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A1W1X2 (LEU1_CAMJJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-isopropylmalate synthase

EC=2.3.3.13
Alternative name(s):
Alpha-IPM synthase
Alpha-isopropylmalate synthase
Gene names
Name:leuA
Ordered Locus Names:CJJ81176_0017
OrganismCampylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176) [Complete proteome] [HAMAP]
Taxonomic identifier354242 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate) By similarity. HAMAP-Rule MF_01025

Catalytic activity

Acetyl-CoA + 3-methyl-2-oxobutanoate + H2O = (2S)-2-isopropylmalate + CoA. HAMAP-Rule MF_01025

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4. HAMAP-Rule MF_01025

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01025

Sequence similarities

Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Branched-chain amino acid biosynthesis
Leucine biosynthesis
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processleucine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_function2-isopropylmalate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5115112-isopropylmalate synthase HAMAP-Rule MF_01025
PRO_1000149163

Sequences

Sequence LengthMass (Da)Tools
A1W1X2 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: D446F96FCB66A1D6

FASTA51156,350
        10         20         30         40         50         60 
MKDNKIIIFD TTLRDGEQAL GSSLGINQKL QIALALENLG VDVIEAGFPV SSQGDFKAVQ 

        70         80         90        100        110        120 
KIASKVKNST ICALSRALDK DIDMAYEALK VAKHFRIHTF IATSTLHMQD KLKKDFDEIL 

       130        140        150        160        170        180 
SMAKRAIIRA RSYTDDVEFS CEDAGRTPID NLCFMVENAI KAGAKTINIP DTVGYTLPSE 

       190        200        210        220        230        240 
FANIIKILFN KVPNIDKAII SVHCHNDLGV ATGNSLSAIL QGARQIECTI NGLGERAGNC 

       250        260        270        280        290        300 
ALEEVVMAIK TRKDYLKGFY TDIKCENIFK TSKLVSAITN ESIPSHKAIV GSNAFSHSSG 

       310        320        330        340        350        360 
IHQDGVLKNR QTYEIISPSA IGIHENRMLM TARSGRAMIK TCLENLGYDE NTYNLDDVYE 

       370        380        390        400        410        420 
RFLRLADKKG QVYDYDLEAL MFLSYENEEE NEFVIEKLSV ISGNIPTACV CMRIKEELKT 

       430        440        450        460        470        480 
EACTGNGPVE AVFNCIARIT NLKPALKAYS INAKSSGVDA QGQVDVDLEF KGRKFHGKGI 

       490        500        510 
STDVIEASAQ AFVSAYNAIY RSLKVEERKM A 

« Hide

References

[1]Fouts D.E., Nelson K.E., Sebastian Y.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 81-176.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000538 Genomic DNA. Translation: EAQ71916.1.
RefSeqYP_001001363.1. NC_008787.1.

3D structure databases

ProteinModelPortalA1W1X2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING354242.CJJ81176_0017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEAQ71916; EAQ71916; CJJ81176_0017.
GeneID4683377.
KEGGcjj:CJJ81176_0017.
PATRIC20053424. VBICamJej103413_1705.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0119.
HOGENOMHOG000046859.
KOK01649.
OMAEGQNALG.
OrthoDBEOG6CGCF3.

Enzyme and pathway databases

BioCycCJEJ354242:GC51-1698-MONOMER.
UniPathwayUPA00048; UER00070.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01025. LeuA_type1.
InterProIPR013709. 2-isopropylmalate_synth_dimer.
IPR002034. AIPM/Hcit_synth_CS.
IPR013785. Aldolase_TIM.
IPR005671. LeuA_bact_synth.
IPR000891. PYR_CT.
[Graphical view]
PfamPF00682. HMGL-like. 1 hit.
PF08502. LeuA_dimer. 1 hit.
[Graphical view]
SMARTSM00917. LeuA_dimer. 1 hit.
[Graphical view]
SUPFAMSSF110921. SSF110921. 1 hit.
TIGRFAMsTIGR00973. leuA_bact. 1 hit.
PROSITEPS00815. AIPM_HOMOCIT_SYNTH_1. 1 hit.
PS00816. AIPM_HOMOCIT_SYNTH_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEU1_CAMJJ
AccessionPrimary (citable) accession number: A1W1X2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways