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C5ARS7 (C5ARS7_METEA) Unreviewed, UniProtKB/TrEMBL

Last modified April 3, 2013. Version 30. 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:
3-isopropylmalate dehydratase large subunit HAMAP-Rule MF_01026
EC=4.2.1.33 HAMAP-Rule MF_01026
Alternative name(s):
Alpha-IPM isomerase HAMAP-Rule MF_01026
Isopropylmalate isomerase HAMAP-Rule MF_01026
Gene names
Name:leuC HAMAP-Rule MF_01026 EMBL ACS42415.1
Ordered Locus Names:MexAM1_META1p4800 EMBL ACS42415.1
OrganismMethylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1) [Complete proteome] [HAMAP] EMBL ACS42415.1
Taxonomic identifier272630 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium ›

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate By similarity. HAMAP-Rule MF_01026 SAAS SAAS004430

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. HAMAP-Rule MF_01026

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP-Rule MF_01026 SAAS SAAS015931

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01026 SAAS SAAS004430

Subunit structure

Heterodimer of LeuC and LeuD By similarity. HAMAP-Rule MF_01026 SAAS SAAS004430

Sequence similarities

Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily. HAMAP-Rule MF_01026

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding3491Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01026
Metal binding4091Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01026
Metal binding4121Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01026

Sequences

Sequence LengthMass (Da)Tools
C5ARS7 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 452ABBF400B1D35E

FASTA46950,620
        10         20         30         40         50         60 
MTAPRTLYDK IWDDHVVDVE PDGSALLYID RHLVHEVTSP QAFEGLRVAG RTVRAPHKTL 

        70         80         90        100        110        120 
AVVDHNVQTS DRSKGIEDPE SRTQLEALAE NVRDFGIEFY DALDQRQGIV HIIGPEQGFT 

       130        140        150        160        170        180 
LPGQTIVCGD SHTSTHGAFG ALAHGIGTSE VEHVLATQTL IQRKAKNMRV TVDGTLPRGV 

       190        200        210        220        230        240 
SAKDIVLAII GEIGTAGGTG HVIEYAGEAI RALSMEGRMT ICNMSIEGGA RAGMVAPDET 

       250        260        270        280        290        300 
TYAYVKGRPK APKGAAFDAA RRYWESLATD EGAHFDREIR LDAANLPPLV SWGTSPEDIV 

       310        320        330        340        350        360 
SILGTVPDPA QIADENKRQS KEKALAYMGL TPGTRMTDVT LDRVFIGSCT NGRIEDLRIV 

       370        380        390        400        410        420 
AKMVEGRKVH DSVSAMVVPG SGLVKAQAEA EGIDRILKDA GFDWREPGCS MCLGMNPDKL 

       430        440        450        460 
RPGERCASTS NRNFEGRQGP RGRTHLVSPA MAAAAAVAGR FVDIREWRG

« Hide

References

[1]"Methylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources."
Vuilleumier S., Chistoserdova L., Lee M.C., Bringel F., Lajus A., Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E. expand/collapse author list , Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C., Lidstrom M.E.
PLoS ONE 4:E5584-E5584(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14718 / DSM 1338 / AM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001510 Genomic DNA. Translation: ACS42415.1.
RefSeqYP_002965692.1. NC_012808.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING272630.MexAM1_META1p4800.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS42415; ACS42415; MexAM1_META1p4800.
GeneID7994573.
KEGGmea:Mex_1p4800.
PATRIC22515241. VBIMetExt101010_4672.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0065.
HOGENOMHOG000226972.
KOK01703.
OMADIRQGIV.
ProtClustDBPRK05478.

Enzyme and pathway databases

UniPathwayUPA00048; UER00071.

Family and domain databases

Gene3D3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
HAMAPMF_01026. LeuC_type1.
InterProIPR004430. 3-IsopropMal_deHydase_lsu.
IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PfamPF00330. Aconitase. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR00170. leuC. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC5ARS7_METEA
AccessionPrimary (citable) accession number: C5ARS7
Entry history
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: April 3, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info