[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=M8650; Kimura H., Matumura S., Suzuki M., Sumino Y.; Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.

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

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Cross-references

Sequence databases

EMBL

D50665; BAA09319.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P12010; 2AYQ. [HSSP ENTRY / PDB]

ModBase

Q12545.

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`	`1 380`	`380`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083607`
`NP_BIND`	`79 90`	`12`	`NAD (By similarity).`
`NP_BIND`	`294 306`	`13`	`NAD (By similarity).`
`METAL`	`229 229`		`Magnesium or manganese (By similarity).`
`METAL`	`254 254`		`Magnesium or manganese (By similarity).`
`METAL`	`258 258`		`Magnesium or manganese (By similarity).`
`BINDING`	`97 97`		`Substrate (By similarity).`
`BINDING`	`107 107`		`Substrate (By similarity).`
`BINDING`	`136 136`		`Substrate (By similarity).`
`BINDING`	`229 229`		`Substrate (By similarity).`
`SITE`	`143 143`	`1`	`Important for catalysis (By similarity).`
`SITE`	`196 196`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 380 AA [This is the length of the unprocessed precursor]

Molecular weight: 40637 Da [This is the MW of the unprocessed precursor]

CRC64: 0F99ACD5251CCB43 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTTYKILVL PGDHIGPEIM AEAIKVLTTI ETHRPNLHFN LTTDLVGGTS IDTHGVPITQ 

        70         80         90        100        110        120 
SVLDAAKASD AVLFGSIGGP EWAGVHPTPE SGLLQLRQHL DAFANLRPCE FLVPSLVGAS 

       130        140        150        160        170        180 
PIREHVVKGT RFIVVRENCG GAYFGEKKEE EDVASDLWVY TRPEIERLAR VSAAVARIMG 

       190        200        210        220        230        240 
RSEDDNQAAT VWSADKANVL ASGRLWRRIT SDIFAKEFPD ITLQHQLADS MAMLMVRDPR 

       250        260        270        280        290        300 
RFNGVIHTDN TFGDILSDIS GAITGTLGLM PSASLCGVPG EGHRSNGIYE PVHGSAPDIS 

       310        320        330        340        350        360 
GKGLANPVAQ ILSVAMMLRY SMGLEKEATA VERAVVKVLD AKSEGGLEIR TGDLGGRATC 

       370        380 
SQVGDAVCEV LGPLLQGKKA

Q12545 in FASTA format

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View entry in raw text format (no links)
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	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