ID E6SI00_THEM7 Unreviewed; 631 AA.
AC E6SI00;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 29-MAY-2013, entry version 21.
DE RecName: Full=Acetolactate synthase;
DE EC=2.2.1.6;
DE Flags: Precursor;
GN OrderedLocusNames=Tmar_1778;
OS Thermaerobacter marianensis (strain ATCC 700841 / DSM 12885 / JCM
OS 10246 / 7p75a).
OC Bacteria; Firmicutes; Clostridia; Clostridiales;
OC Clostridiales Family XVII. Incertae Sedis; Thermaerobacter.
OX NCBI_TaxID=644966;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700841 / DSM 12885 / JCM 10246 / 7p75a;
RX DOI=10.4056/sigs.1373474;
RA Han C., Gu W., Zhang X., Lapidus A., Nolan M., Copeland A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J., Tapia R., Goodwin L.,
RA Pitluck S., Pagani I., Ivanova N., Mavromatis K., Mikhailova N.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.,
RA Jeffries C., Schneider S., Rohde M., Goker M., Pukall R., Woyke T.,
RA Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA Klenk H., Detter J.;
RT "Complete genome sequence of Thermaerobacter marianensis type strain
RT (7p75aT).";
RL Stand. Genomic Sci. 3:337-345(2010).
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; CP002344; ADU51880.1; -; Genomic_DNA.
DR RefSeq; YP_004102607.1; NC_014831.1.
DR EnsemblBacteria; ADU51880; ADU51880; Tmar_1778.
DR GeneID; 10082161; -.
DR KEGG; tmr:Tmar_1778; -.
DR PATRIC; 45380838; VBITheMar50867_1825.
DR HOGENOM; HOG000258448; -.
DR KO; K01652; -.
DR OMA; MENIAYK; -.
DR BioCyc; TMAR644966:GHKT-1817-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; Signal;
KW Thiamine pyrophosphate; Transferase.
FT SIGNAL 1 33 Potential.
FT CHAIN 34 631 Potential.
FT /FTId=PRO_5000669299.
SQ SEQUENCE 631 AA; 66973 MW; 2C93F011D16303F3 CRC64;
MSQPAKQATA TATVTAAGGP PPAARPPSTP PHAMTGAGLR PGTETPPVNR RGPMSGADVV
VQVLLEQGVE WVFGIPGGAV LPLYDALYGA PIRHVLARHE QGAALAADGY ARASGRVGVC
IATSGPGATN LITGLATSYL DSVPVVAITG NVGRAFLGTD AFQEADTFGV SMPVTKHNYL
VLDPEELPAI LREAFAVAAS GRPGPVLVDI PKDIFTATIS TGAWDRPLRR SVSCFGRTAA
DSGTPHIPDL PGRSHLTGRL EEAARLIARA RQPVLYAGGG VIVAGAAEAL RRLAEQAVLP
TTTTLMALGA MPGDHPLFLG MPGMHGTYAA NMALTETDCL VAVGARFDDR VTGKVSAFAP
DAAIIHIDVD AAELGKVKAP RVAIPADARE GLEALREALG RVPPDEWADR SPWLERVNGW
KRDHPYRYDR ERARRELLPQ AVIEELERAT GGDALVVTGV GQHQMWAAMF YRYRRPRQFL
TSGGLGTMGY GLPAAIGAQL ARPDARVLCI DGDGSFQMNV QELSTLAELG LPVKVFIINN
RAHGMVRQWQ DLFYGQRLSA SVFEHQPDFV KLAEAYGIAA FRITHPDELA GTVREALARP
GPVVVDCVVR QEENVLPMVP PGAALREMIV G
//