NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1128/AEM.68.5.2572-2575.2002; PubMed=11976137 [NCBI, ExPASy, EBI, Israel, Japan]
Sabater-Munoz B., Gomez-Valero L., van Ham R.C.H.J., Silva F.J., Latorre A.;
"Molecular characterization of the leucine cluster in Buchnera sp. strain PSY, a primary endosymbiont of the aphid Pemphigus spyrothecae.";
Appl. Environ. Microbiol. 68:2572-2575(2002).

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 (By similarity).
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

AJ426489; CAD20138.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P30125; 1CM7. [HSSP ENTRY / PDB]

ModBase

P59027.

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`	`1 363`	`363`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083659`
`NP_BIND`	`77 90`	`14`	`NAD (By similarity).`
`NP_BIND`	`284 296`	`13`	`NAD (By similarity).`
`METAL`	`226 226`		`Magnesium or manganese (By similarity).`
`METAL`	`250 250`		`Magnesium or manganese (By similarity).`
`METAL`	`254 254`		`Magnesium or manganese (By similarity).`
`BINDING`	`98 98`		`Substrate (By similarity).`
`BINDING`	`108 108`		`Substrate (By similarity).`
`BINDING`	`137 137`		`Substrate (By similarity).`
`BINDING`	`226 226`		`Substrate (By similarity).`
`SITE`	`144 144`	`1`	`Important for catalysis (By similarity).`
`SITE`	`194 194`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 363 AA [This is the length of the unprocessed precursor]

Molecular weight: 40550 Da [This is the MW of the unprocessed precursor]

CRC64: 760AAA94425D6632 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTKIYNLAIL PGDGIGPELL QKDLNFKVLK EQYKLKINTT EYDIGGIAID KYGKALPKET 

        70         80         90        100        110        120 
LDGCKESDSI LFGSVGGPKW QHLPPDQQPE RAALLPIRKY FNLFSNLRPA KLYSTLNHLS 

       130        140        150        160        170        180 
PLRRDISEKG FDILCVRELT GGIYFGKPKG YIKNIIDKKA FDTEIYYASE IKRIAHIGFK 

       190        200        210        220        230        240 
LAQNRKYKIT SVDKANVLES SVLWRETVNT ISKEYPDVKL SHLYIDHAAM QIIKNPDKFD 

       250        260        270        280        290        300 
VILTSNLFGD ILSDECAMIT GSIGMLPSAS LNDSNFGLYE PAGGSAPDIA GKNIANPIAQ 

       310        320        330        340        350        360 
ILSIAMLVRY TMKLPMISDH IESAVIDTLK KGYRTLDIAN DKEKYVSTND IGDIISDILK 


KRI

P59027 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