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B2V7R0 (B2V7R0_SULSY) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 41. 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:SYO3AOP1_0338 EMBL ACD65983.1
OrganismSulfurihydrogenibium sp. (strain YO3AOP1) [Complete proteome] [HAMAP] EMBL ACD65983.1
Taxonomic identifier436114 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesHydrogenothermaceaeSulfurihydrogenibium

Protein attributes

Sequence length165 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
B2V7R0 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 345698F080CC802A

FASTA16518,146
        10         20         30         40         50         60 
MIRGRVWKFK DDVDTDQIIP ARYLVTTDPK ELAKHVMEDA DPTFPSKVKE GDILVAGKNF 

        70         80         90        100        110        120 
GCGSSREHAP LAIKGAGIAA VVAESFARIF FRNAINLGLL IIESPEAARE AEEGDILEID 

       130        140        150        160 
INQGVIRNVT KNKEYKIKPL PENLQAILKA GGLMEYAKEK IKNAS 

« Hide

References

[1]"Complete and draft genome sequences of six members of the Aquificales."
Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S., Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.
J. Bacteriol. 191:1992-1993(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YO3AOP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001080 Genomic DNA. Translation: ACD65983.1.
RefSeqYP_001930537.1. NC_010730.1.

3D structure databases

ProteinModelPortalB2V7R0.
SMRB2V7R0. Positions 1-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436114.SYO3AOP1_0338.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD65983; ACD65983; SYO3AOP1_0338.
GeneID6332711.
KEGGsul:SYO3AOP1_0338.
PATRIC23765383. VBISulSp94719_0350.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0066.
HOGENOMHOG000222940.
KOK01704.
OMAYCMEDAR.
OrthoDBEOG6PZXB8.
ProtClustDBCLSK2338684.

Enzyme and pathway databases

BioCycSSP436114:GI6I-354-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.
IPR011824. IsopropMal_deHydtase_ssu_bac.
[Graphical view]
PANTHERPTHR11670. PTHR11670. 1 hit.
PfamPF00694. Aconitase_C. 1 hit.
[Graphical view]
SUPFAMSSF52016. SSF52016. 1 hit.
TIGRFAMsTIGR02084. leud. 1 hit.
TIGR02087. LEUD_arch. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB2V7R0_SULSY
AccessionPrimary (citable) accession number: B2V7R0
Entry history
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: April 16, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)