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B0RP28 (LEU1_XANCB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:xcc-b100_0870
OrganismXanthomonas campestris pv. campestris (strain B100) [Complete proteome] [HAMAP]
Taxonomic identifier509169 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length520 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 – 5205202-isopropylmalate synthase HAMAP-Rule MF_01025
PRO_1000149334

Sequences

Sequence LengthMass (Da)Tools
B0RP28 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: A8879B31E2E509D9

FASTA52056,222
        10         20         30         40         50         60 
MNTTVSNQTP HIRIFDTTLR DGEQSPGCSM TPQQKLVMAR ALDALGVDII ETGFPASSYS 

        70         80         90        100        110        120 
DREAVAMMGR ELRRPTLAVL SRCLQADIEI SARALEAAAN PRLHVFLSTS PLHREHKLRM 

       130        140        150        160        170        180 
SREQVLESVH KHVTLARGYI DDIEFSAEDA TRTEEDFLAE VTRVAIAAGA TTINLPDTVG 

       190        200        210        220        230        240 
FTTPEEIRGM FSRLIASVEG AEKVIFSTHC HNDLGLAAAN SLAAIEGGAR QVECTINGIG 

       250        260        270        280        290        300 
ERAGNCALEE ITMALKVRGA FYNLDTAINT PRIVSTSQLL QRLVGMPVQR NKAVVGGNAF 

       310        320        330        340        350        360 
AHESGIHQHG MLRHRGTYEI MRPEDVGWES SQMVLGRHSG RAAVEQRLRA LGYLLEEDEA 

       370        380        390        400        410        420 
KLVFEQFKAL CEKQRVVTDA DLQALMQDAT VQEGYRLASM TISDVGSRAN ALVELSDPDG 

       430        440        450        460        470        480 
NRVAETAQGN GPVDALFGAL ASATGVKLEL DSYQVHSVGI GADARGEASL SVRHDGVEYE 

       490        500        510        520 
GTGTSKDIIE ASALAWLDVA NRLLRQRERG VVAGKTAAVA 

« Hide

References

[1]"The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis."
Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A.
J. Biotechnol. 134:33-45(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM920689 Genomic DNA. Translation: CAP50213.1.
RefSeqYP_001902275.1. NC_010688.1.

3D structure databases

ProteinModelPortalB0RP28.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING509169.xccb100_0870.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP50213; CAP50213; xcc-b100_0870.
GeneID6324730.
KEGGxca:xccb100_0870.
PATRIC24081569. VBIXanCam108527_0896.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0119.
KOK01649.
OMALSCHCHN.
OrthoDBEOG6CGCF3.
ProtClustDBPRK00915.

Enzyme and pathway databases

BioCycXCAM509169:GHW4-888-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_XANCB
AccessionPrimary (citable) accession number: B0RP28
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 47 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