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Reviewed, UniProtKB/Swiss-Prot P40811 (ILVI_SALTY)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismSalmonella typhimurium [Complete proteome] [HAMAP]
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574Acetolactate synthase isozyme 3 large subunit
PRO_0000090790

Regions

Nucleotide binding261 – 28222FAD By similarity
Nucleotide binding304 – 32320FAD By similarity
Region397 – 47781Thiamine pyrophosphate binding

Sites

Metal binding4481Magnesium By similarity
Metal binding4751Magnesium By similarity
Binding site511Thiamine pyrophosphate By similarity
Binding site1531FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P40811-1 [UniParc].

Last modified December 19, 2001. Version 3.
Checksum: 72EB67FA2667B398

FASTA57462,896
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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

AE008699 Genomic DNA. Translation: AAL19080.1. Sequence problems.
X55456 Genomic DNA. Translation: CAA39101.1.
PIRS15939.
RefSeqNP_459121.1.

3D structure databases

HSSPHSSP built from PDB template 1N0H based on UniProtKB P07342.
ModBaseSearch...

Genome annotation databases

GeneID1251634.
GenomeReviewsGene locus STM0116 in contig AE006468_GR.
KEGGstm:STM0116.
NMPDRfig|99287.1.peg.114.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP40811.

Enzyme and pathway databases

BioCycSTYP99287:STM0116-MON.
BRENDA2.2.1.6. 2.

Family and domain databases

InterProIPR012846. Acetolactate_synth_lsu.
IPR000399. TPP_bd_CS.
IPR012001. TPP_bd_enzyme_N.
IPR011766. TPP_enzyme_bd_C.
IPR012000. TPP_enzyme_M.
[Graphical view]
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR00118. acolac_lg. 1 hit.
PROSITEPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameILVI_SALTY
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents