[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1128/JB.183.2.785-790.2001; PubMed=11133977 [NCBI, ExPASy, EBI, Israel, Japan] Wernegreen J.J., Moran N.A.; "Vertical transmission of biosynthetic plasmids in aphid endosymbionts (Buchnera)."; J. Bacteriol. 183:785-790(2001).

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

AF197456; AAG31402.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P37412; 1CNZ. [HSSP ENTRY / PDB]

ModBase

Q9EVG3.

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`	`1 365`	`365`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083658`
`NP_BIND`	`78 91`	`14`	`NAD (By similarity).`
`NP_BIND`	`286 298`	`13`	`NAD (By similarity).`
`METAL`	`228 228`		`Magnesium or manganese (By similarity).`
`METAL`	`252 252`		`Magnesium or manganese (By similarity).`
`METAL`	`256 256`		`Magnesium or manganese (By similarity).`
`BINDING`	`99 99`		`Substrate (By similarity).`
`BINDING`	`109 109`		`Substrate (By similarity).`
`BINDING`	`139 139`		`Substrate (By similarity).`
`BINDING`	`228 228`		`Substrate (By similarity).`
`SITE`	`146 146`	`1`	`Important for catalysis (By similarity).`
`SITE`	`196 196`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 365 AA [This is the length of the unprocessed precursor]

Molecular weight: 40966 Da [This is the MW of the unprocessed precursor]

CRC64: 213AEB0F71DF960C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKQYRIAVL PGDGIGPEVM KEAYKILKIL QNYFSLHIEI KEFNIGGIAL DKEGVALPKD 

        70         80         90        100        110        120 
TLLGCENSDA ILFGSVGGKK WNNLPIEKRP ERASLLPLRK HFNLFYNLRP AKLYSELRFL 

       130        140        150        160        170        180 
SPLRSKTXIK NGFDILCIRE LTGGIYFGEP RGRLKKNNIE YAFDTEVYYD YEINRIAHVA 

       190        200        210        220        230        240 
FQLARTRKNK VCSIDKANVL NSSLLWREIV TKVSKNYPDV HLSHLYIDNA TMQIIQNPNQ 

       250        260        270        280        290        300 
FDILLCSNLF GDILSDECAI ITGSIGMLPS ASLNEKNFGL YEPAGGSAPD IAGKNIANPI 

       310        320        330        340        350        360 
AQILSLSMLV RYGMNLKKIA NKIDQSVISV LKKGYRTFDI SDDNNXFLKT NEMGDVIADA 


LINGE

Q9EVG3 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