ILVH_MYCTU
ID ILVH_MYCTU Reviewed; 168 AA.
AC P9WKJ3; L0TE14; O53249; P65161;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Putative acetolactate synthase small subunit;
DE EC=2.2.1.6;
DE AltName: Full=Acetohydroxy-acid synthase small subunit;
DE Short=AHAS;
DE Short=ALS;
GN Name=ilvH; Synonyms=ilvN; OrderedLocusNames=Rv3002c; ORFNames=MTV012.16c;
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 PUPYLATION AT LYS-44, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [3]
RP INDUCTION.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [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:0000250}.
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 -!- 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: Dimer of large and small chains. {ECO:0000250}.
CC -!- INDUCTION: The expression gradually decreases as growth progresses.
CC {ECO:0000269|PubMed:20884690}.
CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45808.1; -; Genomic_DNA.
DR PIR; E70855; E70855.
DR RefSeq; NP_217518.1; NC_000962.3.
DR RefSeq; WP_003415167.1; NZ_NVQJ01000041.1.
DR AlphaFoldDB; P9WKJ3; -.
DR SMR; P9WKJ3; -.
DR STRING; 83332.Rv3002c; -.
DR PaxDb; P9WKJ3; -.
DR DNASU; 887226; -.
DR GeneID; 45426992; -.
DR GeneID; 887226; -.
DR KEGG; mtu:Rv3002c; -.
DR TubercuList; Rv3002c; -.
DR eggNOG; COG0440; Bacteria.
DR OMA; EPYGIKE; -.
DR PhylomeDB; P9WKJ3; -.
DR BRENDA; 2.2.1.6; 3445.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003984; F:acetolactate synthase activity; IBA:GO_Central.
DR GO; GO:1990610; F:acetolactate synthase regulator activity; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR CDD; cd04878; ACT_AHAS; 1.
DR Gene3D; 3.30.70.1150; -; 1.
DR InterPro; IPR004789; Acetalactate_synth_ssu.
DR InterPro; IPR027271; Acetolactate_synth/TF_NikR_C.
DR InterPro; IPR019455; Acetolactate_synth_ssu_C.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR039557; AHAS_ACT.
DR PANTHER; PTHR30239; PTHR30239; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF10369; ALS_ss_C; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR TIGRFAMs; TIGR00119; acolac_sm; 1.
DR PROSITE; PS51671; ACT; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis;
KW Isopeptide bond; Reference proteome; Transferase; Ubl conjugation.
FT CHAIN 1..168
FT /note="Putative acetolactate synthase small subunit"
FT /id="PRO_0000151416"
FT DOMAIN 7..82
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT CROSSLNK 44
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
SQ SEQUENCE 168 AA; 18187 MW; 523488D6114AB354 CRC64;
MSPKTHTLSV LVEDKPGVLA RVAALFSRRG FNIESLAVGA TECKDRSRMT IVVSAEDTPL
EQITKQLNKL INVIKIVEQD DEHSVSRELA LIKVQADAGS RSQVIEAVNL FRANVIDVSP
ESLTVEATGN RGKLEALLRV LEPFGIREIA QSGMVSLSRG PRGIGTAK
