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P93832 (LEU32_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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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 2, chloroplastic
Short name=3-IPM-DH 2
Short name=IMDH 2
EC=1.1.1.85
Alternative name(s):
Beta-IPM dehydrogenase 2
Gene names
Name:IMDH2
Synonyms:IMDH
Ordered Locus Names:At1g80560
ORF Names:T21F11.11
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Catalytic activity

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

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.

Subunit structure

Homodimer By similarity.

Subcellular location

Plastid › chloroplast By similarity.

Sequence similarities

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Chloroplast Potential
Chain34 – 4053723-isopropylmalate dehydrogenase 2, chloroplastic
PRO_0000014454

Regions

Nucleotide binding116 – 12914NAD By similarity
Nucleotide binding322 – 33413NAD By similarity

Sites

Metal binding2641Magnesium or manganese By similarity
Metal binding2881Magnesium or manganese By similarity
Metal binding2921Magnesium or manganese By similarity
Binding site1361Substrate By similarity
Binding site1461Substrate By similarity
Binding site1741Substrate By similarity
Binding site2641Substrate By similarity
Site1811Important for catalysis By similarity
Site2321Important for catalysis By similarity

Experimental info

Sequence conflict1771T → K in AAL32519. Ref.4
Sequence conflict1771T → K in AAM47946. Ref.4

Secondary structure

1 .......................................................................... 405
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P93832 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: D5E22968F19FC7DC

FASTA40543,371
        10         20         30         40         50         60 
MAAALQTNIR TVKVPATFRA VSKQSLAPFR VRCAVASPGK KRYTITLLPG DGIGPEVVSI 

        70         80         90        100        110        120 
AKNVLQQAGS LEGVEFNFRE MPIGGAALDL VGVPLPEETI SAAKESDAVL LGAIGGYKWD 

       130        140        150        160        170        180 
NNEKHLRPEK GLLQIRAALK VFANLRPATV LPQLVDASTL KREVAEGVDL MVVRELTGGI 

       190        200        210        220        230        240 
YFGEPRGIKT NENGEEVGFN TEVYAAHEID RIARVAFETA RKRRGKLCSV DKANVLEASI 

       250        260        270        280        290        300 
LWRKRVTALA SEYPDVELSH MYVDNAAMQL VRDPKQFDTI VTNNIFGDIL SDEASMITGS 

       310        320        330        340        350        360 
IGMLPSASLS DSGPGLFEPI HGSAPDIAGQ DKANPLATIL SAAMLLKYGL GEEKAAKRIE 

       370        380        390        400 
DAVLVALNNG FRTGDIYSAG TKLVGCKEMG EEVLKSVDSQ VPASV

« Hide

References

« Hide 'large scale' references
[1]Salchert K.D.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y10216 mRNA. Translation: CAA71268.1.
AC018849 Genomic DNA. Translation: AAF27137.1.
CP002684 Genomic DNA. Translation: AEE36420.1.
AY062441 mRNA. Translation: AAL32519.1.
AY114627 mRNA. Translation: AAM47946.1.
IPIIPI00522721.
PIRF96837.
RefSeqNP_178171.1. NM_106704.3.
UniGeneAt.5371.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3R8WX-ray2.25A/B/C/D1-405[»]
ProteinModelPortalP93832.
SMRP93832. Positions 41-398.
ModBaseSearch...

Protein-protein interaction databases

IntActP93832. 1 interaction.
STRINGP93832.

Proteomic databases

PRIDEP93832.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G80560.1; AT1G80560.1; AT1G80560.
GeneID844395.
GenomeReviewsGene locus AT1G80560 in contig CT485782_GR.
KEGGath:AT1G80560.
NMPDRfig|3702.1.peg.7645.

Organism-specific databases

TAIRAt1g80560.

Phylogenomic databases

eggNOGKOG0786.
HOGENOMHBG518924.
InParanoidP93832.
OMALDKNNKG.
PhylomeDBP93832.
ProtClustDBCLSN2914436.

Gene expression databases

ArrayExpressP93832.
GenevestigatorP93832.
GermOnlineAT1G80560. Arabidopsis thaliana.

Family and domain databases

InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR004429. Isopropylmalate_DH.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
KOK00052.
PANTHERPTHR11835. IDH_IMDH_dimeric. 1 hit.
PTHR11835:SF13. IPMDH. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00169. LeuB. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLEU32_ARATH
AccessionPrimary (citable) accession number: P93832
Secondary accession number(s): Q540Z4, Q8W4P6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: May 1, 1997
Last modified: December 14, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

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