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Database: UniProt
Entry: Q7VZU8_BORPE
LinkDB: Q7VZU8_BORPE
Original site: Q7VZU8_BORPE 
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
//
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