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Reviewed, UniProtKB/Swiss-Prot P42463 (ILVB_CORGL)

Last modified June 16, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Acetolactate synthase large subunit
      Short name=AHAS
    EC=2.2.1.6
Alternative name(s):
    Acetohydroxy-acid synthase large subunit
      Short name=ALS
Gene names
Name: ilvB
Ordered Locus Names: Cgl1271, cg1435
OrganismCorynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length626 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

2 pyruvate = 2-acetolactate + CO2.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Binds 1 thiamine pyrophosphate per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.

Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4.

Subunit structure

Dimer of large and small chains.

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.

Sequence similarities

Belongs to the TPP enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 626626Acetolactate synthase large subunit
PRO_0000090787

Regions

Nucleotide binding281 – 30222FAD By similarity
Nucleotide binding324 – 34320FAD By similarity
Region416 – 49681Thiamine pyrophosphate binding

Sites

Metal binding4671Magnesium By similarity
Metal binding4941Magnesium By similarity
Binding site731Thiamine pyrophosphate By similarity
Binding site1751FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
P42463-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: C425E93F83B8A946

FASTA62666,846
        10         20         30         40         50         60 
MNVAASQQPT PATVASRGRS AAPERMTGAK AIVRSLEELN ADIVFGIPGG AVLPVYDPLY 

        70         80         90        100        110        120 
SSTKVRHVLV RHEQGAGHAA TGYAQVTGRV GVCIATSGPG ATNLVTPIAD ANLDSVPMVA 

       130        140        150        160        170        180 
ITGQVGSGLL GTDAFQEADI RGITMPVTKH NFMVTNPNDI PQALAEAFHL AITGRPGPVL 

       190        200        210        220        230        240 
VDIPKDVQNA ELDFVWPPKI DLPGYRPVST PHARQIEQAV KLIGEAKKPV LYVGGGVIKA 

       250        260        270        280        290        300 
DAHEELRAFA EYTGIPVVTT LMALGTFPES HELHMGMPGM HGTVSAVGAL QRSDLLIAIG 

       310        320        330        340        350        360 
SRFDDRVTGD VDTFAPDAKI IHADIDPAEI GKIKQVEVPI VGDAREVLAR LLETTKASKA 

       370        380        390        400        410        420 
ETEDISEWVD YLKGLKARFP RGYDEQPGDL LAPQFVIETL SKEVGPDAIY CAGVGQHQMW 

       430        440        450        460        470        480 
AAQFVDFEKP RTWLNSGGLG TMGYAVPAAL GAKAGAPDKE VWAIDGDGCF QMTNQELTTA 

       490        500        510        520        530        540 
AVEGFPIKIA LINNGNLGMV RQWQTLFYEG RYSNTKLRNQ GEYMPDFVTL SEGLGCVAIR 

       550        560        570        580        590        600 
VTKAEEVLPA IQKAREINDR PVVIDFIVGE DAQVWPMVSA GSSNSDIQYA LGLRPFFDGD 

       610        620 
ESAAEDPADI HEAVSDIDAA VESTEA 

« Hide

References

« Hide 'large scale' references
[1]"Isoleucine synthesis in Corynebacterium glutamicum: molecular analysis of the ilvB-ilvN-ilvC operon."
Keilhauer C., Eggeling L., Sahm H.
J. Bacteriol. 175:5595-5603(1993) [PubMed: 8366043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

L09232 Genomic DNA. Translation: AAA62429.1.
BA000036 Genomic DNA. Translation: BAB98664.1.
BX927151 Genomic DNA. Translation: CAF19974.1.
PIRA48648.
RefSeqNP_600493.1.
YP_225560.1.

3D structure databases

HSSPHSSP built from PDB template 1N0H based on UniProtKB P07342.
ModBaseSearch...

2-D gel databases

World-2DPAGE0001:P42463.

Proteomic databases

PRIDEP42463.

Genome annotation databases

GeneID1019252.
3345149.
GenomeReviewsGene locus Cgl1271 in contig BA000036_GR.
Gene locus cg1435 in contig BX927147_GR.
KEGGcgb:cg1435.
cgl:NCgl1222.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP42463.
OMAP42463. DIPRIVH.

Enzyme and pathway databases

BioCycCGLU196627-1:CG1435-MON.
BRENDA2.2.1.6. 812.

Family and domain databases

InterProIPR012846. Acetolactate_synth_lsu.
IPR000399. TPP_bd_CS.
IPR012001. TPP_bd_enzyme_N.
IPR011766. TPP_enzyme_bd_C.
IPR012000. TPP_enzyme_M.
[Graphical view]
PfamPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR00118. acolac_lg. 1 hit.
PROSITEPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameILVB_CORGL
AccessionPrimary (citable) accession number: P42463
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents