Q73B99 (LEU3_BACC1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-isopropylmalate dehydrogenase
EC=1.1.1.85

Alternative name(s):
3-IPM-DH
Beta-IPM dehydrogenase
Short name=IMDH

Gene names

Name:	leuB
Ordered Locus Names:	BCE_1521

Organism

Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]

Taxonomic identifier

222523 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
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. HAMAP MF_01033
Catalytic activity	(2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH. HAMAP MF_01033
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. HAMAP MF_01033
Subunit structure	Homodimer By similarity. HAMAP MF_01033
Subcellular location	Cytoplasm By similarity HAMAP MF_01033.
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: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3-isopropylmalate dehydrogenase activity Inferred from electronic annotation. Source: EC NAD binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro
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 HAMAP MF_01033		PRO_0000083634
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)
	Q73B99 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 484A8DD01C938326	FASTA	354	38,460
	10 20 30 40 50 60 MEKRIVCLAG DGVGPEVMES AKEVLHMVER LYGHHFHLQD EYFGGSAIDL NGQPLPQRTL 70 80 90 100 110 120 AACLASDAVL LGAVGGPRWD SAKERPEKGL LALRKGLGVF ANVRPVTVES ATAHLSPLKK 130 140 150 160 170 180 ADEIDFVVVR ELTGGIYFSY PKERTDEVAT DTLTYHRHEI ERIVSYAFQL ASKRKKKVTS 190 200 210 220 230 240 IDKANVLESS KLWRTVTEEV ALRYPDVELE HILVDAAAME LIRNPGRFDV IVTENLFGDI 250 260 270 280 290 300 LSDEASVLAG SLGMLPSASH AEKGPSLYEP IHGSAPDIAG KNKANPIAMM RSVAMMLGQS 310 320 330 340 350 FGLTREGCAI EEAISAVLKL GKCTADIGGT ETTTSFTKAV MQEMEEQALV GRGR

References

[1]

"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10987.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017194 Genomic DNA. Translation: AAS40450.1.
RefSeq	NP_977842.1. NC_003909.8.
3D structure databases
ProteinModelPortal	Q73B99.
SMR	Q73B99. Positions 1-344.
ModBase	Search...
Protein-protein interaction databases
STRING	Q73B99.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000028930; EBBACP00000028280; EBBACG00000028921.
GeneID	2747116.
GenomeReviews	Gene locus BCE_1521 in contig AE017194_GR.
KEGG	bca:BCE_1521.
NMPDR	fig|222523.1.peg.1514.
PATRIC	18851886. VBIBacCer118379_1447.
TIGR	BCE_1521.
Phylogenomic databases
eggNOG	COG0473.
GeneTree	EBGT00050000000661.
HOGENOM	HBG518924.
OMA	AAMMLRF.
ProtClustDB	PRK00772.
Enzyme and pathway databases
BioCyc	BCER405917:BCE_1521-MONOMER.
Family and domain databases
HAMAP	MF_01033. LeuB_type1. [Tree]
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR024084. IsoPropMal-DH-like_dom. IPR004429. Isopropylmalate_DH. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
KO	K00052.
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_BACC1

Accession

Primary (citable) accession number: Q73B99

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program