Reviewed, UniProtKB/Swiss-Prot Q7WKH4 (LEU32_BORBR)

Names and origin

Protein names

Recommended name:
    3-isopropylmalate dehydrogenase 2
    EC=1.1.1.85
Alternative name(s):
    Beta-IPM dehydrogenase 2
      Short name=IMDH 2
    3-IPM-DH 2

Gene names

Name:	leuB2
Ordered Locus Names:	BB2132

Organism

Bordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

518 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	358 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 – 358	358	3-isopropylmalate dehydrogenase 2		PRO_0000083649
Regions
	Nucleotide binding	282 – 294	13	NAD By similarity
Sites
	Metal binding	224	1	Magnesium or manganese By similarity
	Metal binding	248	1	Magnesium or manganese By similarity
	Metal binding	252	1	Magnesium or manganese By similarity
	Binding site	92	1	Substrate By similarity
	Binding site	102	1	Substrate By similarity
	Binding site	130	1	Substrate By similarity
	Binding site	224	1	Substrate By similarity
	Site	137	1	Important for catalysis By similarity
	Site	192	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WKH4-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 719D3DDAF951DAEC	FASTA	358	38,541
	10 20 30 40 50 60 MTHQIAVLPG DGIGPEIVEQ AERVLKALDL PLELRQAPVG GAAFDQFEHP LPPATLELAQ 70 80 90 100 110 120 GSHAVLFGAV GDWKYDTLPR EFRPEQAILG LRKALGLFAN LRPAILYPEL ASASSLKPEI 130 140 150 160 170 180 VSGLDILIIR ELTGDIYFGT PRGVRTAADG AFAGEREGYD TMRYAESEVR RIARIGFESA 190 200 210 220 230 240 RKRNKKLCSV DKANVLETSQ FWRDLVIEVS RDYPDVELSH MYVDNAAMQL VRNPRQFDVI 250 260 270 280 290 300 VTGNLFGDIL SDEAAMLTGS IGMLPSASLN AAGQGLYEPS HGSAPDIAGQ GIANPLATIL 310 320 330 340 350 SAAMLLRYSL NLAPQADRVE AAVRKVLADG LRTADIHEAG TTKVSTSQMG DAVLKALG

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640443 Genomic DNA. Translation: CAE32628.1.
RefSeq	NP_888675.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2660922.
GenomeReviews	Gene locus BB2132 in contig BX470250_GR.
KEGG	bbr:BB2132.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7WKH4.
Enzyme and pathway databases
BioCyc	BBRO257310:BB2132-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

LEU32_BORBR

Accession

Primary (citable) accession number: Q7WKH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	October 1, 2003
Last modified:	November 4, 2008
This is version 38 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)