ID Q7VZU8_BORPE Unreviewed; 564 AA.
AC Q7VZU8;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:CAE41090.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:CAE41090.1};
GN Name=ilvB {ECO:0000313|EMBL:CAE41090.1};
GN OrderedLocusNames=BP0784 {ECO:0000313|EMBL:CAE41090.1};
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE41090.1, ECO:0000313|Proteomes:UP000002676};
RN [1] {ECO:0000313|Proteomes:UP000002676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC {ECO:0000313|Proteomes:UP000002676};
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; BX640413; CAE41090.1; -; Genomic_DNA.
DR RefSeq; NP_879601.1; NC_002929.2.
DR RefSeq; WP_010930013.1; NZ_CP039022.1.
DR AlphaFoldDB; Q7VZU8; -.
DR STRING; 257313.BP0784; -.
DR PaxDb; 257313-BP0784; -.
DR GeneID; 69600736; -.
DR KEGG; bpe:BP0784; -.
DR PATRIC; fig|257313.5.peg.836; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_4; -.
DR OMA; MATCGEV; -.
DR Proteomes; UP000002676; 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 GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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 Reference proteome {ECO:0000313|Proteomes:UP000002676};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:CAE41090.1}.
FT DOMAIN 5..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 197..333
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 406..547
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 564 AA; 59573 MW; 17B51175A1E30C19 CRC64;
MTQLNGAEAM VRMLQLNGVK HIFGLCGDTS LPFCDALQRL DHGMEHILTR DERSAAYMAD
AYARVTGKVG VCEGPSGGGA TYLLPGLVEA NESSVAVLGI TSDVSVGSRG KYPLTELDQE
ALYRPLTKWN TTIDRADQIP GAVRAAFRAM TTGRPGTAHL CLPYDVQKHE VDPADVWAQP
GHDRFPAMRF APDPAAIEQA AARLVGARAP VILCGGGVVI SGACAALEEL AVTLNAPVCT
TVSGQGSLAD THPLNAGVVG SNGGILATRA VLADADVVLL IGCRAGSTST EHWRFPSREV
PILHIDSDPM VIAANYRTDV AMVGDALLAL QALNREVHAR IDARPTDAVD GKAVAAKAKG
AKLAALQPLA ASLDAPIRPE RVVDALNRLL PAESVVVADP GTPCPYFSAY FEASKPGRHF
ITNRAHGALG FSMAAGMGAA IGRPSAKVVS VMGDGSFGFT VGEMETIVRR KVPLLMIVLS
NSVYGWIKAS QKAGYQERYF SVDFNRTDHA RVAEAYGVKA WRVEDPRELD GVLKAAIEYG
GPALVDIIVQ PLQEAAAPVS QWMG
//