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B7JYP4 (LEU1_CYAP8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 34. 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:PCC8801_0832
OrganismCyanothece sp. (strain PCC 8801) (Synechococcus sp. (strain PCC 8801 / RF-1)) [Complete proteome] [HAMAP]
Taxonomic identifier41431 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Cyanothece

Protein attributes

Sequence length536 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 – 5365362-isopropylmalate synthase HAMAP-Rule MF_01025
PRO_1000149174

Sequences

Sequence LengthMass (Da)Tools
B7JYP4 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 43198448585700A2

FASTA53658,285
        10         20         30         40         50         60 
MSNQPDRIII FDTTLRDGEQ SPGASLTVEE KLTIARSLAR LGVDIIEAGF PYASPGDFEA 

        70         80         90        100        110        120 
VQKIAQTVGT EDGPRICGLA RATQKDIQTA AEAVKPAAKG RIHTFLATSD IHLQYKLKKT 

       130        140        150        160        170        180 
RQEVLAIVPD MVAYAKSLVD DVEFSPEDAG RSDPEFLYQV LERAIAAGAT TINIPDTVGY 

       190        200        210        220        230        240 
TTPSEFGALI GGIKQNVPNI DQAIISVHGH NDLGLAVANF LEAVKNGARQ LECTINGIGE 

       250        260        270        280        290        300 
RAGNAALEEL VMALHVRRQY FNPFLGRPPE STEPLTNINT KEIYRTSRLV SQLTGMMVQP 

       310        320        330        340        350        360 
NKAIVGKNAF AHESGIHQDG VLKNKLTYEI MDAESIGLTH NQIVLGKLSG RNAFRTRLKE 

       370        380        390        400        410        420 
LGFELSDTEI NNAFLRFKEV ADKKKEITDW DLAAIVNDEM QQAPELFRLE LVQVSCGDHA 

       430        440        450        460        470        480 
CPTATVTLRT PDGQELTDAA IGTGPVDAVY KAINRVVQVP NELIEFSVKS VTAGIDAMGE 

       490        500        510        520        530 
VTIRLRYEDK IYSGYAANTD IITASARAYI SALNRLYGSI QDQSATEVTK SEVAAI

« Hide

References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 8801.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001287 Genomic DNA. Translation: ACK64914.1.
RefSeqYP_002371070.1. NC_011726.1.

3D structure databases

ProteinModelPortalB7JYP4.
ModBaseSearch...

Protein-protein interaction databases

STRING41431.PCC8801_0832.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK64914; ACK64914; PCC8801_0832.
GeneID7103172.
KEGGcyp:PCC8801_0832.
PATRIC21573874. VBICyaSp125535_0975.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0119.
HOGENOMHOG000046859.
KOK01649.
OMARDTRINT.
ProtClustDBPRK00915.

Enzyme and pathway databases

BioCycCSP41431:GHLK-850-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_CYAP8
AccessionPrimary (citable) accession number: B7JYP4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: May 1, 2013
This is version 34 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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