Reviewed, UniProtKB/Swiss-Prot P93832 (LEU32_ARATH)

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	405 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	leucine biosynthetic process Inferred from genetic interaction. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast envelope Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR
Molecular function	3-isopropylmalate dehydrogenase activity Inferred from genetic interaction. Source: TAIR NAD or NADH binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 33	33	Chloroplast Potential
	Chain	34 – 405	372	3-isopropylmalate dehydrogenase 2, chloroplastic		PRO_0000014454
Regions
	Nucleotide binding	116 – 129	14	NAD By similarity
	Nucleotide binding	322 – 334	13	NAD By similarity
Sites
	Metal binding	264	1	Magnesium or manganese By similarity
	Metal binding	288	1	Magnesium or manganese By similarity
	Metal binding	292	1	Magnesium or manganese By similarity
	Binding site	136	1	Substrate By similarity
	Binding site	146	1	Substrate By similarity
	Binding site	174	1	Substrate By similarity
	Binding site	264	1	Substrate By similarity
	Site	181	1	Important for catalysis By similarity
	Site	232	1	Important for catalysis By similarity
Experimental info
	Sequence conflict	177	1	T → K in AAL32519. Ref.3
	Sequence conflict	177	1	T → K in AAM47946. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P93832-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: D5E22968F19FC7DC	FASTA	405	43,371
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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. , 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. AY062441 mRNA. Translation: AAL32519.1. AY114627 mRNA. Translation: AAM47946.1.
IPI	IPI00522721.
PIR	F96837.
RefSeq	NP_178171.1.
UniGene	At.5371 Rra.8228 Rsa.3642 Rsa.7184
3D structure databases
SMR	P93832. Positions 43-400.
ModBase	Search...
Protein-protein interaction databases
STRING	P93832.
Proteomic databases
PRIDE	P93832.
Genome annotation databases
GeneID	844395.
GenomeReviews	Gene locus AT1G80560 in contig CT485782_GR.
KEGG	ath:AT1G80560.
NMPDR	fig|3702.1.peg.7645.
Organism-specific databases
TAIR	At1g80560.
Phylogenomic databases
eggNOG	KOG0786.
HOGENOM	HBG518924.
InParanoid	P93832.
OMA	NTAFGLY.
PhylomeDB	P93832.
Enzyme and pathway databases
BRENDA	1.1.1.85. 302.
Gene expression databases
ArrayExpress	P93832.
Genevestigator	P93832.
GermOnline	AT1G80560. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004429. Isopropylmalate_DH. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11835. IDH_IMDH_dimeric. 1 hit. PTHR11835:SF13. IPMDH. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR00169. leuB. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LEU32_ARATH

Accession

Primary (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:	February 9, 2010
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)