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 large subunit

Gene

ilvB

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Miscellaneous

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 large subunit (ilvB)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. no protein annotated in this organism
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 large subunit (ilvB)
  2. Ketol-acid reductoisomerase (NADP(+)) (ilvC)
  3. Dihydroxy-acid dehydratase (ilvD)
  4. no protein annotated in this organism
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 sitei73Thiamine pyrophosphateBy similarity1
Binding sitei175FADBy similarity1
Metal bindingi467MagnesiumBy similarity1
Metal bindingi494MagnesiumBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi281 – 302FADBy similarityAdd BLAST22
Nucleotide bindingi324 – 343FADBy similarityAdd BLAST20

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciCORYNE:G18NG-10844-MONOMER
UniPathwayiUPA00047; UER00055
UPA00049; UER00059

Names & Taxonomyi

Protein namesi
Recommended name:
Acetolactate synthase large subunit (EC:2.2.1.6)
Short name:
AHAS
Alternative name(s):
Acetohydroxy-acid synthase large subunit
Short name:
ALS
Gene namesi
Name:ilvB
Ordered Locus Names:Cgl1271, cg1435
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000582 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000907871 – 626Acetolactate synthase large subunitAdd BLAST626

2D gel databases

World-2DPAGE0001:P42463

Interactioni

Subunit structurei

Dimer of large and small chains.

Protein-protein interaction databases

STRINGi196627.cg1435

Structurei

3D structure databases

ProteinModelPortaliP42463
SMRiP42463
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni416 – 496Thiamine pyrophosphate bindingAdd BLAST81

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105C7K Bacteria
COG0028 LUCA
HOGENOMiHOG000258448
KOiK01652
OMAiQGMVRQW

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.

P42463-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNVAASQQPT PATVASRGRS AAPERMTGAK AIVRSLEELN ADIVFGIPGG
60 70 80 90 100
AVLPVYDPLY SSTKVRHVLV RHEQGAGHAA TGYAQVTGRV GVCIATSGPG
110 120 130 140 150
ATNLVTPIAD ANLDSVPMVA ITGQVGSGLL GTDAFQEADI RGITMPVTKH
160 170 180 190 200
NFMVTNPNDI PQALAEAFHL AITGRPGPVL VDIPKDVQNA ELDFVWPPKI
210 220 230 240 250
DLPGYRPVST PHARQIEQAV KLIGEAKKPV LYVGGGVIKA DAHEELRAFA
260 270 280 290 300
EYTGIPVVTT LMALGTFPES HELHMGMPGM HGTVSAVGAL QRSDLLIAIG
310 320 330 340 350
SRFDDRVTGD VDTFAPDAKI IHADIDPAEI GKIKQVEVPI VGDAREVLAR
360 370 380 390 400
LLETTKASKA ETEDISEWVD YLKGLKARFP RGYDEQPGDL LAPQFVIETL
410 420 430 440 450
SKEVGPDAIY CAGVGQHQMW AAQFVDFEKP RTWLNSGGLG TMGYAVPAAL
460 470 480 490 500
GAKAGAPDKE VWAIDGDGCF QMTNQELTTA AVEGFPIKIA LINNGNLGMV
510 520 530 540 550
RQWQTLFYEG RYSNTKLRNQ GEYMPDFVTL SEGLGCVAIR VTKAEEVLPA
560 570 580 590 600
IQKAREINDR PVVIDFIVGE DAQVWPMVSA GSSNSDIQYA LGLRPFFDGD
610 620
ESAAEDPADI HEAVSDIDAA VESTEA
Length:626
Mass (Da):66,846
Last modified:November 1, 1995 - v1
Checksum:iC425E93F83B8A946
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09232 Genomic DNA Translation: AAA62429.1
BA000036 Genomic DNA Translation: BAB98664.1
BX927151 Genomic DNA Translation: CAF19974.1
PIRiA48648
RefSeqiNP_600493.1, NC_003450.3
WP_011014246.1, NC_006958.1

Genome annotation databases

EnsemblBacteriaiBAB98664; BAB98664; BAB98664
CAF19974; CAF19974; cg1435
GeneIDi1019252
KEGGicgb:cg1435
cgl:NCgl1222
PATRICifig|196627.13.peg.1248

Similar proteinsi

Entry informationi

Entry nameiILVB_CORGL
AccessioniPrimary (citable) accession number: P42463
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 23, 2018
This is version 127 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

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health