Reviewed, UniProtKB/Swiss-Prot Q2T7H6 (LEU3_BURTA)

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:	BTH_II0674

Organism

Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]

Taxonomic identifier

271848 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

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 By similarity.
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_0000250109
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)
	Q2T7H6-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: CE8C13AF0007C5E4	FASTA	355	38,242
	10 20 30 40 50 60 MKIAVLPGDG IGPEIVNEAV KVLNALDEKF ELEHAPVGGA GYEASGHPLP DATLALAKEA 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 RDVMIDVSKE YADVELSHMY VDNAAMQLAK APKQFDVIVT 250 260 270 280 290 300 GNMFGDILSD EASMLTGSIG MLPSASLDKN NKGLYEPSHG SAPDIAGKGI ANPLATILSA 310 320 330 340 350 AMLLRYSLNR AEQADRIERA VKTVLEQGYR TGDIATPGCR QVGTAAMGDA VVAAL

References

[1]

Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Palmer N., Dodson R., Hickey E.K., Gwinn M.L., Dougherty B., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van-Vugt R., Adams M.D., Gocayne J.D., Weidman J., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S., Fujii C., Cotton M.D., Horst K., Tomb J.-F., Roberts K., Hatch B., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000085 Genomic DNA. Translation: ABC35976.1.
RefSeq	YP_438873.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3845853.
GenomeReviews	Gene locus BTH_II0674 in contig CP000085_GR.
KEGG	bte:BTH_II0674.
TIGR	BTH_II0674.
Phylogenomic databases
HOGENOM	Q2T7H6.
Enzyme and pathway databases
BioCyc	BTHA271848:BTH_II0674-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_BURTA

Accession

Primary (citable) accession number: Q2T7H6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2006
Last sequence update:	January 24, 2006
Last modified:	November 4, 2008
This is version 25 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)