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Reviewed, UniProtKB/Swiss-Prot P27696 (ILVB_KLEPN)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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, catabolic
      Short name=ALS
    EC=2.2.1.6
Gene names
Name: budB
Synonyms: ilvK
OrganismKlebsiella pneumoniae
Taxonomic identifier573 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length559 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.

Pathway

Polyol metabolism; 2,3-butanediol biosynthesis; (R,R)-2,3-butanediol from pyruvate: step 1/3.

Miscellaneous

Does not seem to require thiamine pyrophosphate.

Valine resistant.

Sequence similarities

Belongs to the TPP enzyme family.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 559559Acetolactate synthase, catabolic
PRO_0000090797

Regions

Nucleotide binding263 – 28422FAD By similarity
Nucleotide binding304 – 32320FAD By similarity

Sites

Metal binding4471Magnesium By similarity
Binding site1591FAD By similarity

Secondary structure

............................................................................................................. 559
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27696-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 7775373ABEEE603D

FASTA55960,338
        10         20         30         40         50         60 
MDKQYPVRQW AHGADLVVSQ LEAQGVRQVF GIPGAKIDKV FDSLLDSSIR IIPVRHEANA 

        70         80         90        100        110        120 
AFMAAAVGRI TGKAGVALVT SGPGCSNLIT GMATANSEGD PVVALGGAVK RADKAKQVHQ 

       130        140        150        160        170        180 
SMDTVAMFSP VTKYAIEVTA PDALAEVVSN AFRAAEQGRP GSAFVSLPQD VVDGPVSGKV 

       190        200        210        220        230        240 
LPASGAPQMG AAPDDAIDQV AKLIAQAKNP IFLLGLMASQ PENSKALRRL LETSHIPVTS 

       250        260        270        280        290        300 
TYQAAGAVNQ DNFSRFAGRV GLFNNQAGDR LLQLADLVIC IGYSPVEYEP AMWNSGNATL 

       310        320        330        340        350        360 
VHIDVLPAYE ERNYTPDVEL VGDIAGTLNK LAQNIDHRLV LSPQAAEILR DRQHQRELLD 

       370        380        390        400        410        420 
RRGAQLNQFA LHPLRIVRAM QDIVNSDVTL TVDMGSFHIW IARYLYTFRA RQVMISNGQQ 

       430        440        450        460        470        480 
TMGVALPWAI GAWLVNPERK VVSVSGDGGF LQSSMELETA VRLKANVLHL IWVDNGYNMV 

       490        500        510        520        530        540 
AIQEEKKYQR LSGVEFGPMD FKAYAESFGA KGFAVESAEA LEPTLRAAMD VDGPAVVAIP 

       550 
VDYRDNPLLM GQLHLSQIL 

« Hide

References

[1]"Cloning, sequencing and heterologous expression of a Klebsiella pneumoniae gene encoding an FAD-independent acetolactate synthase."
Peng H.-L., Wang P.-Y., Wu C.-M., Hwang D.-C., Chang H.-Y.
Gene 117:125-130(1992) [PubMed: 1644303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate."
Pang S.S., Duggleby R.G., Schowen R.L., Guddat L.W.
J. Biol. Chem. 279:2242-2253(2004) [PubMed: 14557277] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Cross-references

Sequence databases

M73842 Genomic DNA. Translation: AAA25079.1.
PIRJC1218.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1OZFX-ray2.30A/B1-559[»]
1OZGX-ray2.30A/B1-559[»]
1OZHX-ray2.00A/B/C/D1-559[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.2.1.6. 758.

Family and domain databases

InterProIPR012782. Acetolactate_synth_catblc.
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]
TIGRFAMsTIGR02418. acolac_catab. 1 hit.
PROSITEPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameILVB_KLEPN
AccessionPrimary (citable) accession number: P27696
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 16, 2009
This is version 63 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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