NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9244264 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Moya A., Latorre A.;
"Putative evolutionary origin of plasmids carrying the genes involved in leucine biosynthesis in Buchnera aphidicola (endosymbiont of aphids).";
J. Bacteriol. 179:4768-4777(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 (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

Y11966; CAA72702.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P37412; 1CNZ. [HSSP ENTRY / PDB]

ModBase

O31292.

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; Plasmid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 364`	`364`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083662`
`NP_BIND`	`79 92`	`14`	`NAD (By similarity).`
`NP_BIND`	`285 297`	`13`	`NAD (By similarity).`
`METAL`	`227 227`		`Magnesium or manganese (By similarity).`
`METAL`	`251 251`		`Magnesium or manganese (By similarity).`
`METAL`	`255 255`		`Magnesium or manganese (By similarity).`
`BINDING`	`100 100`		`Substrate (By similarity).`
`BINDING`	`110 110`		`Substrate (By similarity).`
`BINDING`	`139 139`		`Substrate (By similarity).`
`BINDING`	`227 227`		`Substrate (By similarity).`
`SITE`	`146 146`	`1`	`Important for catalysis (By similarity).`
`SITE`	`195 195`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 364 AA [This is the length of the unprocessed precursor]

Molecular weight: 40353 Da [This is the MW of the unprocessed precursor]

CRC64: D3EBFFE1DC07ACF2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTKKLYKIAV LPGDGIGPEI IQEAYKIIDV LQKKFSFNVK MHEYDIGGIS IDKHGTALTQ 

        70         80         90        100        110        120 
ETIEGCENSD AILFGSVGGS KWDHLPEIEK PEKAGLLKLR KHFNLFANIR PCKLSQHLLD 

       130        140        150        160        170        180 
ISPLKNSIIK KGIDLICIRE LTGGIYFGKS NKITNIDDPY AFDTEIYFRS EIKRIAKIAF 

       190        200        210        220        230        240 
QIAQSRKKKI VSIDKANVLK SSILWRDTVN KMAYKFPNVK LEHMYIDNAT MELIKNPSSF 

       250        260        270        280        290        300 
DVILCSNLFG DIISDECAAI IGSIGLLPSA SLNKSGFGLY EPAGGSAPNI AGKTIANPIA 

       310        320        330        340        350        360 
QILSLSMLLK YSLHLPFLSS CIDEAVHEAL VKKYMTMDIS KNPQNFLKTN EIGDKISDLL 


AKKA

O31292 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