ID L0IZJ3_9MYCO Unreviewed; 643 AA.
AC L0IZJ3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN ORFNames=Mycsm_04243 {ECO:0000313|EMBL:AGB24494.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB24494.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000673};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003078; AGB24494.1; -; Genomic_DNA.
DR RefSeq; WP_015308070.1; NC_019966.1.
DR AlphaFoldDB; L0IZJ3; -.
DR STRING; 212767.Mycsm_04243; -.
DR KEGG; msa:Mycsm_04243; -.
DR PATRIC; fig|710686.3.peg.4279; -.
DR HOGENOM; CLU_013748_6_0_11; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000010844; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:RHEA.
DR GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; 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:0019310; P:inositol catabolic process; 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 CDD; cd02003; TPP_IolD; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR030817; Myo_inos_IolD.
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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR04377; myo_inos_iolD; 1.
DR PANTHER; PTHR18968:SF9; 3D-(3,5/4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Hydrolase {ECO:0000313|EMBL:AGB24494.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 20..150
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 237..371
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 435..593
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 643 AA; 69253 MW; CFA63A372D405272 CRC64;
MVSKASAFKA AHNEPTVRLT VAQATIRFLA NQYVERDGER RKFFAGCFGI FGHGNVAGIG
QALLQAELDE NGPSLRYVLG RNEQAMVHTA AAYARQKDRL QAWVVTASIG PGSTNMLTGA
ALATINRLPV LLLPSDTFAT RVSAPVLQDL EQPHDNELTV NDAFKPLSRF FDRVWRPEQL
PSALLAAMRV LTDPVETGAA TIALPQDVQA EAFDWPESLF AERTWHIGRP VPERSVIARA
AEVIRSAQRP LIVAGGGVIY SGASDALAAF VEKTGIPVSE TQAGKGSLPY DHRYEVGAIG
STGTTAANDL AAQADVVIGI GTRYSDFTSA SRTAFNDPDV RFVNINVASF DSVKQGGLSV
VADAREALEA LSSALGDYSV TDEYRVKTAE LAQEWDQTVS AAYRVEDDGS ALNQSQVIGL
ANTLSDPRDV VVCAAGSMPG DLHKLWRTRE RKGYHVEYGY SCMGYEIAGG IGIRMAAPDR
DVFIMVGDGS YLMMATELVT AAQEGVKVIV VLVQNHGFAS IGSLSESLGS QRFGTAYRYR
SSDGRLDGDK LPVDLAANAA SLGAEVIRVT TAAEFTDAVK VAKANEHTTV IHVETDPLLY
APDSQSWWDV PVSQVSALES TKTAYETYAE WKKVQRPLTR PSE
//