Reviewed, UniProtKB/Swiss-Prot Q63DX7 (LEU3_BACCZ)

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:	BCE33L1286

Organism

Bacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]

Taxonomic identifier

288681 [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_0000083636
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)
	Q63DX7-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 67E055F07ED68F45	FASTA	354	38,493
	10 20 30 40 50 60 MEKRIVCLAG DGVGPEVMES AKEVLHMVER LYGHHFHLQD EHFGGVAIDL TGQPLPQRTL 70 80 90 100 110 120 AACLASDAVL LGAVGGPRWD GAKERPEKGL LALRKGLGVF ANVRPVTVES ETAHLSPLKK 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 EEAISAVLKS GKCTEDIGGT ETTTSFTKAV MQEMEEQALV GRGR

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000001 Genomic DNA. Translation: AAU18962.1.
RefSeq	YP_082885.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3022955.
GenomeReviews	Gene locus BCE33L1286 in contig CP000001_GR.
KEGG	bcz:BCZK1286.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q63DX7.
Enzyme and pathway databases
BioCyc	BCER288681:BCE33L1286-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_BACCZ

Accession

Primary (citable) accession number: Q63DX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	October 25, 2004
Last modified:	November 4, 2008
This is version 33 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)