ID Q89XE7_BRADU Unreviewed; 564 AA.
AC Q89XE7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Blr0367 protein {ECO:0000313|EMBL:BAC45632.1};
GN OrderedLocusNames=blr0367 {ECO:0000313|EMBL:BAC45632.1};
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:BAC45632.1, 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; BAC45632.1; -; Genomic_DNA.
DR RefSeq; NP_767007.1; NC_004463.1.
DR RefSeq; WP_011083199.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89XE7; -.
DR STRING; 224911.AAV28_41075; -.
DR EnsemblBacteria; BAC45632; BAC45632; BAC45632.
DR GeneID; 64020224; -.
DR KEGG; bja:blr0367; -.
DR PATRIC; fig|224911.44.peg.8890; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_5; -.
DR InParanoid; Q89XE7; -.
DR OrthoDB; 9785276at2; -.
DR PhylomeDB; Q89XE7; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.30.410.40; -; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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.
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 90..113
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT BINDING 92
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 230
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 502..503
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 564 AA; 62120 MW; 3CF7834F42274895 CRC64;
MYDYIIVGGG SAGSVLAHRL SAKSANKVLL CEAGQDTPPG NEPAEIRDSY PGTAYFDPRF
HWTELKVTTQ VVSHNNPTEA RPPLRKYEQA RVLGGGSSIN GQMANRGAPT DYDEWDARGA
EGWTWNDVLP FFKKVERDLD FDGPYHGKDG RIPVRRIPRE HWTRHSQAFA DAFQQAGHQF
VADQNGEFVD GYFAVTHSNQ AEQRVSAAMG YLDRDTRKRA NLTISTNTQV RELLFEGTQC
VGVKARVDGR EQEFRGREII LSSGAIHSPA HLLRAGIGPV GHLKDMGIPV LTGLPGVGQR
LMDHPSISLS SFVRRGARMN EHTRRHMQLG LRYSSGLSGV PKGDMFVVVL SKSAWHAVGA
QIGSLLTFVN KTYSETGQVK LASRDPSAEP IVEFNLLSDR RDLDRLMSGF RKMAAVQMSE
IVRKVTDKPF PAAYTDKVRK IGVVNTGNKI LTRVAAALMD GPAALRHYLI DNFVVEGFTF
DDVMNDDEAL EAFVRKATIG VWHASCSCRM GRADDPMAVV DNQGRVRGVQ GLRVVDASIF
PVVPCANTNF PVLMSAEKIA ATMQ
//
