[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1093/nar/15.2.853; PubMed=3547331 [NCBI, ExPASy, EBI, Israel, Japan] Sekiguchi T., Suda M., Ishii T., Nosoh Y., Tsuda K.; "The nucleotide sequence of 3-isopropylmalate dehydrogenase gene from Bacillus caldotenax."; Nucleic Acids Res. 15:853-853(1987).

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.
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

X04762; CAA28455.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A26447; A26447.

3D structure databases

HSSP

P12010; 2AYQ. [HSSP ENTRY / PDB]

ModBase

P05644.

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

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`	`1 366`	`366`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083633`
`NP_BIND`	`77 90`	`14`	`NAD (By similarity).`
`NP_BIND`	`280 292`	`13`	`NAD (By similarity).`
`METAL`	`223 223`		`Magnesium or manganese (By similarity).`
`METAL`	`246 246`		`Magnesium or manganese (By similarity).`
`METAL`	`250 250`		`Magnesium or manganese (By similarity).`
`BINDING`	`97 97`		`Substrate (By similarity).`
`BINDING`	`107 107`		`Substrate (By similarity).`
`BINDING`	`135 135`		`Substrate (By similarity).`
`BINDING`	`223 223`		`Substrate (By similarity).`
`SITE`	`142 142`	`1`	`Important for catalysis (By similarity).`
`SITE`	`191 191`	`1`	`Important for catalysis (By similarity).`

Sequence information

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

Molecular weight: 39636 Da [This is the MW of the unprocessed precursor]

CRC64: 530C88B3A60C630D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGNYRIAVLP GDGIGKEVTS GAVEVLKAVG IRFGHEFTFE YGLIGGAAID EAGTPLPEET 

        70         80         90        100        110        120 
VRLCRESDAV LLGAVGGPKW DDNPPHLRPE KGLLAIRKQL DLYANLRPVV CYDSLVSRSP 

       130        140        150        160        170        180 
LKPDLVQGVD FVIVRELTGG IYFGQPSAVV ENGEEKAVDT LLYKKEEIER IVRMAFELAR 

       190        200        210        220        230        240 
GRRKKVTSVD KANVLSSSRL WREVAEEVAN EFPDVTLEHM LVDMRMQLIR APKQFDVIVT 

       250        260        270        280        290        300 
ENMFGDILSD EASMLSGSLG MLPSASLSAS GPSLYEPVHG SAPDIAGMNK ANPIAAILSA 

       310        320        330        340        350        360 
AMMLRLSFGL TAEAGGRARV WQALALGSGS RLGQRRPHLS TNEMVEEIKA AVLDYTAIAQ 


IMTVYA

P05644 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
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