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Database: UniProt
Entry: A0A067NNJ7_PLEOS
LinkDB: A0A067NNJ7_PLEOS
Original site: A0A067NNJ7_PLEOS 
ID   A0A067NNJ7_PLEOS        Unreviewed;       625 AA.
AC   A0A067NNJ7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   31-JAN-2018, entry version 24.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   ORFNames=PLEOSDRAFT_1078141 {ECO:0000313|EMBL:KDQ25682.1};
OS   Pleurotus ostreatus PC15.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Pleurotaceae; Pleurotus.
OX   NCBI_TaxID=1137138 {ECO:0000313|EMBL:KDQ25682.1, ECO:0000313|Proteomes:UP000027073};
RN   [1] {ECO:0000313|Proteomes:UP000027073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC15 {ECO:0000313|Proteomes:UP000027073};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A.,
RA   Sun H., LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E.,
RA   Pisabarro A.G., Walton J.D., Blanchette R.A., Henrissat B., Martin F.,
RA   Cullen D., Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy
RT   of the white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC   -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2).
CC       {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.
CC       {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
CC       from pyruvate: step 1/4. {ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; KL198010; KDQ25682.1; -; Genomic_DNA.
DR   EnsemblFungi; KDQ25682; KDQ25682; PLEOSDRAFT_1078141.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000027073; Unassembled WGS sequence.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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   Gene3D; 3.40.50.1220; -; 1.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
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;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU003591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000027073};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027073};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|RuleBase:RU003591}.
FT   DOMAIN       36    199       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      238    381       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      444    589       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   625 AA;  67781 MW;  8BA9269240344604 CRC64;
     MRRPTSSSSP SRSLQLGVAR YTFVPEDRLK FVGLCGAQIV RDVLIRNGVQ HAFAYSGGAN
     IHLTDSICTD GRIKVFLPRH EQGAGHMAEG YARVTGRPGV VSVTSGPGAT NVITPLQDAM
     SDGIPMIVIA GQVSAKDLGT GAFQDADIVG MTQPCTKWAT MVECVEDLPA YVDEAFRVAT
     SGRPGPVLLS IPRDVFEATW RDDHPIVRNI TLPSYPAQIR PPPPRASEPP APKIFGDISE
     AATRINNSER PLIIAGAGLL SSPDGPRILS ELAFRGNIPV ATTLHGLGAF DEDHSISLHM
     LGLHGSVYGN YAAQSADTII VLGARLDERV TANIDGFAVA ARAAGKDGRG GIIHFDIQPK
     KSNRIIDTHI SVVGDVTENL KILEPLIEPR ARAGWLDQIQ TWKTEFPFTY EPSAPGQRVK
     PQEVIEELDK QTNDIKDRVL ITTGVGHHQM WAAQFFTWKQ PRSLITSGAL ATMGFGLPAA
     IGAKVADPTK IVVDIDGDAS FLMSGLELAT AAEYGVGVKV LIFNNNVQGM VYRWQKIFYG
     SRHTLTRMAN PDFVMLAQSM GVHAIQCETA EQLPTKMKEF LEYDNSHPIV MVCQVDEEEE
     LYPIVKPGKA LHELTMHPSL PSVQA
//
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