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D1B363 (D1B363_SULD5) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 27. 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 small subunit HAMAP-Rule MF_01032

EC=4.2.1.33 HAMAP-Rule MF_01032
Alternative name(s):
Alpha-IPM isomerase HAMAP-Rule MF_01032
Isopropylmalate isomerase HAMAP-Rule MF_01032
Gene names
Name:leuD HAMAP-Rule MF_01032
Ordered Locus Names:Sdel_1517 EMBL ACZ12533.1
OrganismSulfurospirillum deleyianum (strain ATCC 51133 / DSM 6946 / 5175) [Complete proteome] [HAMAP] EMBL ACZ12533.1
Taxonomic identifier525898 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeSulfurospirillum

Protein attributes

Sequence length162 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_01032

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. HAMAP-Rule MF_01032

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP-Rule MF_01032

Subunit structure

Heterodimer of LeuC and LeuD By similarity. HAMAP-Rule MF_01032

Sequence similarities

Belongs to the LeuD family. LeuD type 2 subfamily. HAMAP-Rule MF_01032

Sequences

Sequence LengthMass (Da)Tools
D1B363 [UniParc].

Last modified January 19, 2010. Version 1.
Checksum: A1CDB15E64202D1E

FASTA16217,579
        10         20         30         40         50         60 
MSTISGKVWC FGDNIDTDLI IAARYLNTSD PKELAKHVME DADPEFAKKV GEGDIIVAGE 

        70         80         90        100        110        120 
NFGCGSSREH APIALKAAGV SAVVAKSFAR IFYRNAFNTG LPIFELPNTE AIQEGESIAI 

       130        140        150        160 
SMESGEITHG SKTYKFTPIP PFMQELLDAG GLMNYAQKEM KK 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001816 Genomic DNA. Translation: ACZ12533.1.
RefSeqYP_003304568.1. NC_013512.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACZ12533; ACZ12533; Sdel_1517.
GeneID8593057.
KEGGsdl:Sdel_1517.
PATRIC32483835. VBISulDel109514_1540.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000222940.
KOK01704.
OMAGFVIPYE.
OrthoDBEOG6PZXB8.

Enzyme and pathway databases

BioCycSDEL525898:GHVA-1548-MONOMER.
UniPathwayUPA00048; UER00071.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
HAMAPMF_01032. LeuD_type2.
InterProIPR015937. Acoase/IPM_deHydtase.
IPR015928. Aconitase/3IPM_dehydase_swvl.
IPR000573. AconitaseA/IPMdHydase_ssu_swvl.
IPR011827. IsopropMal_deHydtase_ssu.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PfamPF00694. Aconitase_C. 1 hit.
[Graphical view]
SUPFAMSSF52016. SSF52016. 1 hit.
TIGRFAMsTIGR02087. LEUD_arch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD1B363_SULD5
AccessionPrimary (citable) accession number: D1B363
Entry history
Integrated into UniProtKB/TrEMBL: January 19, 2010
Last sequence update: January 19, 2010
Last modified: February 19, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)