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Protein

Acetolactate synthase isozyme 1 large subunit

Gene

ilvB

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

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 (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), 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 (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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei60 – 601Thiamine pyrophosphateBy similarity
Binding sitei162 – 1621FADBy similarity
Metal bindingi444 – 4441MagnesiumBy similarity
Metal bindingi471 – 4711MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi264 – 28522FADBy similarityAdd
BLAST
Nucleotide bindingi307 – 32620FADBy similarityAdd
BLAST

GO - Molecular functioni

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:LARGEILVB-MONOMER.
ECOL316407:JW3646-MONOMER.
MetaCyc:LARGEILVB-MONOMER.
UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetolactate synthase isozyme 1 large subunit (EC:2.2.1.6)
Short name:
AHAS-I
Alternative name(s):
Acetohydroxy-acid synthase I large subunit
Short name:
ALS-I
Gene namesi
Name:ilvB
Ordered Locus Names:b3671, JW3646
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10494. ilvB.

Subcellular locationi

GO - Cellular componenti

  • acetolactate synthase complex Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 562562Acetolactate synthase isozyme 1 large subunitPRO_0000090784Add
BLAST

Proteomic databases

PaxDbiP08142.

2D gel databases

SWISS-2DPAGEP08142.

Interactioni

Subunit structurei

Dimer of large and small chains.

Protein-protein interaction databases

BioGridi4262586. 11 interactions.
DIPiDIP-10019N.
IntActiP08142. 9 interactions.
MINTiMINT-1243593.
STRINGi511145.b3671.

Structurei

3D structure databases

ProteinModelPortaliP08142.
SMRiP08142. Positions 15-562.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni393 – 47381Thiamine pyrophosphate bindingAdd
BLAST

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105C7K. Bacteria.
COG0028. LUCA.
HOGENOMiHOG000258448.
InParanoidiP08142.
KOiK01652.
OMAiCMASSGP.
OrthoDBiEOG6KT2NW.
PhylomeDBiP08142.

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.

P08142-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSGTTSTR KRFTGAEFIV HFLEQQGIKI VTGIPGGSIL PVYDALSQST
60 70 80 90 100
QIRHILARHE QGAGFIAQGM ARTDGKPAVC MACSGPGATN LVTAIADARL
110 120 130 140 150
DSIPLICITG QVPASMIGTD AFQEVDTYGI SIPITKHNYL VRHIEELPQV
160 170 180 190 200
MSDAFRIAQS GRPGPVWIDI PKDVQTAVFE IETQPAMAEK AAAPAFSEES
210 220 230 240 250
IRDAAAMINA AKRPVLYLGG GVINAPARVR ELAEKAQLPT TMTLMALGML
260 270 280 290 300
PKAHPLSLGM LGMHGVRSTN YILQEADLLI VLGARFDDRA IGKTEQFCPN
310 320 330 340 350
AKIIHVDIDR AELGKIKQPH VAIQADVDDV LAQLIPLVEA QPRAEWHQLV
360 370 380 390 400
ADLQREFPCP IPKACDPLSH YGLINAVAAC VDDNAIITTD VGQHQMWTAQ
410 420 430 440 450
AYPLNRPRQW LTSGGLGTMG FGLPAAIGAA LANPDRKVLC FSGDGSLMMN
460 470 480 490 500
IQEMATASEN QLDVKIILMN NEALGLVHQQ QSLFYEQGVF AATYPGKINF
510 520 530 540 550
MQIAAGFGLE TCDLNNEADP QASLQEIINR PGPALIHVRI DAEEKVYPMV
560
PPGAANTEMV GE
Length:562
Mass (Da):60,441
Last modified:August 1, 1988 - v1
Checksum:i70F8A3128031353C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02541 Genomic DNA. Translation: CAA26387.1.
L10328 Genomic DNA. Translation: AAA62023.1.
U00096 Genomic DNA. Translation: AAC76694.1.
AP009048 Genomic DNA. Translation: BAE77622.1.
PIRiA93569. YCEC1L.
RefSeqiNP_418127.1. NC_000913.3.
WP_000168475.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76694; AAC76694; b3671.
BAE77622; BAE77622; BAE77622.
GeneIDi948182.
KEGGiecj:JW3646.
eco:b3671.
PATRICi32122835. VBIEscCol129921_3793.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02541 Genomic DNA. Translation: CAA26387.1.
L10328 Genomic DNA. Translation: AAA62023.1.
U00096 Genomic DNA. Translation: AAC76694.1.
AP009048 Genomic DNA. Translation: BAE77622.1.
PIRiA93569. YCEC1L.
RefSeqiNP_418127.1. NC_000913.3.
WP_000168475.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP08142.
SMRiP08142. Positions 15-562.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262586. 11 interactions.
DIPiDIP-10019N.
IntActiP08142. 9 interactions.
MINTiMINT-1243593.
STRINGi511145.b3671.

2D gel databases

SWISS-2DPAGEP08142.

Proteomic databases

PaxDbiP08142.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76694; AAC76694; b3671.
BAE77622; BAE77622; BAE77622.
GeneIDi948182.
KEGGiecj:JW3646.
eco:b3671.
PATRICi32122835. VBIEscCol129921_3793.

Organism-specific databases

EchoBASEiEB0489.
EcoGeneiEG10494. ilvB.

Phylogenomic databases

eggNOGiENOG4105C7K. Bacteria.
COG0028. LUCA.
HOGENOMiHOG000258448.
InParanoidiP08142.
KOiK01652.
OMAiCMASSGP.
OrthoDBiEOG6KT2NW.
PhylomeDBiP08142.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00055.
UPA00049; UER00059.
BioCyciEcoCyc:LARGEILVB-MONOMER.
ECOL316407:JW3646-MONOMER.
MetaCyc:LARGEILVB-MONOMER.

Miscellaneous databases

PROiP08142.

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. "The nucleotide sequence of the ilvBN operon of Escherichia coli: sequence homologies of the acetohydroxy acid synthase isozymes."
    Wek R.C., Hausser C.A., Hatfield G.W.
    Nucleic Acids Res. 13:3995-4010(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The ilvB locus of Escherichia coli K-12 is an operon encoding both subunits of acetohydroxyacid synthase I."
    Friden P., Donegan J., Mullen J., Tsui P., Freundlich M.
    Nucleic Acids Res. 13:3979-3993(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
    Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
    Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. "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].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

Entry informationi

Entry nameiILVB_ECOLI
AccessioniPrimary (citable) accession number: P08142
Secondary accession number(s): Q2M7Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: January 20, 2016
This is version 149 of the entry and version 1 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, 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

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.