[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1128/JB.185.11.3333-3343.2003; PubMed=12754231 [NCBI, ExPASy, EBI, Israel, Japan] Komatsu H., Imura Y., Ohori A., Nagata Y., Tsuda M.; "Distribution and organization of auxotrophic genes on the multichromosomal genome of Burkholderia multivorans ATCC 17616."; J. Bacteriol. 185:3333-3343(2003).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.; "Complete sequence of chromosome 2 of Burkholderia multivorans ATCC 17616."; Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E., Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N., Hattori M., Tsuda M.; "Complete genome sequence of Burkholderia multivorans ATCC 17616."; Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.

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

AB091435; BAC65259.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000869; ABX18305.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009386; BAG45744.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P12010; 2AYQ. [HSSP ENTRY / PDB]

ModBase

Q845W3.

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

Q845W3.

Genome annotation databases

CMR

Q845W3; Bmul_4627.

Other

ProtoNet

Q845W3.

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.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 355`	`355`	`3-isopropylmalate dehydrogenase.`	`PRO_0000083673`
`NP_BIND`	`280 292`	`13`	`NAD (By similarity).`
`METAL`	`222 222`		`Magnesium or manganese (By similarity).`
`METAL`	`246 246`		`Magnesium or manganese (By similarity).`
`METAL`	`250 250`		`Magnesium or manganese (By similarity).`
`BINDING`	`90 90`		`Substrate (By similarity).`
`BINDING`	`100 100`		`Substrate (By similarity).`
`BINDING`	`128 128`		`Substrate (By similarity).`
`BINDING`	`222 222`		`Substrate (By similarity).`
`SITE`	`135 135`	`1`	`Important for catalysis (By similarity).`
`SITE`	`190 190`	`1`	`Important for catalysis (By similarity).`

Sequence information

Length: 355 AA [This is the length of the unprocessed precursor]

Molecular weight: 38332 Da [This is the MW of the unprocessed precursor]

CRC64: 6ABAFC839D803186 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIAVLPGDG IGPEIVTEAV KVLNALDEKF ELEQAPVGGA GYEARGHPLP DATLKLAKEA 

        70         80         90        100        110        120 
DAILFGAVGD WKYDSLERAL RPEQAILGLR KHLELFANFR PAICYPQLVD ASPLKPELVA 

       130        140        150        160        170        180 
GLDILIVREL NGDIYFGQPR GVRAAPDGPF AGEREGFDTM RYSEPEVRRI AHVAFQAAQK 

       190        200        210        220        230        240 
RAKKLLSVDK SNVLETSQFW RDIMIDVSKE YADVELSHMY VDNAAMQLAK APKQFDVIVT 

       250        260        270        280        290        300 
GNMFGDILSD EASMLTGSIG MLPSASLDKN NKGLYEPSHG SAPDIAGKGI ANPLATILSA 

       310        320        330        340        350 
AMLLRYSLNR AEQADRIERA VKTVLEQGYR TGDIATPGCK QVGTAAMGDA VVAAL

Q845W3 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