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Protein

Acetolactate synthase isozyme 1 large subunit

Gene

ilvB

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

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 sitei60Thiamine pyrophosphateBy similarity1
Binding sitei162FADBy similarity1
Metal bindingi444MagnesiumBy similarity1
Metal bindingi471MagnesiumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi264 – 285FADBy similarityAdd BLAST22
Nucleotide bindingi307 – 326FADBy similarityAdd BLAST20

GO - Molecular functioni

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:LARGEILVB-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10494 ilvB

Subcellular locationi

GO - Cellular componenti

  • acetolactate synthase complex Source: EcoCyc

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000907841 – 562Acetolactate synthase isozyme 1 large subunitAdd BLAST562

Proteomic databases

PaxDbiP08142
PRIDEiP08142

2D gel databases

SWISS-2DPAGEiP08142

Interactioni

Subunit structurei

Dimer of large and small chains.

Protein-protein interaction databases

BioGridi4262586, 11 interactors
DIPiDIP-10019N
IntActiP08142, 9 interactors
STRINGi316385.ECDH10B_3854

Structurei

3D structure databases

ProteinModelPortaliP08142
SMRiP08142
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni393 – 473Thiamine pyrophosphate bindingAdd BLAST81

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105C7K Bacteria
COG0028 LUCA
HOGENOMiHOG000258448
InParanoidiP08142
KOiK01652
OMAiFATCDLN
PhylomeDBiP08142

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.

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
PATRICifig|511145.12.peg.3793

Similar proteinsi

Entry informationi

Entry nameiILVB_ECOLI
AccessioniPrimary (citable) accession number: P08142
Secondary accession number(s): Q2M7Y4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: March 28, 2018
This is version 158 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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