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A0RQK7 (LEU1_CAMFF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:CFF8240_1344
OrganismCampylobacter fetus subsp. fetus (strain 82-40) [Complete proteome] [HAMAP]
Taxonomic identifier360106 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter ›

Protein attributes

Sequence length506 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.

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: HAMAP

   Molecular_function2-isopropylmalate synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5065062-isopropylmalate synthase HAMAP-Rule MF_01025
PRO_1000149159

Sequences

Sequence LengthMass (Da)Tools
A0RQK7 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: EA0FBEE7E49F01E2

FASTA50654,896
        10         20         30         40         50         60 
MDNNKIIVFD TTLRDGEQSP GASMNTEEKI QIALQLERLG VDVMEAGFAA ASPGDFDAIN 

        70         80         90        100        110        120 
QIAKQIHSIR IASLARALEK DIKAAGEAIS PAKNRRIHTF IATSPIHMEH KLKMTPDEVI 

       130        140        150        160        170        180 
KRAVEAVKYA KTFVDDVEFS CEDAGRSDIV FLKEICAAVV EAGARTLNLP DTVGFRMPDE 

       190        200        210        220        230        240 
IYNMVKSMVD FIGDRAIISV HNHNDLGLAV ANTLASIKAG ARQVECTING LGERAGNAAL 

       250        260        270        280        290        300 
EEIVMTIRTR SDEFAPLYTD IVTKEIYATS RLVASITGIE PQPNKAIVGK NAFAHESGIH 

       310        320        330        340        350        360 
QDGMLKCAQT YEIIKAEDIG AEKNSLVLGK HSGRHAFKDK LINLGFDLDD NEINEAFIKF 

       370        380        390        400        410        420 
KELCDKKKEI FDDDIRALVS HEIIKIPEIY SIQTLSTSSC NAGHSSAAVS IKFSDNIISD 

       430        440        450        460        470        480 
AALGNGTADA IFKVIDRISG ISGELKDYKV NAVSQGKDAL AKITVKVVFE GSSCATIGHG 

       490        500 
LDIDTMMASA KAYVSALNSY LSMKNR

« Hide

References

[1]"Sequence of Campylobacter fetus subsp. fetus 82-40."
Fouts D.E., Nelson K.E.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 82-40.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000487 Genomic DNA. Translation: ABK82096.1.
RefSeqYP_892490.1. NC_008599.1.

3D structure databases

ProteinModelPortalA0RQK7.
ModBaseSearch...

Protein-protein interaction databases

STRING360106.CFF8240_1344.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK82096; ABK82096; CFF8240_1344.
GeneID4539073.
KEGGcff:CFF8240_1344.
PATRIC20037206. VBICamFet25865_1308.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0119.
HOGENOMHOG000046859.
KOK01649.
OMAVWSVHCH.
ProtClustDBPRK00915.

Enzyme and pathway databases

BioCycCFET360106:GHTH-1359-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. 2-isopropylmalate_synth_dimer. 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_CAMFF
AccessionPrimary (citable) accession number: A0RQK7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: January 9, 2007
Last modified: May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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