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Q58673 (LEUD_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Isopropylmalate/citramalate isomerase small subunit

EC=4.2.1.33
EC=4.2.1.35
Alternative name(s):
(R)-2-methylmalate dehydratase
(R)-citramalate dehydratase
3-isopropylmalate dehydratase
Alpha-isopropylmalate dehydratase
Citraconate hydratase
Isopropylmalate isomerase
Short name=IPMI
Maleate hydratase
Short name=Malease
EC=4.2.1.31
Gene names
Name:leuD
Ordered Locus Names:MJ1277
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Enzyme with broad specificity that catalyzes reversible hydroxyacid isomerizations via dehydration/hydration reactions. Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate, a step involved in leucine biosynthesis. Catalyzes the isomerization between 2-methylmalate and 3-methylmalate, via the formation of 2-methylmaleate (citraconate), a step involved in isoleucine biosynthesis. Also displays malease activity, i.e. catalyzes the hydration of maleate to form (R)-malate. Ref.2

Catalytic activity

(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate. Ref.2

(R)-2-methylmalate = 2-methylmaleate + H2O. Ref.2

2-methylmaleate + H2O = (2R,3S)-3-methylmalate. Ref.2

(R)-malate = maleate + H2O. Ref.2

Pathway

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

Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 2/3. HAMAP-Rule MF_01032

Subunit structure

Heterotetramer of 2 LeuC and 2 LeuD. The heterotetramer that can be formed in vitro between HacA and LeuD is inactive. Ref.2

Sequence similarities

Belongs to the LeuD family.

Biophysicochemical properties

Kinetic parameters:

KM=80 µM for 2-methylmaleate Ref.2

KM=810 µM for (R)-2-methylmalate

KM=1900 µM for racemic 2-isopropylmalate

KM=39 µM for racemic 3-isopropylmalate

KM=400 µM for maleate

Vmax=15 µmol/min/mg enzyme for 2-methylmaleate hydration reaction

Vmax=1.5 µmol/min/mg enzyme for (R)-2-methylmalate dehydration reaction

Vmax=4.2 µmol/min/mg enzyme for 2-isopropylmalate dehydration reaction

Vmax=1.8 µmol/min/mg enzyme for 3-isopropylmalate dehydration reaction

Vmax=34 µmol/min/mg enzyme for maleate hydration reaction

pH dependence:

Optimum pH is 7.5.

Temperature dependence:

Optimum temperature is 70 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168Isopropylmalate/citramalate isomerase small subunit HAMAP-Rule MF_01032
PRO_0000141937

Secondary structure

....................................... 168
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q58673 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A53C2CA883B6CCD7

FASTA16818,377
        10         20         30         40         50         60 
MRSIIKGRVW KFGNNVDTDA ILPARYLVYT KPEELAQFVM TGADPDFPKK VKPGDIIVGG 

        70         80         90        100        110        120 
KNFGCGSSRE HAPLGLKGAG ISCVIAESFA RIFYRNAINV GLPLIECKGI SEKVNEGDEL 

       130        140        150        160 
EVNLETGEIK NLTTGEVLKG QKLPEFMMEI LEAGGLMPYL KKKMAESQ 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii."
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. expand/collapse author list , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]"Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in Methanocaldococcus jannaschii."
Drevland R.M., Waheed A., Graham D.E.
J. Bacteriol. 189:4391-4400(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[3]"Crystal structure of LeuD from Methanococcus jannaschii."
Lee E.H., Cho Y.W., Hwang K.Y.
Biochem. Biophys. Res. Commun. 419:160-164(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB99283.1.
PIRD64459.
RefSeqNP_248273.1. NC_000909.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3VBAX-ray2.00A/B/C/D/E/F1-168[»]
ProteinModelPortalQ58673.
SMRQ58673. Positions 4-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ1277.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB99283; AAB99283; MJ_1277.
GeneID1452175.
KEGGmja:MJ_1277.

Phylogenomic databases

eggNOGCOG0066.
KOK01704.
OMAGFVIPYE.
ProtClustDBCLSK876515.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13648.
SABIO-RKQ58673.
UniPathwayUPA00047; UER00067.
UPA00048; 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 nameLEUD_METJA
AccessionPrimary (citable) accession number: Q58673
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names