(data stored in ACNUC7421 zone)

HOGENOM: PENCW_10_PE1012

ID   PENCW_10_PE1012                      STANDARD;      PRT;   694 AA.
AC   PENCW_10_PE1012; B6H4R2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Acetolactate synthase; EC=2.2.1 6;Flags: Precursor;
DE   (PENCW_10.PE1012).
GN   ORFNames=Pc13g10120;
OS   PENICILLIUM CHRYSOGENUM WISCONSIN 54-1255.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; mitosporic Trichocomaceae;
OC   Penicillium; Penicillium chrysogenum complex.
OX   NCBI_TaxID=500485;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PENCW_10.PE1012.
CC       Penicillium chrysogenum (strain ATCC 28089 / DSM 1075 / Wisconsin 54-
CC       1255) contig Pc00c13, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:B6H4R2_PENCW
CC   -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2).
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC       similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 1/4.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC   -!- GENE_FAMILY: HOG000258448 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B6H4R2; -.
DR   EMBL; AM920428; CAP92081.1; -; Genomic_DNA.
DR   RefSeq; XP_002559434.1; XM_002559388.1.
DR   ProteinModelPortal; B6H4R2; -.
DR   STRING; B6H4R2; -.
DR   GeneID; 8303943; -.
DR   KEGG; pcs:Pc13g10120; -.
DR   OrthoDB; EOG44TSH5; -.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; 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:0009082; P:branched chain family amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
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   TIGRFAMs; TIGR00118; Acolac_lg; 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
DR   HOGENOMDNA; PENCW_10.PE1012; -.
KW   CAP92081.100028832-2caffold_90100000011;
KW   Pc13g10120 protein;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Magnesium; Metal-binding; Signal;
KW   Thiamine pyrophosphate; Transferase.
SQ   SEQUENCE   694 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MMPLRPSKSA LRAFHLQKQL AGRRPFSTSF VASAASPHRS SVQKRTQSTA TASNPESRPV
     PSPAFNQEPH RNEISPLQHR QLPELDDSMV GMSGGEIFHE MMLRQGVKHV FGYPGGAILP
     VFDAIYNSKH FEFILPKHEQ GAGHMAEGYA RASGKPGVVL VTSGPGATNV ITPMQDAMSD
     GTPMVVFCGQ VPTSAIGTDS FQEADVIGIS RACTKWNVMV KSVGELPRRI QEAFEIATSG
     RPGPVLVDLP KDVTAGILRN PIPMHSTIPS LPSAATVAAR EMSRKQLEGT INRVANLVNV
     AKKPILYVGQ GLLARPDGPE ILKEFADKAC IPVTTTLQGL GGFDELDPKA LHMLGMHGSA
     YANMAMQEAD LIIAVGARFD DRVTLSIPKF APQAKLAATE GRGGIVHFEI MPKNINKVVQ
     ANEAVEGDCA DNLRLLLPHV KAVSERPEWF EQINDWKQRF PLSLYDRQTE DGPIKPQAVI
     EKLSELTADR KEKTIITTGV GQHQMWTAQH FRWRHPRTMI TSGGLGTMGY GLPAALGAKV
     ARPDCLVIDI DGDASFNMTL TELSTAAQFN IGVKVLLINN EEQGMVTQWQ NLFYEDRYSH
     THQQNPDFVP LAKAMRIGAD TCFKPSELEE KLKWLIEHDG PALLEVITDR KVPVLPMVPS
     GRGLHEFLVY DEAKDLERKE LMRERNVDFS VRKE
//

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