Reviewed, UniProtKB/Swiss-Prot Q81G11 (LEU3_BACCR)

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:	BC_1401

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	354 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 – 354	354	3-isopropylmalate dehydrogenase		PRO_0000083635
Regions
	Nucleotide binding	76 – 87	12	NAD By similarity
	Nucleotide binding	273 – 285	13	NAD By similarity
Sites
	Metal binding	215	1	Magnesium or manganese By similarity
	Metal binding	239	1	Magnesium or manganese By similarity
	Metal binding	243	1	Magnesium or manganese By similarity
	Binding site	94	1	Substrate By similarity
	Binding site	104	1	Substrate By similarity
	Binding site	130	1	Substrate By similarity
	Binding site	215	1	Substrate By similarity
	Site	137	1	Important for catalysis By similarity
	Site	183	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81G11-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 77E0C59152DE97D0	FASTA	354	38,473
	10 20 30 40 50 60 MEKRIVCLAG DGVGPEVMES AKEVLHMVER LYGHHFHLQD EYFGGVAIDL TGQPLPQRTL 70 80 90 100 110 120 AACLASDAVL LGAVGGPRWD SAKERPEKGL LALRKGLGVF ANVRPVTVES ATAHLSPLKN 130 140 150 160 170 180 ADEIDFVVVR ELTGGIYFSY PKERTEEVAT DTLTYHRHEI ERIVSYAFQL ANKRKKKVTS 190 200 210 220 230 240 IDKANVLESS KLWRTVTEEV ALRYPNVEVE HILVDAAAME LIRNPGRFDV IVTENLFGDI 250 260 270 280 290 300 LSDEASVLAG SLGMLPSASH AEKGPSLYEP IHGSAPDIAG KNKANPIAMM RSVAMMLGQS 310 320 330 340 350 FGLTREGYAI EEAVSAVLKS GKCTADIGGT ETTTSFTKAV IQEMEEQALV GRGR

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016877 Genomic DNA. Translation: AAP08382.1.
RefSeq	NP_831181.1.
3D structure databases
HSSP	HSSP built from PDB template 2AYQ based on UniProtKB P12010.
ModBase	Search...
Genome annotation databases
GeneID	1203750.
GenomeReviews	Gene locus BC_1401 in contig AE016877_GR.
KEGG	bce:BC1401.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q81G11.
Enzyme and pathway databases
BioCyc	BCER226900:BC_1401-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_BACCR

Accession

Primary (citable) accession number: Q81G11

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	June 1, 2003
Last modified:	November 4, 2008
This is version 42 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)