NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Svalofs Karat 20516-K;
DOI=10.1007/BF00040671; PubMed=1371407 [NCBI, ExPASy, EBI, Israel, Japan]
Ellerstroem M., Josefsson L.G., Rask L., Ronne H.;
"Cloning of a cDNA for rape chloroplast 3-isopropylmalate dehydrogenase by genetic complementation in yeast.";
Plant Mol. Biol. 18:557-566(1992).

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: 3-carboxy-2-hydroxy-4-methylpentanoate + NAD⁺ = 3-carboxy-4-methyl-2-oxopentanoate + 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: Homodimer (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast.
SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X59970; CAA42596.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S20510; S20510.

3D structure databases

HSSP

Q56268; 1A05. [HSSP ENTRY / PDB]

ModBase

P29102.

Family and domain databases

InterPro

IPR004429; 3-isopropylmalate_DHase.
IPR001804; IsoCit_IM_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.718.10; IDH_IMDH; 1.

PANTHER

PTHR11835; IDH_IMDH_dimeric; 1.
PTHR11835:SF13; IPMDH; 1.

Pfam

PF00180; Iso_dh; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00169; leuB; 1.

PROSITE

PS00470; IDH_IMDH; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Chloroplast; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase; Plastid; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 34`	`34`	`Chloroplast (Potential).`
`CHAIN`	`35 406`	`372`	`3-isopropylmalate dehydrogenase, chloroplastic.`	`PRO_0000014456`
`NP_BIND`	`117 130`	`14`	`NAD (By similarity).`
`NP_BIND`	`323 335`	`13`	`NAD (By similarity).`
`METAL`	`265 265`		`Magnesium or manganese (By similarity).`
`METAL`	`289 289`		`Magnesium or manganese (By similarity).`
`METAL`	`293 293`		`Magnesium or manganese (By similarity).`
`BINDING`	`137 137`		`Substrate (By similarity).`
`BINDING`	`147 147`		`Substrate (By similarity).`
`BINDING`	`175 175`		`Substrate (By similarity).`
`BINDING`	`265 265`		`Substrate (By similarity).`
`SITE`	`182 182`	`1`	`Important for catalysis (By similarity).`
`SITE`	`233 233`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 406 AA [This is the length of the unprocessed precursor]

Molecular weight: 43351 Da [This is the MW of the unprocessed precursor]

CRC64: 2C8CCEA3B28FF192 [This is a checksum on the sequence]

        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

P29102 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools