNG RIGYQPRGKG LGGSSAINAM VYIRGNKWDY DHWAALGNAG
WSYADVLPYF KRSENNADFD GEYHGKGGPL HVNKLRSDNP IHDVFHQAAR EAQFRIREDF
NEEDHEGLGS YQVTQHGGER WSAARAYVDP HMGKRANLRV ETQAHATRIL FEGRRAVGVE
YRQGKELKQL RARREVILAS GAFQSPQLLM LSGVGDGDAL AAHGIGVVHH LPGVGRNLQD
HPDFVFVYAS DYPHFVHASL GRLPSLLRAI QRYRRERRGL MTTNFAECGG FLKTQAHLDV
PDIQLHFIIA MLDDHGRKKH KEAGFSCHVC LLRPKSRGSV WLKSADPLAA PMIDPNFLGE
AEDLETMVAG FKTTRRLMET PAMRALQKKD MFTSDVKTDD DIRAILRNRV DTVYHPVGTC
KMGTDAMAVV DPQLKVHGVE AMRVVDASIM PTLIGGNTNA PTIMIGEKAA DMIRAEVRAN
//
