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Protein

Acetolactate synthase isozyme 3 large subunit

Gene

ilvI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 pyruvate = 2-acetolactate + CO2.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity
  • thiamine diphosphateBy similarityNote: Binds 1 thiamine pyrophosphate per subunit.By similarity

Enzyme regulationi

Sensitive to valine inhibition.

Pathway: L-isoleucine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase (ilvB), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase (ilvI), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (ilvC), Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathway: L-valine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase (ilvB), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase (ilvI), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (ilvC), Ketol-acid reductoisomerase (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD), Dihydroxy-acid dehydratase (ilvD)
  4. Branched-chain-amino-acid aminotransferase (ilvE)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511Thiamine pyrophosphateBy similarity
Binding sitei153 – 1531FADBy similarity
Metal bindingi448 – 4481MagnesiumBy similarity
Metal bindingi475 – 4751MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi261 – 28222FADBy similarityAdd
BLAST
Nucleotide bindingi304 – 32320FADBy similarityAdd
BLAST

GO - Molecular functioni

  • acetolactate synthase activity Source: EcoCyc
  • flavin adenine dinucleotide binding Source: InterPro
  • magnesium ion binding Source: EcoCyc
  • thiamine pyrophosphate binding Source: EcoCyc

GO - Biological processi

  • isoleucine biosynthetic process Source: EcoCyc
  • valine biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

FAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciEcoCyc:ACETOLACTSYNIII-ICHAIN-MONOMER.
ECOL316407:JW0076-MONOMER.
MetaCyc:ACETOLACTSYNIII-ICHAIN-MONOMER.
UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ilvI
Ordered Locus Names:b0077, JW0076
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10500. ilvI.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 574574Acetolactate synthase isozyme 3 large subunitPRO_0000090789Add
BLAST

Proteomic databases

PaxDbiP00893.
PRIDEiP00893.

Interactioni

Subunit structurei

Dimer of large and small chains.

Protein-protein interaction databases

DIPiDIP-6850N.
IntActiP00893. 7 interactions.
STRINGi511145.b0077.

Structurei

3D structure databases

ProteinModelPortaliP00893.
SMRiP00893. Positions 4-565.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni397 – 47781Thiamine pyrophosphate bindingAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiCOG0028.
HOGENOMiHOG000258448.
InParanoidiP00893.
KOiK01652.
OMAiVGMPGMH.
OrthoDBiEOG6KT2NW.
PhylomeDBiP00893.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR012846. 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]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00118. acolac_lg. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00893-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMLSGAEMV VRSLIDQGVK QVFGYPGGAV LDIYDALHTV GGIDHVLVRH
60 70 80 90 100
EQAAVHMADG LARATGEVGV VLVTSGPGAT NAITGIATAY MDSIPLVVLS
110 120 130 140 150
GQVATSLIGY DAFQECDMVG ISRPVVKHSF LVKQTEDIPQ VLKKAFWLAA
160 170 180 190 200
SGRPGPVVVD LPKDILNPAN KLPYVWPESV SMRSYNPTTT GHKGQIKRAL
210 220 230 240 250
QTLVAAKKPV VYVGGGAITA GCHQQLKETV EALNLPVVCS LMGLGAFPAT
260 270 280 290 300
HRQALGMLGM HGTYEANMTM HNADVIFAVG VRFDDRTTNN LAKYCPNATV
310 320 330 340 350
LHIDIDPTSI SKTVTADIPI VGDARQVLEQ MLELLSQESA HQPLDEIRDW
360 370 380 390 400
WQQIEQWRAR QCLKYDTHSE KIKPQAVIET LWRLTKGDAY VTSDVGQHQM
410 420 430 440 450
FAALYYPFDK PRRWINSGGL GTMGFGLPAA LGVKMALPEE TVVCVTGDGS
460 470 480 490 500
IQMNIQELST ALQYELPVLV VNLNNRYLGM VKQWQDMIYS GRHSQSYMQS
510 520 530 540 550
LPDFVRLAEA YGHVGIQISH PHELESKLSE ALEQVRNNRL VFVDVTVDGS
560 570
EHVYPMQIRG GGMDEMWLSK TERT
Length:574
Mass (Da):62,984
Last modified:November 1, 1997 - v2
Checksum:iB62DEF64338CBF8C
GO

Sequence cautioni

The sequence CAA25755.1 differs from that shown. Reason: Frameshift at position 523. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2032TL → SV in CAA25755 (PubMed:6308579).Curated
Sequence conflicti202 – 2032TL → SV in CAA38854 (Ref. 5) Curated
Sequence conflicti206 – 2061A → V in CAA25755 (PubMed:6308579).Curated
Sequence conflicti206 – 2061A → V in CAA38854 (Ref. 5) Curated
Sequence conflicti254 – 2541A → V in CAA25755 (PubMed:6308579).Curated
Sequence conflicti254 – 2541A → V in CAA38854 (Ref. 5) Curated
Sequence conflicti422 – 4221T → S in CAA25755 (PubMed:6308579).Curated
Sequence conflicti422 – 4221T → S in CAA38854 (Ref. 5) Curated
Sequence conflicti437 – 4382LP → FA in CAA38854 (Ref. 5) Curated
Sequence conflicti507 – 5093LAE → RG in CAA25755 (PubMed:6308579).Curated
Sequence conflicti507 – 5093LAE → RG in CAA38854 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiE64729. YCEC3I.
RefSeqiYP_025294.2. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC73188; AAC73188; b0077.
BAB96646; BAB96646; BAB96646.
GeneIDi948793.
KEGGiecj:Y75_p0077.
eco:b0077.
PATRICi32115257. VBIEscCol129921_0080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiE64729. YCEC3I.
RefSeqiYP_025294.2. NC_000913.3.

3D structure databases

ProteinModelPortaliP00893.
SMRiP00893. Positions 4-565.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6850N.
IntActiP00893. 7 interactions.
STRINGi511145.b0077.

Proteomic databases

PaxDbiP00893.
PRIDEiP00893.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73188; AAC73188; b0077.
BAB96646; BAB96646; BAB96646.
GeneIDi948793.
KEGGiecj:Y75_p0077.
eco:b0077.
PATRICi32115257. VBIEscCol129921_0080.

Organism-specific databases

EchoBASEiEB0495.
EcoGeneiEG10500. ilvI.

Phylogenomic databases

eggNOGiCOG0028.
HOGENOMiHOG000258448.
InParanoidiP00893.
KOiK01652.
OMAiVGMPGMH.
OrthoDBiEOG6KT2NW.
PhylomeDBiP00893.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.
BioCyciEcoCyc:ACETOLACTSYNIII-ICHAIN-MONOMER.
ECOL316407:JW0076-MONOMER.
MetaCyc:ACETOLACTSYNIII-ICHAIN-MONOMER.

Miscellaneous databases

PROiP00893.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR012846. 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]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00118. acolac_lg. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiILVI_ECOLI
AccessioniPrimary (citable) accession number: P00893
Secondary accession number(s): P78045
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: June 24, 2015
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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).By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.