Reviewed, UniProtKB/Swiss-Prot Q62AI9 (LEU3_BURMA)

Names and origin

Protein names

Recommended name:
    3-isopropylmalate dehydrogenase
    EC=1.1.1.85
Alternative name(s):
    Beta-IPM dehydrogenase
      Short name=IMDH
    3-IPM-DH

Gene names

Name:	leuB
Ordered Locus Names:	BMAA1726

Organism

Burkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]

Taxonomic identifier

13373 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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	(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + 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 structure	Homodimer By similarity.
Subcellular location	CytoplasmBy similarity.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis
Cellular component	Cytoplasm
Ligand	Magnesium Manganese Metal-binding NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	leucine biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
Molecular function	3-isopropylmalate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 355	355	3-isopropylmalate dehydrogenase		PRO_0000083672
Regions
	Nucleotide binding	280 – 292	13	NAD By similarity
Sites
	Metal binding	222	1	Magnesium or manganese By similarity
	Metal binding	246	1	Magnesium or manganese By similarity
	Metal binding	250	1	Magnesium or manganese By similarity
	Binding site	90	1	Substrate By similarity
	Binding site	100	1	Substrate By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	222	1	Substrate By similarity
	Site	135	1	Important for catalysis By similarity
	Site	190	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q62AI9-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 8BB994DF67538F7A	FASTA	355	38,187
	10 20 30 40 50 60 MKIAVLPGDG IGPEIVNEAV KVLNALDEKF ELEQAPVGGA GYEASGHPLP DATLALAKEA 70 80 90 100 110 120 DAILFGAVGD WKYDSLERAL RPEQAILGLR KHLELFANFR PAICYPQLVD ASPLKPELVA 130 140 150 160 170 180 GLDILIVREL NGDIYFGQPR GVRAAPDGPF AGAREGFDTM RYSEPEVRRI AHVAFQAARK 190 200 210 220 230 240 RAKKLLSVDK SNVLETSQFW RDVMIDVSKE YADVELSHMY VDNAAMQLAK APKQFDVIVT 250 260 270 280 290 300 GNMFGDILSD EASMLTGSIG MLPSASLDQR NKGLYEPSHG SAPDIAGKGI ANPLATILSA 310 320 330 340 350 AMLLRYSLNR AEQADRIERA VKAVLEQGYR TGDIATPGCK QVGTAAMGDA VVAAL

References

[1]

"Structural flexibility in the Burkholderia mallei genome." Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E., Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M. , Kolonay J.F., Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004) [PubMed: 15377793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 23344.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000011 Genomic DNA. Translation: AAU45711.1.
RefSeq	YP_106289.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3087377.
GenomeReviews	Gene locus BMAA1726 in contig CP000011_GR.
KEGG	bma:BMAA1726.
TIGR	BMAA1726.
Phylogenomic databases
HOGENOM	Q62AI9.
Enzyme and pathway databases
BioCyc	BMAL243160:BMA_A1726-MON.
Family and domain databases
HAMAP	MF_01033. [Tree]
InterPro	IPR004429. 3-isopropylmalate_DHase. IPR001804. IsoCit_IM_DHase. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11835. IDH_IMDH_dimeric. 1 hit. PTHR11835:SF13. IPMDH. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR00169. leuB. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LEU3_BURMA

Accession

Primary (citable) accession number: Q62AI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	October 25, 2004
Last modified:	November 4, 2008
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)