Reviewed, UniProtKB/Swiss-Prot Q9SA14 (LEU31_ARATH)

Names and origin

Protein names

Recommended name:
    3-isopropylmalate dehydrogenase 1, chloroplastic
      Short name=3-IPM-DH 1
      Short name=IMDH 1
    EC=1.1.1.85
Alternative name(s):
    Beta-IPM dehydrogenase 1

Gene names

Name:	IMDH1
Ordered Locus Names:	At1g31180
ORF Names:	F28K20.14

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 › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 caution	The sequence AAD21684.1 differs from that shown. Reason: Erroneous gene model prediction.

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 response to salt stress Inferred from expression pattern. Source: TAIR
Cellular component	chloroplast stroma Inferred from direct assay. Source: TAIR thylakoid 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 – 34	34	Chloroplast Potential
	Chain	35 – 404	370	3-isopropylmalate dehydrogenase 1, chloroplastic		PRO_0000014453
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)
	Q9SA14-1 [UniParc]. Last modified June 12, 2007. Version 2. Checksum: D0A7E06E85AC40D0	FASTA	404	43,847
	10 20 30 40 50 60 MAAFLQTNIR LEIIPGRYSS LTDHKFRAPY RIRCAAASPV KKRYNITLLP GDGIGPEVIS 70 80 90 100 110 120 VAKNVLQKAG FLQGLEFDFQ EMPFGGAALD LVGVPLPEET STAAKQSDAI LLGAIGGYKW 130 140 150 160 170 180 DKNEKHLRPE MGLLNIRRDL NVFANLRPAT VLPQLVDAST LKKEVAQGVD MMIVRELTGG 190 200 210 220 230 240 IYFGEPRGIT INENGEEVGF NTEIYAAHEI DRIARVAFET ARKRRGKLCS VDKANVLDAS 250 260 270 280 290 300 ILWRKRVTAL ASEYPDVELS HMYVDNAAMQ LVRDPKQFDT IVTNNIFGDI LSDEASMITG 310 320 330 340 350 360 SIGMLPSASL GESGPGLFEP IHGSAPDIAG QDKANPLATI LSAAMLLKYG LGEEKAAKMI 370 380 390 400 EDAVVDALNK GFRTGDIYSP GNKLVGCKEM GEEVLKSVDS KVPV

References

[1]	"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.
[2]	"Arabidopsis ORF clones." Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC004793 Genomic DNA. Translation: AAD21684.1. Sequence problems. BT025974 mRNA. Translation: ABG25063.1.
IPI	IPI00544447.
PIR	H86437.
RefSeq	NP_174403.1.
UniGene	At.40403
3D structure databases
HSSP	HSSP built from PDB template 1A05 based on UniProtKB Q56268.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9SA14. 1 interaction.
STRING	Q9SA14.
Proteomic databases
PRIDE	Q9SA14.
ProMEX	Q9SA14.
Genome annotation databases
GeneID	840006.
GenomeReviews	Gene locus AT1G31180 in contig CT485782_GR.
KEGG	ath:AT1G31180.
NMPDR	fig|3702.1.peg.3461.
Organism-specific databases
TAIR	At1g31180.
Phylogenomic databases
OMA	REGYNTM.
Enzyme and pathway databases
BRENDA	1.1.1.85. 302.
Gene expression databases
ArrayExpress	Q9SA14.
Genevestigator	Q9SA14.
GermOnline	AT1G31180. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004429. Isopropylmalate_DH. [Graphical view]
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

LEU31_ARATH

Accession

Primary (citable) accession number: Q9SA14
Secondary accession number(s): Q1EBW0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	June 12, 2007
Last modified:	November 3, 2009
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)