NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.;
"Complete sequence of chromosome 2 of Burkholderia sp. 383.";
Submitted (OCT-2005) 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 (By similarity).
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

CP000152; ABB12242.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_372886.1; -.

3D structure databases

ModBase

Q393X4.

Enzyme and pathway databases

BioCyc

BSP36773:BCEP18194_B2131-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

Q393X4.

Genome annotation databases

GeneID

3753896; -.

GenomeReviews

CP000152_GR; Bcep18194_B2131.

KEGG

bur:Bcep18194_B2131; -.

NMPDR

fig|269483.3.peg.2136; -.

Phylogenomic databases

HOGENOM

Q393X4; -.

Genome annotation databases

CMR

Q393X4; Bcep18194_B2131.

Other

ProtoNet

Q393X4.

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_0000250108`
`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: 38336 Da [This is the MW of the unprocessed precursor]

CRC64: 116892E5CB59E424 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKIAVLPGDG IGPEIVNEAV KVLNALDEKF ELEQAPVGGA GYEASGHPLP DATLKLAKEA 

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

       130        140        150        160        170        180 
GLDILIVREL NGDIYFGQPR GVRTAPDGLF AGEREGFDTM RYSEPEVRRI AHVAFQAARK 

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

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

       310        320        330        340        350 
AMMLRYSLNR AEQADRIERA VKTVLEQGYR TGDIATPGGQ QVGTTAMGDA VVAAL

Q393X4 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