(data stored in ACNUC7421 zone)

SWISSPROT: Q758Q8_ASHGO

ID   Q758Q8_ASHGO            Unreviewed;       668 AA.
AC   Q758Q8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 117.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   ORFNames=AGOS_AEL305C {ECO:0000313|EMBL:AAS52379.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52379.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52379.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 1/4. {ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU003591}.
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DR   EMBL; AE016818; AAS52379.1; -; Genomic_DNA.
DR   RefSeq; NP_984555.1; NM_209908.1.
DR   STRING; 33169.AAS52379; -.
DR   EnsemblFungi; AAS52379; AAS52379; AGOS_AEL305C.
DR   GeneID; 4620730; -.
DR   KEGG; ago:AGOS_AEL305C; -.
DR   HOGENOM; HOG000258448; -.
DR   InParanoid; Q758Q8; -.
DR   KO; K01652; -.
DR   OMA; MRSYNPV; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005948; C:acetolactate synthase complex; IEA:EnsemblFungi.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:EnsemblFungi.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02015; TPP_AHAS; 1.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
DR   InterPro; IPR039368; AHAS_TPP.
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; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00118; acolac_lg; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q758Q8.
DR   SWISS-2DPAGE; Q758Q8.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|RuleBase:RU003591};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN          75..237
FT                   /note="TPP_enzyme_N"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          271..415
FT                   /note="TPP_enzyme_M"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          477..624
FT                   /note="TPP_enzyme_C"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          36..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   668 AA;  72180 MW;  CC6D5459B05DE789 CRC64;
     MLRRVTVRQL ANVRALARAT RPLAVARAFS GAAGRLGAEA QEAPRRRAPG PRGETEPQGA
     AGAHEMDHSM IGFSGGEIFH EMMRRHNVDT VFGYPGGAIL PVYDAIYNSD AFNFVLPKHE
     QGAGHMAEGY ARASGKPGVV LVTSGPGATN VVTPMADALA DGVPMVVFTG QVPKAAIGTD
     AFQEADVVGI SRSCTKWNVM VNHVEELPRR INEAFEIATS GRPGPVLVDL PKDVTAAILR
     SPIPLASALP STTLAQLTRQ AADIDGVRSL ADASRLINMA QKPVLYVGAG ILNSTRGPEF
     LRELAEKAQI PVTTTLQALG AFDQEDSKSV DMLGMHGSAA ANLTVQNADL IIALGARFDD
     RVTGNIAKFA PEAQRAAREQ RGGIVHFEIS PKNINKVVDA QVAVEGDVTA NLEKLLPLIK
     PVAERKEWLG QIASWKSEYP YDYSRETPGS RIKPQTVITR LSEIANATGK EVIVTTGVGQ
     HQMWAAQHWT WKKPRTFITS GGLGTMGFGL PAAIGAQVAK PDAIVIDIDG DASLNMTLME
     MSSAVQAGAP VKILLLNNEE QGMVTQWQSL FYEHRYSHTH QLNPDFVKLA DAMGFKAMRL
     EAQSDMEPML QEFINCKEPV LLEVAVEKKV PVLPMVPAGK ALHEFIYFDP EVERQQAELR
     SRRTGGKH
//

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