Skip Header

Contribute Send feedback
Read comments (?) or add your own

P95313 (LEU3_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3-isopropylmalate dehydrogenase
EC=1.1.1.85
Alternative name(s):
3-IPM-DH
Beta-IPM dehydrogenase
Short name=IMDH
Gene names
Name:leuB
Ordered Locus Names:Rv2995c, MT3073
ORF Names:MTV012.09
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. HAMAP MF_01035

Catalytic activity

(2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH. HAMAP MF_01035

Cofactor

Binds 1 magnesium or manganese ion per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4. HAMAP MF_01035

Subunit structure

Homodimer. Ref.4

Subcellular location

Cytoplasm HAMAP MF_01035.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3363363-isopropylmalate dehydrogenase HAMAP MF_01035
PRO_0000083803

Regions

Nucleotide binding271 – 28313NAD By similarity

Sites

Metal binding2111Magnesium or manganese By similarity
Metal binding2351Magnesium or manganese By similarity
Metal binding2391Magnesium or manganese By similarity
Binding site871Substrate By similarity
Binding site971Substrate By similarity
Binding site1211Substrate By similarity
Binding site2111Substrate By similarity
Site1281Important for catalysis By similarity
Site1781Important for catalysis By similarity

Secondary structure

1 ......................................................... 336
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P95313 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: E78718100CCA5B42

FASTA33635,306
        10         20         30         40         50         60 
MKLAIIAGDG IGPEVTAEAV KVLDAVVPGV QKTSYDLGAR RFHATGEVLP DSVVAELRNH 

        70         80         90        100        110        120 
DAILLGAIGD PSVPSGVLER GLLLRLRFEL DHHINLRPAR LYPGVASPLS GNPGIDFVVV 

       130        140        150        160        170        180 
REGTEGPYTG NGGAIRVGTP NEVATEVSVN TAFGVRRVVA DAFERARRRR KHLTLVHKTN 

       190        200        210        220        230        240 
VLTFAGGLWL RTVDEVGECY PDVEVAYQHV DAATIHMITD PGRFDVIVTD NLFGDIITDL 

       250        260        270        280        290        300 
AAAVCGGIGL AASGNIDATR ANPSMFEPVH GSAPDIAGQG IADPTAAIMS VALLLSHLGE 

       310        320        330 
HDAAARVDRA VEAHLATRGS ERLATSDVGE RIAAAL

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the leuB genes from Mycobacterium bovis BCG and Mycobacterium tuberculosis."
Han M.Y., Son M.Y., Lee S.H., Kim J.K., Huh J.S., Kim J.H., Choe I.S., Chung T.W., Choe Y.K.
Biochem. Mol. Biol. Int. 41:657-663(1997) [PubMed: 9111927] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[3]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[4]"The high-resolution Structure of LeuB (Rv2995c) from Mycobacterium tuberculosis."
Singh R.K., Kefala G., Janowski R., Mueller-Dieckmann C., von Kries J.-P., Weiss M.S.
J. Mol. Biol. 346:1-11(2005) [PubMed: 15663922] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-336, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U78887 Genomic DNA. Translation: AAC45174.1.
BX842581 Genomic DNA. Translation: CAA16080.1.
AE000516 Genomic DNA. Translation: AAK47402.1.
PIRF70854.
RefSeqNP_217511.1. NC_000962.2.
NP_337588.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W0DX-ray1.65A/B/C/D2-336[»]
2G4OX-ray2.00A/B/C/D2-336[»]
ProteinModelPortalP95313.
SMRP95313. Positions 2-336.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000001783; EBMYCP00000001783; EBMYCG00000001781.
EBMYCT00000072772; EBMYCP00000070831; EBMYCG00000072767.
GeneID888182.
925200.
GenomeReviewsGene locus MT3073 in contig AE000516_GR.
Gene locus Rv2995c in contig AL123456_GR.
KEGGmtc:MT3073.
mtu:Rv2995c.
PATRIC18128524. VBIMycTub22151_3360.
TIGRMT3073.

Organism-specific databases

TubercuListRv2995c.

Phylogenomic databases

GeneTreeEBGT00050000016921.
HOGENOMHBG518924.
OMAAATIFMV.
PhylomeDBP95313.
ProtClustDBPRK03437.

Family and domain databases

HAMAPMF_01035. LeuB_type2.
[Tree]
InterProIPR023698. 3-isopropylmalate_DH_LeuB.
IPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
KOK00052.
PANTHERPTHR11835. IDH_IMDH_dimeric. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEU3_MYCTU
AccessionPrimary (citable) accession number: P95313
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: January 25, 2012
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents