(data stored in SCRATCH zone)

HOGENOM: CITK8_1_PE101

ID   CITK8_1_PE101                        STANDARD;      PRT;   548 AA.
AC   CITK8_1_PE101; A8ACR8;
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; (CITK8_1.PE101).
GN   OrderedLocusNames=CKO_00107;
OS   CITROBACTER KOSERI ATCC BAA-895.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CITK8_1.PE101.
CC       Citrobacter koseri ATCC BAA-895, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:A8ACR8_CITK8
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; A8ACR8; -.
DR   EMBL; CP000822; ABV11281.1; -; Genomic_DNA.
DR   RefSeq; YP_001451717.1; NC_009792.1.
DR   ProteinModelPortal; A8ACR8; -.
DR   STRING; A8ACR8; -.
DR   GeneID; 5583049; -.
DR   GenomeReviews; CP000822_GR; CKO_00107.
DR   KEGG; cko:CKO_00107; -.
DR   eggNOG; COG0028; -.
DR   OMA; HSWRYDH; -.
DR   ProtClustDB; PRK08978; -.
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; CITK8_1.PE101; -.
KW   acetolactate synthase 2 catalytic subunit;
KW   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW   Complete proteome; Magnesium; Metal-binding; Thiamine pyrophosphate;
KW   Transferase.
SQ   SEQUENCE   548 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNGAQWVVHA LRAQGVETVF GYPGGAIMPV YDALYDGGVE HLLCRHEQGA AMAAIGYARS
     TGKTGVCIAT SGPGATNLIT GLADALLDSV PVVAITGQVS APFIGTDAFQ EVDVLGLSLA
     CTKHSFLVQS LEELPRIMAE AFRVANSGRP GPVLVDIPKD IQLANGSLEP YFTTVENETA
     FPHADVEQAR RMMAQAQKPM LYVGGGVGMA QAVPALREFI AATQMPVTCT LKGLGAVDAD
     YPYYLGMLGM HGTKAANFAV QECDLLIAVG ARFDDRVTGK LNTFAPSASV IHMDIDPAEM
     NKLRQAHVAL QGDLNALLPA LQQPLNIDAW RQHNAELRTE HAWRYDHPGE AIYAPLLLKQ
     LSERKPADSV VTTDVGQHQM WSAQHMTYTR PENFITSSGL GTMGFGLPAA VGAQVARPND
     TVICISGDGS FMMNVQELGT VKRKQLPLKI VLLDNQRLGM VRQWQQLFFQ ERYSETTLTD
     NPDFLMLASA FGIPGQHITR KDQVEAALDT MLNSDGPYLL HVSIDELENV WPLVPPGASN
     SEMLEKLS
//

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