Reviewed, UniProtKB/Swiss-Prot P40811 (ILVI_SALTY)

Names and origin

Protein names

Recommended name:
    Acetolactate synthase isozyme 3 large subunit
    EC=2.2.1.6
Alternative name(s):
    AHAS-III
    Acetohydroxy-acid synthase III large subunit
    ALS-III

Gene names

Name:	ilvI
Ordered Locus Names:	STM0116

Organism

Salmonella typhimurium [Complete proteome] [HAMAP]

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	574 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.
Enzyme regulation	Sensitive to valine inhibition.
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.
Subunit structure	Dimer of chain H and chain I.
Miscellaneous	S.typhimurium contains genes for 3 AHAS isozymes: ilvBN, ilvGM and ilvIH. Contains 1 molecule of FAD per monomer. The role of this cofactor is not clear considering that the reaction does not involve redox chemistry By similarity.
Sequence similarities	Belongs to the TPP enzyme family.
Sequence caution	The sequence AAL19080.1 differs from that shown. Reason: Erroneous termination at position 12. Translated as Arg.

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	FAD binding Inferred from electronic annotation. Source: InterPro 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 – 574	574	Acetolactate synthase isozyme 3 large subunit		PRO_0000090790
Regions
	Nucleotide binding	261 – 282	22	FAD By similarity
	Nucleotide binding	304 – 323	20	FAD By similarity
	Region	397 – 477	81	Thiamine pyrophosphate binding
Sites
	Metal binding	448	1	Magnesium By similarity
	Metal binding	475	1	Magnesium By similarity
	Binding site	51	1	Thiamine pyrophosphate By similarity
	Binding site	153	1	FAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	P40811-1 [UniParc]. Last modified December 19, 2001. Version 3. Checksum: 72EB67FA2667B398	FASTA	574	62,896
	10 20 30 40 50 60 MEMLSGAEMV VRSLIDQGVK QVFGYPGGAV LDIYDALHTV GGIDHVLVRH EQAAVHMADG 70 80 90 100 110 120 LARATGDVGV VLVTSGPGAT NAITGIATAY MDSIPLVILS GQVATSLIGY DAFQECDMVG 130 140 150 160 170 180 ISRPVVKHSF LVKQTEDIPL VLKKAFWLAA SGRPGPVVVD LPKDILNPAK KMPYAWPETV 190 200 210 220 230 240 SMRSYNPTTS GHKGQIKRAL QTLASAKKPV VYVGGGAISA ACYAPLRHII ETFNLPVVSS 250 260 270 280 290 300 LMGLGAFPAT HRQSLGMLGM HGTYEANMTM HNADVIFAVG VRFDDRTTNN LAKYCPNATV 310 320 330 340 350 360 LHIDIDPTSI SKTVNADIPV VGDARLVLEQ MLELLAQDAP SQPQDDIRDW WQQIESWRAR 370 380 390 400 410 420 QCLKYDAESE SIKPQAVIET LWRLTKGDAY VTSDVGQHQM FAALYYPFDK PRRWINSGGL 430 440 450 460 470 480 GTMGFGLPAA LGVKMALPKE MVVCVTGDGS IQMNIQELST ALQYELPVLV LNLNNRYLGM 490 500 510 520 530 540 VKQWQDMIYS GRHSQSYMQS LPDFVRLAEA YGHVGLQINR PDELESKLSE ALEHVRNNRL 550 560 570 VFVDVTVDGS EHVYPMQIRG GGMDEMWLSK TERT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[2]	"Nucleotide sequence of the ilvH-fruR gene region of Escherichia coli K12 and Salmonella typhimurium LT2." Jahreis K., Postma P.W., Lengeler J.W. Mol. Gen. Genet. 226:332-336(1991) [PubMed: 1851954] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 516-574. Strain: LT2.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE008699 Genomic DNA. Translation: AAL19080.1. Sequence problems. X55456 Genomic DNA. Translation: CAA39101.1.
PIR	S15939.
RefSeq	NP_459121.1.
3D structure databases
HSSP	HSSP built from PDB template 1N0H based on UniProtKB P07342.
ModBase	Search...
Genome annotation databases
GeneID	1251634.
GenomeReviews	Gene locus STM0116 in contig AE006468_GR.
KEGG	stm:STM0116.
NMPDR	fig|99287.1.peg.114.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P40811.
Enzyme and pathway databases
BioCyc	STYP99287:STM0116-MON.
BRENDA	2.2.1.6. 2.
Family and domain databases
InterPro	IPR012846. Acetolactate_synth_lsu. 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]
TIGRFAMs	TIGR00118. acolac_lg. 1 hit.
PROSITE	PS00187. TPP_ENZYMES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ILVI_SALTY

Accession

Primary (citable) accession number: P40811

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	December 19, 2001
Last modified:	June 16, 2009
This is version 74 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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