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Q48LY5 (LEU1_PSE14) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:PSPPH_1329
OrganismPseudomonas syringae pv. phaseolicola (strain 1448A / Race 6) [Complete proteome] [HAMAP]
Taxonomic identifier264730 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length556 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_00572

Catalytic activity

Acetyl-CoA + 3-methyl-2-oxobutanoate + H2O = (2S)-2-isopropylmalate + CoA. HAMAP-Rule MF_00572

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4. HAMAP-Rule MF_00572

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00572

Sequence similarities

Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 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 – 5565562-isopropylmalate synthase HAMAP-Rule MF_00572
PRO_1000025031

Sequences

Sequence LengthMass (Da)Tools
Q48LY5 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: D5EF436B9D587FB9

FASTA55661,525
        10         20         30         40         50         60 
MTMLKDPSKK YRAFPTIDLP DRTWPSKTID AAPIWCSSDL RDGNQSLIEP MDAAKKLRFW 

        70         80         90        100        110        120 
KTLVSVGVKE IEASFPSASQ TDFDFVRTLI EDGHIPDDTT IQVLTQARED LIARTFESLR 

       130        140        150        160        170        180 
GAKKAIVHLY NATSPSFRRI VFNQDKAGVK EIAVNAAKLF VKYAAQQPET QWTFEYSPET 

       190        200        210        220        230        240 
FSATELEFAK EVCDAVIEVW NPTPENKVIL NLPATVEVAT PNIYADQIEW FGRNITRRDS 

       250        260        270        280        290        300 
VLISLHTHND RGTGVAATEL GLMAGADRVE GCLFGNGERT GNVDLVTVAL NLYTQGIDPE 

       310        320        330        340        350        360 
LDFSDIDGVR KVVEECNQIP VHPRHPYVGD LVHTAFSGSH QDAIRKGFTQ QKDGELWEVP 

       370        380        390        400        410        420 
YLPIDPADIG RSYEAVIRVN SQSGKGGITY LLEQEYGISL PRRMQIEFSQ VVQGETDRLG 

       430        440        450        460        470        480 
LEMSAQQIHS LLRREYLQAN TPYALISHKL QEENGNSAVD AEVHVDGETQ HWRGKGKGAL 

       490        500        510        520        530        540 
EALVAGLPVA VEIMDYNEHA IGSGTTAKAA AYIELRVNGE RAVHGVGIDE NITTASFRAL 

       550 
FSALNRSLSQ TQAKAA 

« Hide

References

[1]"Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola 1448A reveals divergence among pathovars in genes involved in virulence and transposition."
Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., Creasy T., Davidsen T.M., Haft D.H. expand/collapse author list , Zafar N., Zhou L., Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., Buell R.
J. Bacteriol. 187:6488-6498(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1448A / Race 6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000058 Genomic DNA. Translation: AAZ36794.1.
RefSeqYP_273587.1. NC_005773.3.

3D structure databases

ProteinModelPortalQ48LY5.
SMRQ48LY5. Positions 6-547.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264730.PSPPH_1329.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ36794; AAZ36794; PSPPH_1329.
GeneID3559420.
KEGGpsp:PSPPH_1329.
PATRIC19971781. VBIPseSyr78478_1396.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0119.
HOGENOMHOG000110941.
KOK01649.
OMAVERCNQI.
OrthoDBEOG62G5PZ.

Enzyme and pathway databases

BioCycPSAV264730:GKDE-1332-MONOMER.
UniPathwayUPA00048; UER00070.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00572. LeuA_type2.
InterProIPR013709. 2-isopropylmalate_synth_dimer.
IPR002034. AIPM/Hcit_synth_CS.
IPR013785. Aldolase_TIM.
IPR005668. IPM_Synthase.
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.
TIGRFAMsTIGR00970. leuA_yeast. 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_PSE14
AccessionPrimary (citable) accession number: Q48LY5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 13, 2005
Last modified: May 14, 2014
This is version 58 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