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A1KTV6 (LEU1_NEIMF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:NMC1034
OrganismNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18) [Complete proteome] [HAMAP]
Taxonomic identifier272831 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length517 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 – 5175172-isopropylmalate synthase HAMAP-Rule MF_01025
PRO_1000149226

Sequences

Sequence LengthMass (Da)Tools
A1KTV6 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 97E99448542990D6

FASTA51755,425
        10         20         30         40         50         60 
MTQANRVIIF DTTLRDGEQS PGAAMTKEEK IRVARQLEKL GVDIIEAGFA AASPGDFEAV 

        70         80         90        100        110        120 
NAIAKTITKS TVCSLSRAIE RDIRQAGEAV APAPKKRIHT FIATSPIHME YKLKMKPKQV 

       130        140        150        160        170        180 
IEAAVKAVKI AREYTDDVEF SCEDALRSEI DFLAEICGAV IEAGATTINI PDTVGYSIPY 

       190        200        210        220        230        240 
KTEEFFRELI VKTPNGGKVV WSAHCHNDLG LAVANSLAAL KGGARQVECT VNGLGERAGN 

       250        260        270        280        290        300 
ASVEEIVMAL KVRHDLFGLE TGIDTTQIVP SSKLVSTITG YPVQPNKAIV GANAFSHESG 

       310        320        330        340        350        360 
IHQDGVLKHR ETYEIMSAES VGWATNRLSL GKLSGRNAFK TKLADLGIEL ESEEALNAAF 

       370        380        390        400        410        420 
ARFKELADKK REIFDEDLHA LVSDEMGSMN AESYKFISQK ISTETGEEPR ADIVFSIKGE 

       430        440        450        460        470        480 
EKRASATGSG PVDAIFKAIE SVAQSGATLQ IYSVNAVTQG TESQGETSVR LARGNRVVNG 

       490        500        510 
QGADTDVLVA TAKAYLSALS KLEFSAAKPK AQGSGTI 

« Hide

References

[1]"Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18."
Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., Quail M.A., Achtman M. expand/collapse author list , Barrell B.G., Saunders N.J., Parkhill J.
PLoS Genet. 3:230-240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700532 / DSM 15464 / FAM18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM421808 Genomic DNA. Translation: CAM10296.1.
RefSeqYP_975085.1. NC_008767.1.

3D structure databases

ProteinModelPortalA1KTV6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272831.NMC1034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM10296; CAM10296; NMC1034.
GeneID4675871.
KEGGnmc:NMC1034.
PATRIC20352013. VBINeiMen17609_1259.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0119.
HOGENOMHOG000046859.
KOK01649.
OMAWSVHCHN.
OrthoDBEOG6CGCF3.
ProtClustDBPRK00915.

Enzyme and pathway databases

BioCycNMEN272831:GJDX-999-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_NEIMF
AccessionPrimary (citable) accession number: A1KTV6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 6, 2007
Last modified: February 19, 2014
This is version 57 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