Reviewed, UniProtKB/Swiss-Prot P66946 (ILVG_MYCTU)

Names and origin

Protein names

Recommended name:
    Probable acetolactate synthase
    EC=2.2.1.6
Alternative name(s):
    Acetohydroxy-acid synthase
    ALS

Gene names

Name:	ilvG
Ordered Locus Names:	Rv1820, MT1868
ORF Names:	MTCY1A11.23c

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	547 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	2 pyruvate = 2-acetolactate + CO2.
Cofactor	Binds 1 magnesium ion per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4.
Sequence similarities	Belongs to the TPP enzyme family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Ligand	FAD Flavoprotein Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	branched chain family amino acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	acetolactate synthase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW thiamin pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 547	547	Probable acetolactate synthase		PRO_0000090805
Regions
	Nucleotide binding	299 – 318	20	FAD By similarity
	Region	388 – 468	81	Thiamine pyrophosphate binding
Sites
	Metal binding	439	1	Magnesium By similarity
	Metal binding	466	1	Magnesium By similarity
	Binding site	57	1	Thiamine pyrophosphate By similarity
	Binding site	159	1	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P66946-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 2D5CC10B21406887	FASTA	547	57,521
	10 20 30 40 50 60 MSTDTAPAQT MHAGRLIARR LKASGIDTVF TLSGGHLFSI YDGCREEGIR LIDTRHEQTA 70 80 90 100 110 120 AFAAEGWSKV TRVPGVAALT AGPGITNGMS AMAAAQQNQS PLVVLGGRAP ALRWGMGSLQ 130 140 150 160 170 180 EIDHVPFVAP VARFAATAQS AENAGLLVDQ ALQAAVSAPS GVAFVDFPMD HAFSMSSDNG 190 200 210 220 230 240 RPGALTELPA GPTPAGDALD RAAGLLSTAQ RPVIMAGTNV WWGHAEAALL RLVEERHIPV 250 260 270 280 290 300 LMNGMARGVV PADHRLAFSR ARSKALGEAD VALIVGVPMD FRLGFGGVFG STTQLIVADR 310 320 330 340 350 360 VEPAREHPRP VAAGLYGDLT ATLSALAGSG GTDHQGWIEE LATAETMARD LEKAELVDDR 370 380 390 400 410 420 IPLHPMRVYA ELAALLERDA LVVIDAGDFG SYAGRMIDSY LPGCWLDSGP FGCLGSGPGY 430 440 450 460 470 480 ALAAKLARPQ RQVVLLQGDG AFGFSGMEWD TLVRHNVAVV SVIGNNGIWG LEKHPMEALY 490 500 510 520 530 540 GYSVVAELRP GTRYDEVVRA LGGHGELVSV PAELRPALER AFASGLPAVV NVLTDPSVAY PRRSNLA

References

[1]

"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.

[2]

"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX842577 Genomic DNA. Translation: CAB01459.1. AE000516 Genomic DNA. Translation: AAK46141.1.
PIR	E70720.
RefSeq	NP_216336.1. NP_336327.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	885738. 923757.
GenomeReviews	Gene locus MT1868 in contig AE000516_GR. Gene locus Rv1820 in contig AL123456_GR.
KEGG	mtc:MT1868. mtu:Rv1820.
TIGR	MT1868.
Organism-specific databases
TubercuList	Rv1820.
Phylogenomic databases
HOGENOM	P66946.
OMA	P66946. VRHNVPV.
Enzyme and pathway databases
BRENDA	2.2.1.6. 809.
Family and domain databases
InterPro	IPR000399. TPP_bd_CS. IPR012001. TPP_bd_enzyme_N. IPR011766. TPP_enzyme_bd_C. IPR012000. TPP_enzyme_M. [Graphical view]
Pfam	PF02775. TPP_enzyme_C. 1 hit. PF00205. TPP_enzyme_M. 1 hit. PF02776. TPP_enzyme_N. 1 hit. [Graphical view]
PROSITE	PS00187. TPP_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ILVG_MYCTU

Accession

Primary (citable) accession number: P66946
Secondary accession number(s): Q50613

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	June 16, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)