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P00893 (ILVI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetolactate synthase isozyme 3 large subunit

EC=2.2.1.6
Alternative name(s):
AHAS-III
ALS-III
Acetohydroxy-acid synthase III large subunit
Gene names
Name:ilvI
Ordered Locus Names:b0077, JW0076
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 large and small chains.

Miscellaneous

E.coli 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 CAA25755.1 differs from that shown. Reason: Frameshift at position 523.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574Acetolactate synthase isozyme 3 large subunit
PRO_0000090789

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

Experimental info

Sequence conflict202 – 2032TL → SV in CAA25755. Ref.1
Sequence conflict202 – 2032TL → SV in CAA38854. Ref.5
Sequence conflict2061A → V in CAA25755. Ref.1
Sequence conflict2061A → V in CAA38854. Ref.5
Sequence conflict2541A → V in CAA25755. Ref.1
Sequence conflict2541A → V in CAA38854. Ref.5
Sequence conflict4221T → S in CAA25755. Ref.1
Sequence conflict4221T → S in CAA38854. Ref.5
Sequence conflict437 – 4382LP → FA in CAA38854. Ref.5
Sequence conflict507 – 5093LAE → RG in CAA25755. Ref.1
Sequence conflict507 – 5093LAE → RG in CAA38854. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P00893 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: B62DEF64338CBF8C

FASTA57462,984
        10         20         30         40         50         60 
MEMLSGAEMV VRSLIDQGVK QVFGYPGGAV LDIYDALHTV GGIDHVLVRH EQAAVHMADG 

        70         80         90        100        110        120 
LARATGEVGV VLVTSGPGAT NAITGIATAY MDSIPLVVLS GQVATSLIGY DAFQECDMVG 

       130        140        150        160        170        180 
ISRPVVKHSF LVKQTEDIPQ VLKKAFWLAA SGRPGPVVVD LPKDILNPAN KLPYVWPESV 

       190        200        210        220        230        240 
SMRSYNPTTT GHKGQIKRAL QTLVAAKKPV VYVGGGAITA GCHQQLKETV EALNLPVVCS 

       250        260        270        280        290        300 
LMGLGAFPAT HRQALGMLGM HGTYEANMTM HNADVIFAVG VRFDDRTTNN LAKYCPNATV 

       310        320        330        340        350        360 
LHIDIDPTSI SKTVTADIPI VGDARQVLEQ MLELLSQESA HQPLDEIRDW WQQIEQWRAR 

       370        380        390        400        410        420 
QCLKYDTHSE KIKPQAVIET LWRLTKGDAY VTSDVGQHQM FAALYYPFDK PRRWINSGGL 

       430        440        450        460        470        480 
GTMGFGLPAA LGVKMALPEE TVVCVTGDGS IQMNIQELST ALQYELPVLV VNLNNRYLGM 

       490        500        510        520        530        540 
VKQWQDMIYS GRHSQSYMQS LPDFVRLAEA YGHVGIQISH PHELESKLSE ALEQVRNNRL 

       550        560        570 
VFVDVTVDGS EHVYPMQIRG GGMDEMWLSK TERT 

« Hide

References

« Hide 'large scale' references
[1]"Molecular structure of ilvIH and its evolutionary relationship to ilvG in Escherichia coli K12."
Squires C.H., Defelice M., Devereux J., Calvo J.M.
Nucleic Acids Res. 11:5299-5313(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Regulation of transcription at the 2-minute region of the genetic map of Escherichia coli."
Ayala J.A.
Submitted (JAN-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Unusual organization of the ilvIH promoter of Escherichia coli."
Haughn G.W., Squires C.H., Defelice M., Largo C.T., Calvo J.M.
J. Bacteriol. 163:186-198(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
[7]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X01609 Genomic DNA. Translation: CAA25755.1. Frameshift.
U00096 Genomic DNA. Translation: AAC73188.2.
AP009048 Genomic DNA. Translation: BAB96646.2.
X55034 Genomic DNA. Translation: CAA38854.1.
M10738 Genomic DNA. Translation: AAA24026.1.
PIRYCEC3I. E64729.
RefSeqYP_025294.2. NC_000913.3.
YP_488383.1. NC_007779.1.

3D structure databases

ProteinModelPortalP00893.
SMRP00893. Positions 4-565.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6850N.
IntActP00893. 7 interactions.
STRING511145.b0077.

Proteomic databases

PaxDbP00893.
PRIDEP00893.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73188; AAC73188; b0077.
BAB96646; BAB96646; BAB96646.
GeneID12930386.
948793.
KEGGecj:Y75_p0077.
eco:b0077.
PATRIC32115257. VBIEscCol129921_0080.

Organism-specific databases

EchoBASEEB0495.
EcoGeneEG10500. ilvI.

Phylogenomic databases

eggNOGCOG0028.
HOGENOMHOG000258448.
KOK01652.
OMAKFDKPNR.
OrthoDBEOG6KT2NW.
PhylomeDBP00893.

Enzyme and pathway databases

BioCycEcoCyc:ACETOLACTSYNIII-ICHAIN-MONOMER.
ECOL316407:JW0076-MONOMER.
MetaCyc:ACETOLACTSYNIII-ICHAIN-MONOMER.
UniPathwayUPA00047; UER00055.
UPA00049; UER00059.

Gene expression databases

GenevestigatorP00893.

Family and domain databases

Gene3D3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProIPR012846. Acetolactate_synth_lsu.
IPR029035. DHS-like_NAD/FAD-binding_dom.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsTIGR00118. acolac_lg. 1 hit.
PROSITEPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP00893.

Entry information

Entry nameILVI_ECOLI
AccessionPrimary (citable) accession number: P00893
Secondary accession number(s): P78045
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: June 11, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene