ID E8RAX4_DESPD Unreviewed; 560 AA.
AC E8RAX4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 03-APR-2013, entry version 19.
DE RecName: Full=Acetolactate synthase;
DE EC=2.2.1.6;
GN OrderedLocusNames=Despr_0441;
OS Desulfobulbus propionicus (strain ATCC 33891 / DSM 2032 / 1pr3).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobulbaceae; Desulfobulbus.
OX NCBI_TaxID=577650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33891 / DSM 2032 / 1pr3;
RX PubMed=21475592;
RA Pagani I., Lapidus A., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Chertkov O., Davenport K., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Mavromatis K., Ivanova N., Mikhailova N.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brambilla E., Kannan K.P., Djao O.D.,
RA Rohde M., Pukall R., Spring S., Goker M., Sikorski J., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of Desulfobulbus propionicus type strain
RT (1pr3).";
RL Stand. Genomic Sci. 4:100-110(2011).
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.
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DR EMBL; CP002364; ADW16622.1; -; Genomic_DNA.
DR RefSeq; YP_004193913.1; NC_014972.1.
DR EnsemblBacteria; ADW16622; ADW16622; Despr_0441.
DR GeneID; 10173145; -.
DR KEGG; dpr:Despr_0441; -.
DR PATRIC; 46934231; VBIDesPro114934_0461.
DR HOGENOM; HOG000258448; -.
DR KO; K01652; -.
DR OMA; DSAIITT; -.
DR BioCyc; DPRO577650:GH80-446-MONOMER; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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 PANTHER; PTHR18968:SF13; PTHR18968:SF13; 1.
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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Complete proteome; Magnesium; Metal-binding; Thiamine pyrophosphate;
KW Transferase.
SQ SEQUENCE 560 AA; 59644 MW; ABFDD7D1BBC9A8F6 CRC64;
MSRLNGAQLI IGFLERQGIR IVSGIPGGAN LPLYDALASS PTIRHVLARH EQGAGFIAQG
MARASGQIGV CFATSGPGAT NILTALADAF LDSVPLVCIT GQVARSLLGT DAFQEVDTYG
LSMPITKHNY LVRSAAELLT ILPKAFHLAG SGRPGPVLID VPKDVQTEVV EFGAWPELVS
TADHQPGCPE SIRTAATMIN EAERPILYLG GGVIHAGAAA EARRLAEQGA IPTVMTLMGL
GILPSDHPLS LGMLGMHACR ATNLAMEECD LLIAAGVRFD DRATGRISDF CPKAKVIHVD
IDASEINKLR PADAGITGDA RHAFAALLPQ VRERQRSAWN GRIRQLQQDY PRFQTEDFAP
GRPFSLIRKV AELAGPEAII STDVGKHQMW VAQAYPLTDQ RQLLTSGGLG TMGFGLPAAI
GASLAFPERP VVCFSGDGSL QMNIQELATA VEQRAPVKIV VLNNQSLGLV RQQQRLFYEQ
HYFASSYGIA VDFAAIARGF GMQAYDLGSA DNPDTLLCEA MRHPGPCLIN VPIDIEAEVT
PMVPPGAANT TMIGDSYACN
//
