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D8MDJ3 (D8MDJ3_LEUGT) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 19. 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
Ordered Locus Names:LEGAS_0263
OrganismLeuconostoc gasicomitatum (strain DSM 15947 / CECT 5767 / JCM 12535 / LMG 18811 / TB1-10) [Complete proteome] [HAMAP] EMBL CBL90911.1
Taxonomic identifier762550 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Leuconostoc ›

Protein attributes

Sequence length460 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 SAAS SAAS004430

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 binding3391Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01026
Metal binding3991Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01026
Metal binding4021Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01026

Sequences

Sequence LengthMass (Da)Tools
D8MDJ3 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: 123845047F32D05E

FASTA46050,606
        10         20         30         40         50         60 
MSKTLFDKIW EKHVITGEIG EAQLIYVDLH LIHEVTSPQP FDGLRNTNRR VRRPDLTFAT 

        70         80         90        100        110        120 
MDHNVSTKDI FNVQDHMSRL QMDTLVKNTK EFGVPLASIG DDKQGIVHVV GPERGLTQPA 

       130        140        150        160        170        180 
KLIVCGDSHT ATHGAFGAIA FGIGTSEVEH VLATQTIWQV KPKTMGIKVT GKLLKNTYAK 

       190        200        210        220        230        240 
DIIMGIIAKY GVSFGVGYAI EFYGETVENL SMEARMTMCN MSIEAGSRTG MVQPDQTTFD 

       250        260        270        280        290        300 
YIEGREQAPK DFEAAKNYWL QFYTDDESDF DETLTFDVSN LKPMVTWGTN PGMATPVDQS 

       310        320        330        340        350        360 
LPAIKDDNDA NANAYEYIGL HPHMKATDIN LDYIFIGSCT NSRYEDLEIA ANMMKGHHLA 

       370        380        390        400        410        420 
PNVTAWIVPG SRAIRNRAIK SGIAKIFEDA GCEWREPGCS ACLAMNPDKI PAGKHVASTS 

       430        440        450        460 
NRNFIGRQGA GSRTHLASPA MVAAAGIAGY FVDITVDEFV

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References

[1]"Genome sequence and comparative genomics of a food spoilage lactic acid bacterium Leuconostoc gasicomitatum 18811T."
Johansson P., Paulin L., Vihavainen E.J., Salovuori N., Alatalo E.R., Bjoerkroth J.K., Auvinen P.
Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 15947 / CECT 5767 / JCM 12535 / LMG 18811 / TB1-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FN822744 Genomic DNA. Translation: CBL90911.1.
RefSeqYP_003771730.1. NC_014319.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCBL90911; CBL90911; LEGAS_0263.
GeneID9399465.
KEGGlgs:LEGAS_0263.
PATRIC42382166. VBILeuGas160647_0271.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000226972.
KOK01703.
OMADIRQGIV.

Enzyme and pathway databases

BioCycLGAS762550:GHH1-1424-MONOMER.
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 nameD8MDJ3_LEUGT
AccessionPrimary (citable) accession number: D8MDJ3
Entry history
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: May 1, 2013
This is version 19 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