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D2BHR4 (D2BHR4_DEHSV) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 24. 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_01027
EC=4.2.1.33 HAMAP-Rule MF_01027
Alternative name(s):
Alpha-IPM isomerase HAMAP-Rule MF_01027
Isopropylmalate isomerase HAMAP-Rule MF_01027
Gene names
Name:leuC HAMAP-Rule MF_01027 EMBL ACZ61864.1
Ordered Locus Names:DhcVS_732
OrganismDehalococcoides sp. (strain VS) [Complete proteome] [HAMAP]
Taxonomic identifier311424 [NCBI]
Taxonomic lineageBacteria › Chloroflexi › Dehalococcoidetes › Dehalococcoidales › Dehalococcoidaceae › Dehalococcoides ›

Protein attributes

Sequence length417 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_01027

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. HAMAP-Rule MF_01027

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP-Rule MF_01027 SAAS SAAS015931

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01027

Subunit structure

Heterodimer of LeuC and LeuD By similarity. HAMAP-Rule MF_01027

Sequence similarities

Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily. HAMAP-Rule MF_01027

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding2981Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01027
Metal binding3581Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01027
Metal binding3611Iron-sulfur (4Fe-4S) By similarity HAMAP-Rule MF_01027

Sequences

Sequence LengthMass (Da)Tools
D2BHR4 [UniParc].

Last modified February 9, 2010. Version 1.
Checksum: D28A3BE8FF36517D

FASTA41744,725
        10         20         30         40         50         60 
MMNLVEKILA AHSGKTQVSP GDFINAKVDL VLANDITAPI AVKEFKKIGV SKVFDPKKIV 

        70         80         90        100        110        120 
FVPDHFVPNK DIASAEQVKM VREFAREQGI LFFECGKMGV EHVILHEQGL VLPGDIVVGA 

       130        140        150        160        170        180 
DSHTCTYGAL GAFTTGMGST DIAAAMATGE VWMKVPPTIK FNYTGKLPKW IGGKDLILFT 

       190        200        210        220        230        240 
IGQIGVDGAL YSAMYFCGEA IDALSMENRF TMSNMAIEAG GKAGLFRVDE KTLEYVTPRA 

       250        260        270        280        290        300 
KRQYTVYDND ADASYAKTYN FDISKLEPQV SLPHSPANAR PISQIGKIKV DQVIIGSCTN 

       310        320        330        340        350        360 
GRLEDLAISA KLLEVNKVNP DLRTIVIPGS QQVYLDALKA GYIETFINAG VAVSTPTCGP 

       370        380        390        400        410 
CLGGHMGILA AGERCLATTN RNFVGRMGSP KSEVYLAGPA VAAATAIKGY IAHPDEI

« Hide

References

[1]"Localized plasticity in the streamlined genomes of vinyl chloride respiring Dehalococcoides."
McMurdie P.J., Behrens S.F., Muller J.A., Goke J., Ritalahti K.M., Wagner R., Goltsman E., Lapidus A., Holmes S., Loffler F.E., Spormann A.M.
PLoS Genet. 5:E1000714-E1000714(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001827 Genomic DNA. Translation: ACZ61864.1.
RefSeqYP_003330192.1. NC_013552.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACZ61864; ACZ61864; DhcVS_732.
GeneID8657665.
KEGGdev:DhcVS_732.
PATRIC32058362. VBIDehSp95780_0695.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000226971.
KOK01703.
OMALVCPDSH.

Enzyme and pathway databases

BioCycDSP311424:GJ8J-707-MONOMER.
UniPathwayUPA00048; UER00071.

Family and domain databases

Gene3D3.30.499.10. 2 hits.
3.40.1060.10. 1 hit.
HAMAPMF_01027. LeuC_type2.
InterProIPR015931. 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.
IPR011826. HAcnase/IPMdehydase_lsu_prok.
IPR006251. Homoacnase/IPMdehydase_lsu.
IPR011823. IsopropMal_deHydtase_lsu_bac.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF6. PTHR11670:SF6. 1 hit.
PfamPF00330. Aconitase. 2 hits.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR01343. hacA_fam. 1 hit.
TIGR02086. IPMI_arch. 1 hit.
TIGR02083. LEU2. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD2BHR4_DEHSV
AccessionPrimary (citable) accession number: D2BHR4
Entry history
Integrated into UniProtKB/TrEMBL: February 9, 2010
Last sequence update: February 9, 2010
Last modified: May 1, 2013
This is version 24 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