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C5D5M0 (LEU1_GEOSW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:GWCH70_2593
OrganismGeobacillus sp. (strain WCH70) [Complete proteome] [HAMAP]
Taxonomic identifier471223 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length515 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 – 5155152-isopropylmalate synthase HAMAP-Rule MF_01025
PRO_1000213314

Sequences

Sequence LengthMass (Da)Tools
C5D5M0 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: BD59459DE3FDC9BB

FASTA51556,758
        10         20         30         40         50         60 
MRKINIFDTT LRDGEQSAGI NLNLQEKLEI ARQLERLGVD IIEAGFPASS KGDFQAVKQI 

        70         80         90        100        110        120 
AETIKTCSVT GLARSVQSDI DAAWEALKGG AEPRLHLFIA TSPIHMKYKL QMTPEQVIET 

       130        140        150        160        170        180 
AVESVKYAKR YFPIVQWSAE DACRSELPFL AKIITEVIKA GATVINIPDT VGYITPKEYG 

       190        200        210        220        230        240 
NIFTFLSNNV PNIEKVSLSA HCHDDLGMAV ANSLAAIEHG ATQIEGTING IGERAGNAAL 

       250        260        270        280        290        300 
EEIAVALYIR KDYYQAETRL NLQEIKRTSN LVSKLTGVVI PPNKAVIGKN AFAHESGIHQ 

       310        320        330        340        350        360 
DGVLKEKTTY EIISPELVGV QSNSMVLGKH SGRHALRNRV EELGYTLSDE EVNKLFVRFK 

       370        380        390        400        410        420 
ELADKKKDIT DDDLVALIFE EKFDHFKDFY QLSSLQVQYG TNQIPTAVVV LKDGQGNEIQ 

       430        440        450        460        470        480 
EAATGAGSVE ALYNTLERCF KTSVTLLDYR IESVSGGRDA LAQVFVKVRV NDIETSGRGT 

       490        500        510 
AQDVLEASAK AYINAVNRVF MIETMRAENQ KVAMQ 

« Hide

References

[1]"Complete sequence of chromosome of Geopacillus sp. WCH70."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Brumm P., Mead D.A., Richardson P.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WCH70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001638 Genomic DNA. Translation: ACS25288.1.
RefSeqYP_002950554.1. NC_012793.1.

3D structure databases

ProteinModelPortalC5D5M0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING471223.GWCH70_2593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS25288; ACS25288; GWCH70_2593.
GeneID7976353.
KEGGgwc:GWCH70_2593.
PATRIC21974248. VBIGeoSp101709_2726.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0119.
HOGENOMHOG000046859.
KOK01649.
OMALSCHCHN.
OrthoDBEOG6CGCF3.
ProtClustDBPRK00915.

Enzyme and pathway databases

BioCycGSP471223:GH2C-2688-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_GEOSW
AccessionPrimary (citable) accession number: C5D5M0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 37 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