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
//