Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetolactate synthase isozyme 3 small subunit

Gene

ilvH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

2 pyruvate = 2-acetolactate + CO2.

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), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (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), Acetolactate synthase isozyme 2 small subunit (ilvM), Acetolactate synthase isozyme 3 large subunit (ilvI), Acetolactate synthase isozyme 3 small subunit (ilvH), Acetolactate synthase isozyme 2 large subunit (ilvG)
  2. Ketol-acid reductoisomerase (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.

GO - Molecular functioni

  • acetolactate synthase activity Source: EcoCyc
  • amino acid binding Source: InterPro

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

Enzyme and pathway databases

BioCyciEcoCyc:ACETOLACTSYNIII-HCHAIN-MONOMER.
ECOL316407:JW0077-MONOMER.
MetaCyc:ACETOLACTSYNIII-HCHAIN-MONOMER.
UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetolactate synthase isozyme 3 small subunit (EC:2.2.1.6)
Alternative name(s):
ALS-III
Acetohydroxy-acid synthase III small subunit
Short name:
AHAS-III
Gene namesi
Name:ilvH
Synonyms:brnP
Ordered Locus Names:b0078, JW0077
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10499. ilvH.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 163163Acetolactate synthase isozyme 3 small subunitPRO_0000151410Add
BLAST

Proteomic databases

EPDiP00894.
PaxDbiP00894.
PRIDEiP00894.

2D gel databases

SWISS-2DPAGEP00894.

Interactioni

Subunit structurei

Dimer of large and small chains.

Protein-protein interaction databases

BioGridi4259381. 5 interactions.
DIPiDIP-10024N.
IntActiP00894. 1 interaction.
STRINGi511145.b0078.

Structurei

Secondary structure

1
163
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Helixi15 – 2410Combined sources
Turni25 – 273Combined sources
Beta strandi31 – 377Combined sources
Beta strandi41 – 5212Combined sources
Helixi54 – 6613Combined sources
Beta strandi70 – 756Combined sources
Helixi76 – 783Combined sources
Beta strandi81 – 9212Combined sources
Helixi96 – 10712Combined sources
Beta strandi111 – 1155Combined sources
Beta strandi117 – 12610Combined sources
Helixi128 – 13811Combined sources
Turni139 – 1413Combined sources
Beta strandi142 – 1498Combined sources
Beta strandi153 – 1575Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F1FX-ray1.75A/B1-163[»]
ProteinModelPortaliP00894.
SMRiP00894. Positions 2-163.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00894.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 7875ACTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ACT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4108ZP8. Bacteria.
COG0440. LUCA.
HOGENOMiHOG000046747.
InParanoidiP00894.
KOiK01653.
OMAiPYGIREI.
OrthoDBiEOG6X3W8W.
PhylomeDBiP00894.

Family and domain databases

InterProiIPR004789. Acetalactate_synth_ssu.
IPR019455. Acetolactate_synth_ssu_C.
IPR002912. ACT_dom.
[Graphical view]
PfamiPF10369. ALS_ss_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00119. acolac_sm. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRILSVLLE NESGALSRVI GLFSQRGYNI ESLTVAPTDD PTLSRMTIQT
60 70 80 90 100
VGDEKVLEQI EKQLHKLVDV LRVSELGQGA HVEREIMLVK IQASGYGRDE
110 120 130 140 150
VKRNTEIFRG QIIDVTPSLY TVQLAGTSGK LDAFLASIRD VAKIVEVARS
160
GVVGLSRGDK IMR
Length:163
Mass (Da):17,977
Last modified:July 19, 2003 - v3
Checksum:iD6E28AE94A55606E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321D → S (PubMed:6308579).Curated
Sequence conflicti132 – 1321D → S (PubMed:1630901).Curated
Sequence conflicti132 – 1321D → S (PubMed:1851954).Curated
Sequence conflicti159 – 1635DKIMR → VK in CAA25756 (PubMed:6308579).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01609 Genomic DNA. Translation: CAA25756.1.
X55457 Genomic DNA. No translation available.
X55034 Genomic DNA. Translation: CAA38855.1.
U00096 Genomic DNA. Translation: AAC73189.1.
AP009048 Genomic DNA. Translation: BAB96647.2.
M35034 Genomic DNA. Translation: AAA24627.1.
PIRiF64729. YCEC3H.
RefSeqiNP_414620.1. NC_000913.3.
WP_001300383.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73189; AAC73189; b0078.
BAB96647; BAB96647; BAB96647.
GeneIDi947267.
KEGGiecj:JW0077.
eco:b0078.
PATRICi32115259. VBIEscCol129921_0081.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01609 Genomic DNA. Translation: CAA25756.1.
X55457 Genomic DNA. No translation available.
X55034 Genomic DNA. Translation: CAA38855.1.
U00096 Genomic DNA. Translation: AAC73189.1.
AP009048 Genomic DNA. Translation: BAB96647.2.
M35034 Genomic DNA. Translation: AAA24627.1.
PIRiF64729. YCEC3H.
RefSeqiNP_414620.1. NC_000913.3.
WP_001300383.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F1FX-ray1.75A/B1-163[»]
ProteinModelPortaliP00894.
SMRiP00894. Positions 2-163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259381. 5 interactions.
DIPiDIP-10024N.
IntActiP00894. 1 interaction.
STRINGi511145.b0078.

2D gel databases

SWISS-2DPAGEP00894.

Proteomic databases

EPDiP00894.
PaxDbiP00894.
PRIDEiP00894.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73189; AAC73189; b0078.
BAB96647; BAB96647; BAB96647.
GeneIDi947267.
KEGGiecj:JW0077.
eco:b0078.
PATRICi32115259. VBIEscCol129921_0081.

Organism-specific databases

EchoBASEiEB0494.
EcoGeneiEG10499. ilvH.

Phylogenomic databases

eggNOGiENOG4108ZP8. Bacteria.
COG0440. LUCA.
HOGENOMiHOG000046747.
InParanoidiP00894.
KOiK01653.
OMAiPYGIREI.
OrthoDBiEOG6X3W8W.
PhylomeDBiP00894.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.
BioCyciEcoCyc:ACETOLACTSYNIII-HCHAIN-MONOMER.
ECOL316407:JW0077-MONOMER.
MetaCyc:ACETOLACTSYNIII-HCHAIN-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP00894.
PROiP00894.

Family and domain databases

InterProiIPR004789. Acetalactate_synth_ssu.
IPR019455. Acetolactate_synth_ssu_C.
IPR002912. ACT_dom.
[Graphical view]
PfamiPF10369. ALS_ss_C. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00119. acolac_sm. 1 hit.
PROSITEiPS51671. ACT. 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 TO 132.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 130-163.
    Strain: K12.
  6. "Molecular cloning, nucleotide sequence, and expression of shl, a new gene in the 2-minute region of the genetic map of Escherichia coli."
    Leclerc G., Noel G., Drapeau G.R.
    J. Bacteriol. 172:4696-4700(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 130-163.

Entry informationi

Entry nameiILVH_ECOLI
AccessioniPrimary (citable) accession number: P00894
Secondary accession number(s): P78046, Q47637
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 19, 2003
Last modified: March 16, 2016
This is version 142 of the entry and version 3 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.

Keywords - Technical termi

3D-structure, Complete proteome, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.