[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Sekiguchi T., Ortega-Cesena J., Nosoh Y., Ohashi S., Tsuda K., Kanaya S.; "DNA and amino-acid sequences of 3-isopropylmalate dehydrogenase of Bacillus coagulans. Comparison with the enzymes of Saccharomyces cerevisiae and Thermus thermophilus."; Biochim. Biophys. Acta 867:36-44(1986).
[2]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND SUBUNIT. PubMed=9498551 [NCBI, ExPASy, EBI, Israel, Japan] Tsuchiya D., Sekiguchi T., Takenaka A.; "Crystal structure of 3-isopropylmalate dehydrogenase from the moderate facultative thermophile, Bacillus coagulans: two strategies for thermostabilization of protein structures."; J. Biochem. 122:1092-1104(1997).

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.
PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4 .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.

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

M33099; AAA22554.1; ALT_SEQ; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24537; DEBSIC.

3D structure databases

PDB

1V53; X-ray; 2.85 A; A/B=1-366.	[ExPASy / RCSB / EBI]
1V5B; X-ray; 2.95 A; A/B/C/D/E/F/G/H=1-366.	[ExPASy / RCSB / EBI]
2AYQ; X-ray; 3.00 A; A/B=1-366.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1V53; -.
1V5B; -.
2AYQ; -.

ModBase

P12010.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003862;	Molecular function: 3-isopropylmalate dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0009098;	Biological process: leucine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01033; -; 1.
PBIL [Tree]

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

P12010; -.

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

Keywords

3D-structure; 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`	`1 366`	`366`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083638`
`NP_BIND`	`76 89`	`14`	`NAD (By similarity).`
`NP_BIND`	`280 292`	`13`	`NAD (By similarity).`
`METAL`	`222 222`		`Magnesium or manganese (By similarity).`
`METAL`	`246 246`		`Magnesium or manganese (By similarity).`
`METAL`	`250 250`		`Magnesium or manganese (By similarity).`
`BINDING`	`96 96`		`Substrate (By similarity).`
`BINDING`	`106 106`		`Substrate (By similarity).`
`BINDING`	`134 134`		`Substrate (By similarity).`
`BINDING`	`222 222`		`Substrate (By similarity).`
`SITE`	`141 141`	`1`	`Important for catalysis (By similarity).`
`SITE`	`190 190`	`1`	`Important for catalysis (By similarity).`
`STRAND`	`3 11`	`9`
`HELIX`	`14 29`	`16`
`STRAND`	`36 40`	`5`
`HELIX`	`45 51`	`7`
`STRAND`	`52 55`	`4`
`HELIX`	`57 64`	`8`
`STRAND`	`66 73`	`8`
`HELIX`	`77 79`	`3`
`STRAND`	`80 82`	`3`
`HELIX`	`84 86`	`3`
`HELIX`	`88 99`	`12`
`STRAND`	`103 109`	`7`
`HELIX`	`112 114`	`3`
`TURN`	`115 117`	`3`
`STRAND`	`118 120`	`3`
`HELIX`	`122 125`	`4`
`STRAND`	`129 135`	`7`
`STRAND`	`137 139`	`3`
`TURN`	`140 142`	`3`
`STRAND`	`146 151`	`6`
`STRAND`	`155 163`	`9`
`HELIX`	`164 180`	`17`
`STRAND`	`183 189`	`7`
`TURN`	`191 193`	`3`
`HELIX`	`195 208`	`14`
`STRAND`	`214 220`	`7`
`HELIX`	`221 230`	`10`
`HELIX`	`232 234`	`3`
`STRAND`	`236 240`	`5`
`HELIX`	`242 252`	`11`
`TURN`	`253 256`	`4`
`STRAND`	`263 267`	`5`
`STRAND`	`269 271`	`3`
`STRAND`	`273 279`	`7`
`HELIX`	`283 285`	`3`
`HELIX`	`294 308`	`15`
`HELIX`	`311 326`	`16`
`STRAND`	`329 334`	`6`
`HELIX`	`344 354`	`11`

Sequence information

Length: 366 AA [This is the length of the unprocessed precursor]

Molecular weight: 39809 Da [This is the MW of the unprocessed precursor]

CRC64: 05958B786718408E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKMKLAVLPG DGIGPEVMDA AIRVLKTVLD NDGHEAVFEN ALIGGAAIDE AGTPLPEETL 

        70         80         90        100        110        120 
DICRRSDAIL LGAVGGPKWD HNPASLRPEK GLLGLRKEMG LFANLRPVKA YATLLNASPL 

       130        140        150        160        170        180 
KRERVENVDL VIVRELTGGL YFGRPSERRG PGENEVVDTL AYTREEIERI IEKAFQLAQI 

       190        200        210        220        230        240 
RRKKLASVDK ANVLESSRMW REIAEETAKK YPDVELSHML VDSTSMQLIA NPGQFDVIVT 

       250        260        270        280        290        300 
ENMFGDILSD EASVITGSLG MLPSASLRSD RFGMYEPVHG SAPDIAGQGK ANPLGTVLSA 

       310        320        330        340        350        360 
ALMLRYSFGL EKEAAAIEKA VDDVLQDGYC TGDLQVANGK VVSTIELTDR LIEKLNNSAA 


RPRIFQ

P12010 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