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Protein

Acetolactate synthase isozyme 3 large subunit

Gene

ilvI

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

Functioni

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

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.

Pathwayi: 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 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Putative acetolactate synthase isozyme 2 large subunit (ilvG), Acetolactate synthase isozyme 2 large subunit (ilvG), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. 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.

Pathwayi: 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 1 small subunit (ilvN), Acetolactate synthase isozyme 1 large subunit (ilvB), Putative acetolactate synthase isozyme 2 large subunit (ilvG), Acetolactate synthase isozyme 2 large subunit (ilvG), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. 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)DescriptionActionsGraphical viewLength
Binding sitei51Thiamine pyrophosphateBy similarity1
Binding sitei153FADBy similarity1
Metal bindingi448MagnesiumBy similarity1
Metal bindingi475MagnesiumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi261 – 282FADBy similarityAdd BLAST22
Nucleotide bindingi304 – 323FADBy similarityAdd BLAST20

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

Keywordsi

Molecular functionTransferase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
LigandFAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciEcoCyc:ACETOLACTSYNIII-ICHAIN-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10500 ilvI

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000907891 – 574Acetolactate synthase isozyme 3 large subunitAdd BLAST574

Proteomic databases

PaxDbiP00893
PRIDEiP00893

Interactioni

Subunit structurei

Dimer of large and small chains.

Protein-protein interaction databases

BioGridi4259380, 38 interactors
DIPiDIP-6850N
IntActiP00893, 7 interactors
STRINGi316407.85674319

Structurei

3D structure databases

ProteinModelPortaliP00893
SMRiP00893
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni397 – 477Thiamine pyrophosphate bindingAdd BLAST81

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105C7K Bacteria
COG0028 LUCA
HOGENOMiHOG000258448
InParanoidiP00893
KOiK01652
OMAiQGMVRQW
PhylomeDBiP00893

Family and domain databases

InterProiView protein in InterPro
IPR012846 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
PfamiView protein in Pfam
PF02775 TPP_enzyme_C, 1 hit
PF00205 TPP_enzyme_M, 1 hit
PF02776 TPP_enzyme_N, 1 hit
SUPFAMiSSF52467 SSF52467, 1 hit
SSF52518 SSF52518, 2 hits
TIGRFAMsiTIGR00118 acolac_lg, 1 hit
PROSITEiView protein in PROSITE
PS00187 TPP_ENZYMES, 1 hit

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 differs from that shown. Reason: Frameshift at position 523.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti202 – 203TL → SV in CAA25755 (PubMed:6308579).Curated2
Sequence conflicti202 – 203TL → SV in CAA38854 (Ref. 5) Curated2
Sequence conflicti206A → V in CAA25755 (PubMed:6308579).Curated1
Sequence conflicti206A → V in CAA38854 (Ref. 5) Curated1
Sequence conflicti254A → V in CAA25755 (PubMed:6308579).Curated1
Sequence conflicti254A → V in CAA38854 (Ref. 5) Curated1
Sequence conflicti422T → S in CAA25755 (PubMed:6308579).Curated1
Sequence conflicti422T → S in CAA38854 (Ref. 5) Curated1
Sequence conflicti437 – 438LP → FA in CAA38854 (Ref. 5) Curated2
Sequence conflicti507 – 509LAE → RG in CAA25755 (PubMed:6308579).Curated3
Sequence conflicti507 – 509LAE → RG in CAA38854 (Ref. 5) Curated3

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
RefSeqiWP_001295534.1, NZ_LN832404.1
YP_025294.2, NC_000913.3

Genome annotation databases

EnsemblBacteriaiAAC73188; AAC73188; b0077
BAB96646; BAB96646; BAB96646
GeneIDi948793
KEGGiecj:JW0076
eco:b0077
PATRICifig|1411691.4.peg.2203

Similar proteinsi

Entry informationi

Entry nameiILVI_ECOLI
AccessioniPrimary (citable) accession number: P00893
Secondary accession number(s): P78045
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 158 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health