[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 14830 / CBS 6330 / DSM 2031 / MS-5 / NRRL Y-17506; Biasio W.; Thesis (2000), University of Vienna, Austria.

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

AJ279020; CAC10274.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P12010; 2AYQ. [HSSP ENTRY / PDB]

ModBase

Q9HDQ5.

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`	`1 359`	`359`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083606`
`NP_BIND`	`77 88`	`12`	`NAD (By similarity).`
`NP_BIND`	`287 298`	`12`	`NAD (By similarity).`
`METAL`	`223 223`		`Magnesium or manganese (By similarity).`
`METAL`	`248 248`		`Magnesium or manganese (By similarity).`
`METAL`	`252 252`		`Magnesium or manganese (By similarity).`
`BINDING`	`95 95`		`Substrate (By similarity).`
`BINDING`	`105 105`		`Substrate (By similarity).`
`BINDING`	`134 134`		`Substrate (By similarity).`
`BINDING`	`223 223`		`Substrate (By similarity).`
`SITE`	`141 141`	`1`	`Important for catalysis (By similarity).`
`SITE`	`190 190`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 359 AA [This is the length of the unprocessed precursor]

Molecular weight: 37728 Da [This is the MW of the unprocessed precursor]

CRC64: 1E888608B8C732F0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKSIVLLPG DHVGTEVVAE AVKVLKAIER TTPGTSFSFS THLIGGAAID ATGVPLPDEA 

        70         80         90        100        110        120 
LEAAKASDAV LLGAVGGPKW GTGDVRPEQG LLKIRKELGL YANLRPCSFA SSKLVDLSPL 

       130        140        150        160        170        180 
KREIVEGTDF VVVRELVGGI YFGERKEDDG SGVASDTETY SVPEVERITR MAAFLALQHN 

       190        200        210        220        230        240 
PPQTVWSLDK ANVLASSRLW RKTVTRVMTE EFPTVPFQHQ LIDSAAMILV QKPTKLNGVV 

       250        260        270        280        290        300 
LTSNMFGDII SDEASVIPGS LGLLPSASLA SLPDTNTAFG LYEPCHGSAP DLPAGKVNPL 

       310        320        330        340        350 
ACILSAAMML RLSLDNAAAA DRIEQAVREV IDSGVATADL GGSSSTGEVG DAIVKALEK

Q9HDQ5 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