[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/s002849910052; PubMed=10688696 [NCBI, ExPASy, EBI, Israel, Japan] Soler T., Latorre A., Sabater B., Silva F.J.; "Molecular characterization of the Leucine plasmid from Buchnera aphidicola, primary endosymbiont of the aphid Acyrthosiphon pisum."; Curr. Microbiol. 40:264-268(2000).
[2]	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).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Tokyo 1998; DOI=10.1038/35024074; PubMed=10993077 [NCBI, ExPASy, EBI, Israel, Japan] Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."; Nature 407:81-86(2000).

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.
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

AJ006878; CAB56191.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF197457; AAG31405.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001071; BAA95424.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_057969.1; -.

3D structure databases

HSSP

P37412; 1CNZ. [HSSP ENTRY / PDB]

ModBase

P56933.

Enzyme and pathway databases

BioCyc

BSP107806:BUPL05-MON; -.

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.

BLOCKS

P56933.

Genome annotation databases

GeneID

1109450; -.

GenomeReviews

AP001071_GR; BUpL05.

KEGG

buc:BUpL05; -.

Phylogenomic databases

HOGENOM

P56933; -.

Genome annotation databases

CMR

P56933; BUpL05.

Other

ProtoNet

P56933.

UniRef

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

Keywords

Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; Cytoplasm; Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; Oxidoreductase; Plasmid.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 363`	`363`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083655`
`NP_BIND`	`78 91`	`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`	`99 99`		`Substrate (By similarity).`
`BINDING`	`109 109`		`Substrate (By similarity).`
`BINDING`	`138 138`		`Substrate (By similarity).`
`BINDING`	`227 227`		`Substrate (By similarity).`
`SITE`	`145 145`	`1`	`Important for catalysis (By similarity).`
`SITE`	`195 195`	`1`	`Important for catalysis (By similarity).`
`CONFLICT`	`101 101`		`H -> Y (in Ref. 1; CAB56191).`
`CONFLICT`	`186 186`		`R -> K (in Ref. 1; CAB56191).`
`CONFLICT`	`200 200`		`Q -> R (in Ref. 1; CAB56191).`
`CONFLICT`	`206 207`		`RE -> GK (in Ref. 1; CAB56191).`
`CONFLICT`	`363 363`		`E -> K (in Ref. 1 and 2).`

Sequence information

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

Molecular weight: 40479 Da [This is the MW of the unprocessed precursor]

CRC64: AB7D6DCF8FFD8D70 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKNYRIAVL SGDGIGPEVM QEACKILNVL KKYFFLSLEI QKFNIGGIAI EREGVALPKT 

        70         80         90        100        110        120 
TLLGCENSDS ILLGSVGGKK WDNLPVEQRP ERAALLPLRK HFNLFSNLRP AKLYPELKCL 

       130        140        150        160        170        180 
SPLRSDIVKN GFDILCVREL TGGIYFGEPK GFVNKNNTKY AFDTEIYHEY EIIRIAHLAF 

       190        200        210        220        230        240 
KLARSRKKKV CSIDKSNVLQ SSILWREVVE SVSKKYPDVH LSHLYIDNAA MQIIKDPNQF 

       250        260        270        280        290        300 
DVLLCSNLFG DIISDECATI TGSIGMLPSA SFNEKNFGLY EPAGGSAPDI EGKNIANPIA 

       310        320        330        340        350        360 
QILSLSMLVR YGMNLNQIAD KIDKAVNNVL KKGYRTSDIS HDNNFLKTDE MGDLIVDSLI 


NGE

P56933 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