ID A5EBE9_BRASB Unreviewed; 595 AA.
AC A5EBE9;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Putative acetolactate synthase large subunit {ECO:0000313|EMBL:ABQ33493.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:ABQ33493.1};
GN OrderedLocusNames=BBta_1253 {ECO:0000313|EMBL:ABQ33493.1};
OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=288000 {ECO:0000313|EMBL:ABQ33493.1, ECO:0000313|Proteomes:UP000000246};
RN [1] {ECO:0000313|EMBL:ABQ33493.1, ECO:0000313|Proteomes:UP000000246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTAi1 / ATCC BAA-1182 {ECO:0000313|Proteomes:UP000000246};
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP000494; ABQ33493.1; -; Genomic_DNA.
DR AlphaFoldDB; A5EBE9; -.
DR STRING; 288000.BBta_1253; -.
DR KEGG; bbt:BBta_1253; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_5; -.
DR Proteomes; UP000000246; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd00568; TPP_enzymes; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
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:SF166; 2-HYDROXYACYL-COA LYASE 2; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:ABQ33493.1}.
FT DOMAIN 3..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..336
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..563
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 595 AA; 63822 MW; 11C6B5693AF94D6E CRC64;
MKMNGATALV SMLSGYGVDV IFGVPGDTNV ALYEALRMTK GAPRHILCRD ERSAVFMADC
YARLSGKPGV AEVPSGAGAL YGLPGVAEAN KSSVPLILLV NDIPQPGVGR GTLTELPVQD
LFKPISKRAE TLAHVRKLPE VVRRAFREAT GGRPGAVVLA LPEDILYQDL PSEGVSLHVE
PQCRQAPSYR SRPADADLDS ALNAILAAER PLIVAGGGAN RSAAAEAITA FAERLGIPVV
TTITGQGVIR DDHKLGIGII GDNGFHPHAV WALGRADLVI YVGCRMGSVA TMNWQWPVPN
GETRIVQVDL EPEVIGNTYA IDFPLVGDAR AVVEALIAKA PADHASVTAA WVDEINSRRA
DFWDVMAPHL QSDEVPLRPE RVIETLNRCL PMPCNVVSDA GTPTPYATRF LRLRDPQSKL
VIPRFYGGLG YAIPAVIGAY FAAPHLRPVG LFGDGSLGMS AGELETLSRL QVPAVLIHFN
NACFGWIKAL QRVVDRDRAR KASEHSPAVP VNDPTFSVDF GKYDMSRLAS VYGIRSFRVE
TPAQLEAALR EAFELNEPVF IDVAVESIAD RLPPVFSWLK KVGADPAAVG VQAAL
//