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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: Annotation score: 4 out of 5-Protein inferred from homologyi

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 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

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

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

Proteomic databases

PRIDEiP42463.

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.
OMAiMVWPMVP.

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.

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.
PATRICi21494584. VBICorGlu203724_1248.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP42463.
SMRiP42463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg1435.

2D gel databases

World-2DPAGE0001:P42463.

Proteomic databases

PRIDEiP42463.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB98664; BAB98664; BAB98664.
CAF19974; CAF19974; cg1435.
GeneIDi1019252.
KEGGicgb:cg1435.
cgl:NCgl1222.
PATRICi21494584. VBICorGlu203724_1248.

Phylogenomic databases

eggNOGiENOG4105C7K. Bacteria.
COG0028. LUCA.
HOGENOMiHOG000258448.
KOiK01652.
OMAiMVWPMVP.

Enzyme and pathway databases

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

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...

Entry informationi

Entry nameiILVB_CORGL
AccessioniPrimary (citable) accession number: P42463
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.