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Database: UniProt
Entry: Q5YPI0_NOCFA
LinkDB: Q5YPI0_NOCFA
Original site: Q5YPI0_NOCFA 
ID   Q5YPI0_NOCFA            Unreviewed;       558 AA.
AC   Q5YPI0;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 96.
DE   RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE            EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN   Name=ilvB3 {ECO:0000313|EMBL:BAD59911.1};
GN   OrderedLocusNames=NFA_50590 {ECO:0000313|EMBL:BAD59911.1};
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=247156 {ECO:0000313|EMBL:BAD59911.1, ECO:0000313|Proteomes:UP000006820};
RN   [1] {ECO:0000313|EMBL:BAD59911.1, ECO:0000313|Proteomes:UP000006820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152 {ECO:0000313|EMBL:BAD59911.1,
RC   ECO:0000313|Proteomes:UP000006820};
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC         Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000673};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004974}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; AP006618; BAD59911.1; -; Genomic_DNA.
DR   RefSeq; WP_011211593.1; NC_006361.1.
DR   AlphaFoldDB; Q5YPI0; -.
DR   STRING; 247156.NFA_50590; -.
DR   GeneID; 61135635; -.
DR   KEGG; nfa:NFA_50590; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_1_11; -.
DR   OMA; MATCGEV; -.
DR   OrthoDB; 4494979at2; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000006820; 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   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF167; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVB2-RELATED; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006820};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          17..134
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          206..331
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          394..533
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   558 AA;  58481 MW;  67F21A2013618CEC CRC64;
     MTETITVTEV SGVETATAGA ALVDGLLDHG VDTVFGIPGV QTYELFEALG RAGDRIELIS
     ARHEQACAYM AMGYAQSTGR LGVCSVVPGP GILNAAAGLL TARGTNSPVL CLTGEIPTDF
     MGKGFGHLHE MPDQLTTLRS FVKSADNVLH PSEAKQVLAR AIRAAREGRP GPAVVATPWN
     VLTQSAPVAP AVPLDIVQPA VDPSAVAAAA ELIATARHPM ILVGGGARGA VAEINALATL
     LQAPVVAHRS GKGIVDEAAP LGFTCAEGFA RWLDCDLVLT IGTRAELLWF RWPKKPAAVP
     SINIDIDPTG HTRLQPTVAI TAGAAAATAA LLDALVAAGV HRPDRTAEFT ELKAAIRVEI
     DAYLQPHRDY LAAIRRALPA DGFFVEEVSQ IGFASYFSFP VSAPRQFVTC GYQGNLGYGF
     PTALGVKAAH RDRAVVAVSG DGGFQFGIQE LATAVQHRLG VAVVVFDNAA FGNVKADQER
     IYGRAVGSEL RNPDFVAVAR AYGAHGCRVD APEDLERAVA AAVDRDLPSV IVVPMPLEPG
     VAPWRYLMPD LPPGSYAP
//
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