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Database: UniProt
Entry: Q89E56_BRADU
LinkDB: Q89E56_BRADU
Original site: Q89E56_BRADU 
ID   Q89E56_BRADU            Unreviewed;       536 AA.
AC   Q89E56;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   SubName: Full=Bll7231 protein {ECO:0000313|EMBL:BAC52496.1};
GN   OrderedLocusNames=bll7231 {ECO:0000313|EMBL:BAC52496.1};
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:BAC52496.1, 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   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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DR   EMBL; BA000040; BAC52496.1; -; Genomic_DNA.
DR   RefSeq; NP_773871.1; NC_004463.1.
DR   AlphaFoldDB; Q89E56; -.
DR   STRING; 224911.AAV28_33815; -.
DR   EnsemblBacteria; BAC52496; BAC52496; BAC52496.
DR   KEGG; bja:bll7231; -.
DR   PATRIC; fig|224911.5.peg.7423; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_8_0_5; -.
DR   InParanoid; Q89E56; -.
DR   OMA; QHATYHI; -.
DR   OrthoDB; 9773408at2; -.
DR   PhylomeDB; Q89E56; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   CDD; cd02002; TPP_BFDC; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF86; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVX-RELATED; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002526}.
FT   DOMAIN          22..127
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          397..534
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   536 AA;  56560 MW;  7F482C79E682F48A CRC64;
     MPRTMIGQMD HSKSPVVGAK RMNGAESLVR TMVKGGVDVC FTNPGTSEMH FVAALDRVPG
     MRCVLGLFEG VVTGAADGYF RMKGTPASTL LHLGPGLANG LANLHNAKKA NSGIVNIVGQ
     HAVYHIGYNA PLTSDIEGLA RPMSSWVRTS PDSKSVAADG AAAIAAAKSA PPQIATLILP
     ADTAWNEADG IAEVPAEQQR ASYSPQAVEQ AAKILHGDGE GTLLLMTGSA LSEQGLALAE
     RIAAKTGCTV MGPTFRPKMA RGRGRFSIDR IHYVIENALP MLAKFRHIVL VESDDPVAFF
     AYPNKPSVLR PEGCDVHRMT SWGENSVAAL EALAGAVKAS AKDVKPQAVQ ELVKPTGALT
     HASIAQSIAY AIPENAILVD ESLTTGRAFF PPTAAAAPHD WLQNMGGSIG FSTPLSIGAA
     IACPDRKVIT MVGDGSAMYT IQSLWTQARE NLNIVTIVFA NRIYQILRGE FDNVGAGEPG
     QRANDMLRLD RPTLDFVALA KGMGVPGRAV TNADEFNKAL AEAVAEPGPR LIEVQM
//
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