Reviewed, UniProtKB/Swiss-Prot P29102 (LEU3_BRANA)

Names and origin

Protein names	Recommended name:     3-isopropylmalate dehydrogenase, chloroplastic       Short name=3-IPM-DH       Short name=IMDH     EC=1.1.1.85 Alternative name(s):     Beta-IPM dehydrogenase
Organism	Brassica napus (Rape)
Taxonomic identifier	3708 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Brassica

Protein attributes

Sequence length	406 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.
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
Gene Ontology (GO)
Biological process	leucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-isopropylmalate dehydrogenase activity Inferred from electronic annotation. Source: EC 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 – 34	34	Chloroplast Potential
	Chain	35 – 406	372	3-isopropylmalate dehydrogenase, chloroplastic		PRO_0000014456
Regions
	Nucleotide binding	117 – 130	14	NAD By similarity
	Nucleotide binding	323 – 335	13	NAD By similarity
Sites
	Metal binding	265	1	Magnesium or manganese By similarity
	Metal binding	289	1	Magnesium or manganese By similarity
	Metal binding	293	1	Magnesium or manganese By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	147	1	Substrate By similarity
	Binding site	175	1	Substrate By similarity
	Binding site	265	1	Substrate By similarity
	Site	182	1	Important for catalysis By similarity
	Site	233	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P29102-1 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 2C8CCEA3B28FF192	FASTA	406	43,351
	10 20 30 40 50 60 MAAALQTNIR PVKFPATLRA LTKQSSPAPF RVRCAAASPG KKRYNITLLP GDGIGPEVIS 70 80 90 100 110 120 IAKNVLQQAG SLEGLEFSFQ EMPVGGAALD LVGVPLPEET VSAAKESDAV LLGAIGGYKW 130 140 150 160 170 180 DKNEKHLKPE TGLLQLRAGL KVFANLRPAT VLPQLVDAST LKREVAEGVD LMVVRELTGG 190 200 210 220 230 240 IYFGVPRGIK TNENGEEVGY NTEVYAAHEI DRIARVAFET ARKRRGKLCS VDKANVLDAS 250 260 270 280 290 300 ILWRRRVTAL AAEYPDVELS HMYVDNAAMQ LVRDPKQFDT IVTNNIFGDI LSDEASMITG 310 320 330 340 350 360 SIGMLPSASL SDSGPGLFEP IHGSAPDIAG QDKANPLATI LSAAMLLKYG LGEEKAAKRI 370 380 390 400 EDAVLGALNK GFRTGDIYSA GTKLVGCKEM GEEVLKSVDS HVQASV

References

[1]	"Cloning of a cDNA for rape chloroplast 3-isopropylmalate dehydrogenase by genetic complementation in yeast." Ellerstroem M., Josefsson L.G., Rask L., Ronne H. Plant Mol. Biol. 18:557-566(1992) [PubMed: 1371407] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Svalofs Karat 20516-K.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X59970 mRNA. Translation: CAA42596.1.
PIR	S20510.
3D structure databases
SMR	P29102. Positions 44-399.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.85. 393.
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

LEU3_BRANA

Accession

Primary (citable) accession number: P29102

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	February 9, 2010
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)