[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00384606; PubMed=2897248 [NCBI, ExPASy, EBI, Israel, Japan] Takagi M., Kobayashi N., Sugimoto M., Fujii T., Watari J., Yano K.; "Nucleotide sequencing analysis of a LEU gene of Candida maltosa which complements leuB mutation of Escherichia coli and leu2 mutation of Saccharomyces cerevisiae."; Curr. Genet. 11:451-457(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=G587; DOI=10.1007/BF00309549; PubMed=7859302 [NCBI, ExPASy, EBI, Israel, Japan] Becher D., Schulze S., Kasuske A., Schulze H., Samsonova I.A., Oliver S.G.; "Molecular analysis of a leu2-mutant of Candida maltosa demonstrates the presence of multiple alleles."; Curr. Genet. 26:208-216(1994).

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: Cytoplasm.
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

X05459; CAA29024.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X72940; CAA51445.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S48228; S48228.

3D structure databases

HSSP

P12010; 2AYQ. [HSSP ENTRY / PDB]

ModBase

P07139.

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; Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 373`	`373`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083604`
`NP_BIND`	`82 93`	`12`	`NAD (By similarity).`
`NP_BIND`	`295 306`	`12`	`NAD (By similarity).`
`METAL`	`231 231`		`Magnesium or manganese (By similarity).`
`METAL`	`256 256`		`Magnesium or manganese (By similarity).`
`METAL`	`260 260`		`Magnesium or manganese (By similarity).`
`BINDING`	`100 100`		`Substrate (By similarity).`
`BINDING`	`110 110`		`Substrate (By similarity).`
`BINDING`	`139 139`		`Substrate (By similarity).`
`BINDING`	`231 231`		`Substrate (By similarity).`
`SITE`	`146 146`	`1`	`Important for catalysis (By similarity).`
`SITE`	`198 198`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 373 AA [This is the length of the unprocessed precursor]

Molecular weight: 40173 Da [This is the MW of the unprocessed precursor]

CRC64: 256E9886219BA529 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVKTKTITI LPGDHVGTEI VNEAIKVLEA IEAATPYQKI HFDFKHHLIG GAAIDATGVP 

        70         80         90        100        110        120 
LPDDALESAK NSDAVLLGAV GGPKWGTGAL RPEQGLLKIR KELNLYANIR PCNFASDSLL 

       130        140        150        160        170        180 
ELSPLRPEVV KGTNLIIVRE LVGGIYFGDR EEQEESADKQ TAWDTEKYTV DEVTRITRMA 

       190        200        210        220        230        240 
AFMALQHTPP LPIWSLDKAN VLASSRLWRR TVDKVISEEF PTLSVQHQLI DSAAMILIQN 

       250        260        270        280        290        300 
PTKLNGIIIT SNMFGDIISD EASVIPGSLG LLPSASLASL PDTNTAFGLY EPCHGSAPDL 

       310        320        330        340        350        360 
PANKVNPIAT ILSAASMLRL SLDCVKEAEA LEEAVKQVLD KGIRTADLRG TSSTTEVGDA 

       370 
IVEAVTKILK EKA

P07139 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