ILVG_MYCTU
ID ILVG_MYCTU Reviewed; 547 AA.
AC P9WG39; L0T9C7; P66946; Q50613;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Acetolactate synthase large subunit IlvG;
DE Short=ALS;
DE EC=2.2.1.6;
DE AltName: Full=Acetohydroxy-acid synthase large subunit;
DE Short=AHAS;
GN Name=ilvG; OrderedLocusNames=Rv1820; ORFNames=MTCY1A11.23c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20884690; DOI=10.1099/mic.0.041343-0;
RA Singh V., Chandra D., Srivastava B.S., Srivastava R.;
RT "Biochemical and transcription analysis of acetohydroxyacid synthase
RT isoforms in Mycobacterium tuberculosis identifies these enzymes as
RT potential targets for drug development.";
RL Microbiology 157:29-37(2011).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the conversion of 2 pyruvate molecules into
CC acetolactate in the first common step of the biosynthetic pathway of
CC the branched-amino acids such as leucine, isoleucine, and valine.
CC {ECO:0000269|PubMed:20884690}.
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:0000269|PubMed:20884690};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.89 mM for pyruvate {ECO:0000269|PubMed:20884690};
CC Vmax=1.39 umol/min/mg enzyme {ECO:0000269|PubMed:20884690};
CC pH dependence:
CC Optimum pH is between 6 and 7. {ECO:0000269|PubMed:20884690};
CC Temperature dependence:
CC Optimum temperature is between 35 and 40 degrees Celsius.
CC {ECO:0000269|PubMed:20884690};
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 from
CC pyruvate: step 1/4.
CC -!- SUBUNIT: Heterodimer of large catalytic subunit and small regulatory
CC subunit. {ECO:0000250}.
CC -!- INDUCTION: The expression is almost identical during the mid-
CC exponential and extended stationary phase.
CC {ECO:0000269|PubMed:20884690}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44586.1; -; Genomic_DNA.
DR PIR; E70720; E70720.
DR RefSeq; NP_216336.1; NC_000962.3.
DR RefSeq; WP_003409218.1; NZ_NVQJ01000013.1.
DR AlphaFoldDB; P9WG39; -.
DR SMR; P9WG39; -.
DR STRING; 83332.Rv1820; -.
DR iPTMnet; P9WG39; -.
DR PaxDb; P9WG39; -.
DR DNASU; 885738; -.
DR GeneID; 885738; -.
DR KEGG; mtu:Rv1820; -.
DR TubercuList; Rv1820; -.
DR eggNOG; COG0028; Bacteria.
DR OMA; PGPYGCL; -.
DR PhylomeDB; P9WG39; -.
DR BRENDA; 2.2.1.6; 3445.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; IBA:GO_Central.
DR GO; GO:0003984; F:acetolactate synthase activity; IDA:MTBBASE.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:MTBBASE.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0009097; P:isoleucine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009099; P:valine biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
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-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 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; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW Acetylation; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; FAD; Flavoprotein; Magnesium;
KW Metal-binding; Reference proteome; Thiamine pyrophosphate; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..547
FT /note="Acetolactate synthase large subunit IlvG"
FT /id="PRO_0000090805"
FT REGION 388..468
FT /note="Thiamine pyrophosphate binding"
FT BINDING 57
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 299..318
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:21969609"
SQ SEQUENCE 547 AA; 57521 MW; 2D5CC10B21406887 CRC64;
MSTDTAPAQT MHAGRLIARR LKASGIDTVF TLSGGHLFSI YDGCREEGIR LIDTRHEQTA
AFAAEGWSKV TRVPGVAALT AGPGITNGMS AMAAAQQNQS PLVVLGGRAP ALRWGMGSLQ
EIDHVPFVAP VARFAATAQS AENAGLLVDQ ALQAAVSAPS GVAFVDFPMD HAFSMSSDNG
RPGALTELPA GPTPAGDALD RAAGLLSTAQ RPVIMAGTNV WWGHAEAALL RLVEERHIPV
LMNGMARGVV PADHRLAFSR ARSKALGEAD VALIVGVPMD FRLGFGGVFG STTQLIVADR
VEPAREHPRP VAAGLYGDLT ATLSALAGSG GTDHQGWIEE LATAETMARD LEKAELVDDR
IPLHPMRVYA ELAALLERDA LVVIDAGDFG SYAGRMIDSY LPGCWLDSGP FGCLGSGPGY
ALAAKLARPQ RQVVLLQGDG AFGFSGMEWD TLVRHNVAVV SVIGNNGIWG LEKHPMEALY
GYSVVAELRP GTRYDEVVRA LGGHGELVSV PAELRPALER AFASGLPAVV NVLTDPSVAY
PRRSNLA
