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Database: UniProt
Entry: A5EIZ7_BRASB
LinkDB: A5EIZ7_BRASB
Original site: A5EIZ7_BRASB 
ID   A5EIZ7_BRASB            Unreviewed;       611 AA.
AC   A5EIZ7;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Putative acetolactate synthase {ECO:0000313|EMBL:ABQ36141.1};
GN   OrderedLocusNames=BBta_4075 {ECO:0000313|EMBL:ABQ36141.1};
OS   Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=288000 {ECO:0000313|EMBL:ABQ36141.1, ECO:0000313|Proteomes:UP000000246};
RN   [1] {ECO:0000313|EMBL:ABQ36141.1, 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   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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DR   EMBL; CP000494; ABQ36141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5EIZ7; -.
DR   STRING; 288000.BBta_4075; -.
DR   KEGG; bbt:BBta_4075; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_4_0_5; -.
DR   Proteomes; UP000000246; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02002; TPP_BFDC; 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; 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:SF164; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 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;
FT   DOMAIN          40..168
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          451..606
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   611 AA;  66351 MW;  3F004D39317F1AD2 CRC64;
     MHPDACSIAC AAMPTNWGPR TVTKLPLPDP QSRATTHHRT AHYFLEALID LGVEYIFANL
     GTDHVSLIEE IARWDSEGRR HPEVILCPHE VVAVHMAMGY AMTTGRGQAV FVHVDAGTAN
     ACMAIQNAFR YRLPVLLIAG RAPFAIHGEL PGGRDTYVHF VQDSFDQGSI VRPYVKWEYT
     LPSGVVVKEA LTRAAAFMHS DPPGPVSMML PREVLAEAWD DDAMPAYPPA RYGSVRAGGV
     DPERAQAIAD ALMTAENPIA LTAYLGRSAE AVSVLDRLAL VCGIRVVEFN PITMNICQDS
     PCFAGSDPAA LVADADLGLL IDIDVPFIPQ LLKSADRLRW IQIDIDALKA DIPMWGFATD
     LRIQGDSAVI LRQVLEIVIA RGNDSYMRKV RDRIASWRPA REAAQAKRMA AAANKGSPGA
     INPAYLFARL QALLSEDDIV VNEAVRNAPV LQQQLRRTKP MTYVGLAGGG LGFSGGMALG
     LKLANPSHRV VQIVGDGAFH FAAPDSVYAV SQQYRLPIFS VILDNKGWQA VKASVQRVYP
     DGVAQQTDSF LSRLATGRQD EQRRLVDIAR AFGAHGERVD DPDELDAAIR SCLAALDDGR
     AAVLHVNITP L
//
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