ILVB2_MYCTU
ID ILVB2_MYCTU Reviewed; 552 AA.
AC O06335; L0TE78;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Putative acetolactate synthase large subunit IlvB2;
DE Short=ALS;
DE EC=2.2.1.6;
DE AltName: Full=Acetohydroxy-acid synthase large subunit;
DE Short=AHAS;
GN Name=ilvB2; OrderedLocusNames=Rv3470c;
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 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).
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 -!- 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 -!- 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 up-regulated in the mid-exponential and
CC extended stationary phase. {ECO:0000269|PubMed:20884690}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46292.1; -; Genomic_DNA.
DR PIR; C70567; C70567.
DR RefSeq; NP_217987.1; NC_000962.3.
DR RefSeq; WP_003900704.1; NZ_NVQJ01000087.1.
DR AlphaFoldDB; O06335; -.
DR SMR; O06335; -.
DR STRING; 83332.Rv3470c; -.
DR PaxDb; O06335; -.
DR DNASU; 888041; -.
DR GeneID; 888041; -.
DR KEGG; mtu:Rv3470c; -.
DR PATRIC; fig|83332.111.peg.3864; -.
DR TubercuList; Rv3470c; -.
DR eggNOG; COG0028; Bacteria.
DR InParanoid; O06335; -.
DR OMA; FNDFYPS; -.
DR PhylomeDB; O06335; -.
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; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
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; 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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; FAD;
KW Flavoprotein; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..552
FT /note="Putative acetolactate synthase large subunit IlvB2"
FT /id="PRO_0000396952"
FT REGION 394..474
FT /note="Thiamine pyrophosphate binding"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 262..285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 309..328
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 552 AA; 57257 MW; 5A6CE9C099652D9D CRC64;
MTVGDHLVAR MRAAGISVVC GLPTSRLDSL LVRLSRDAGF QIVLARHEGG AGYLADGFAR
ASGKSAAVFV AGPGATNVIS AVANASVNQV PMLILTGEVA VGEFGLHSQQ DTSDDGLGLG
ATFRRFCRCS VSIESIANAR SKIDSAFRAL ASIPRGPVHI ALPRDLVDER LPAHQLGTAA
AGLGGLRTLA PCGPDVADEV IGRLDRSRAP MLVLGNGCRL DGIGEQIVAF CEKAGLPFAT
TPNGRGIVAE THPLSLGVLG IFGDGRADEY LFDTPCDLLI AVGVSFGGLV TRSFSPRWRG
LKADVVHVDP DPSAVGRFVA TSLGITTSGR AFVNALNCGR PPRFCRRVGV RPPAPAALPG
TPQARGESIH PLELMHELDR ELAPNATICA DVGTCISWTF RGIPVRRPGR FFATVDFSPM
GCGIAGAIGV ALARPEEHVI CIAGDGAFLM HGTEISTAVA HGIRVTWAVL NDGQMSASAG
PVSGRMDPSP VARIGANDLA AMARALGAEG IRVDTRCELR AGVQKALAAT GPCVLDIAID
PEINKPDIGL GR
