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G0FKP2 (G0FKP2_AMYMD) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
2-isopropylmalate synthase HAMAP-Rule MF_00572

EC=2.3.3.13 HAMAP-Rule MF_00572
Alternative name(s):
Alpha-IPM synthase HAMAP-Rule MF_00572
Alpha-isopropylmalate synthase HAMAP-Rule MF_00572
Gene names
Name:leuA HAMAP-Rule MF_00572 EMBL AFO82283.1
ORF Names:AMES_8751 EMBL AFO82283.1, RAM_45590 EMBL AEK47583.1
OrganismAmycolatopsis mediterranei S699 EMBL AEK47583.1
Taxonomic identifier713604 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeAmycolatopsis

Protein attributes

Sequence length561 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_00572

Catalytic activity

Acetyl-CoA + 3-methyl-2-oxobutanoate + H2O = (2S)-2-isopropylmalate + CoA. SAAS SAAS005668 HAMAP-Rule MF_00572

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4. SAAS SAAS002034 HAMAP-Rule MF_00572

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00572

Sequence similarities

Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. HAMAP-Rule MF_00572

Sequences

Sequence LengthMass (Da)Tools
G0FKP2 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: 75344EEE767F198B

FASTA56162,838
        10         20         30         40         50         60 
MPVHRYRPWY DVVENIDLPD RTWPEKRIDR APLWCAVDLR DGNQALIDPM SPARKRKFFD 

        70         80         90        100        110        120 
LLVRMGYKEI EVGFPAASQT DFDFVREIIE EHAIPDDVSI QVLTQCRPEL IERTFKSLEG 

       130        140        150        160        170        180 
APRAIVHIYN STSILQRRVV FREEREGIKK IATQAAEMVV ELAAKQPDTD FRFQYSPESY 

       190        200        210        220        230        240 
TGTELSYALE VCNAVTEIWQ PTPEKPVILN LPATVEMATP NVYADSIEWM SRNLDRRDSV 

       250        260        270        280        290        300 
ILSLHPHNDR GTGIAAAELG YQAGADRIEG CLFGNGERTG NVDLVALGMN LYSQGIDPQI 

       310        320        330        340        350        360 
DFSDMDEIKR TVEYCNQLPV GERSPWGGDL VFTAFSGSHQ DAINKGLDAL KDAADKAGVP 

       370        380        390        400        410        420 
IDEYPWEVPY LPIDPKDVGR MYEAVIRVNS QSGKGGVAYI MKAEHQLDLP RRLQIEFSKV 

       430        440        450        460        470        480 
IQRYTDTEGG EVDPATMYNA FSAEYLELKT PLELVRQHVR DNGDGEYDIT ATVKVEGDEH 

       490        500        510        520        530        540 
EVTGRGNGPI AAFFDALSTV GFDLRLLDYN EHTLSPGDDA RAASYIECAI SDRVFWGIGI 

       550        560 
DPSIVTASLR AVVSAVNRAN R 

« Hide

References

[1]"Whole Genome Sequence of the Rifamycin B-Producing Strain Amycolatopsis mediterranei S699."
Verma M., Kaur J., Kumar M., Kumari K., Saxena A., Anand S., Nigam A., Ravi V., Raghuvanshi S., Khurana P., Tyagi A.K., Khurana J.P., Lal R.
J. Bacteriol. 193:5562-5563(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: S699 EMBL AEK47583.1.
[2]"Complete Genome Sequence of Amycolatopsis mediterranei S699 Based on De Novo Assembly via a Combinatorial Sequencing Strategy."
Tang B., Zhao W., Zheng H., Zhuo Y., Zhang L., Zhao G.P.
J. Bacteriol. 194:5699-5700(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: S699 EMBL AFO82283.1.
[3]Biao T.
Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: S699 EMBL AFO82283.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002896 Genomic DNA. Translation: AEK47583.1.
CP003729 Genomic DNA. Translation: AFO82283.1.
RefSeqYP_005537040.1. NC_017186.1.
YP_006555228.1. NC_018266.1.

3D structure databases

ProteinModelPortalG0FKP2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEK47583; AEK47583; RAM_45590.
AFO82283; AFO82283; AMES_8751.
GeneID12125827.
13409574.
KEGGamm:AMES_8751.
amn:RAM_45590.

Phylogenomic databases

KOK01649.

Enzyme and pathway databases

UniPathwayUPA00048; UER00070.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00572. LeuA_type2.
InterProIPR013709. 2-isopropylmalate_synth_dimer.
IPR002034. AIPM/Hcit_synth_CS.
IPR013785. Aldolase_TIM.
IPR005668. IPM_Synthase.
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.
TIGRFAMsTIGR00970. leuA_yeast. 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 nameG0FKP2_AMYMD
AccessionPrimary (citable) accession number: G0FKP2
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: April 3, 2013
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)