Reviewed, UniProtKB/Swiss-Prot Q97EE2 (LEU3_CLOAB)

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:	CA_C3171

Organism

Clostridium acetobutylicum [Complete proteome] [HAMAP]

Taxonomic identifier

1488 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	357 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 – 357	357	3-isopropylmalate dehydrogenase		PRO_0000083680
Regions
	Nucleotide binding	77 – 90	14	NAD By similarity
	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	97	1	Substrate By similarity
	Binding site	107	1	Substrate By similarity
	Binding site	136	1	Substrate By similarity
	Binding site	224	1	Substrate By similarity
	Site	143	1	Important for catalysis By similarity
	Site	192	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q97EE2-1 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: E24DF0A2BD2EBC2C	FASTA	357	38,980
	10 20 30 40 50 60 MKEYKVAVIP GDGIGVEIVG EALKVLEKVG AKYDTKFNFT EVKAGGCAID EFGVPLPNET 70 80 90 100 110 120 LEICKNSDAV LLGAVGGPKW DTLPGEKRPE KALMGLRGGL GLYANLRPAK VYDILKSASP 130 140 150 160 170 180 LKEEIINKGV DLLVVRELTG GIYFGERGRD IQNGINSAYD TERYNVEEIK RIAHVAFKAA 190 200 210 220 230 240 LKRNKKVTSV DKANILESSR LWRETVTEVA KEYPEVELNY LYVDNAAMQL VREPSQFDVI 250 260 270 280 290 300 VTSNIFGDIL TDEASMVTGS IGMLPSASLR NDTFGMYEPI HGSAPDIAGQ DLANPLAQIL 310 320 330 340 350 SVAMMLEYSF NMTEAARDVE DAVEKVLNSG YRTGDIYTEG SKKVGTKEMG KLVLAEL

References

[1]

"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum." Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R. J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE001437 Genomic DNA. Translation: AAK81108.1.
PIR	A97290.
RefSeq	NP_349768.1.
3D structure databases
HSSP	HSSP built from PDB template 1A05 based on UniProtKB Q56268.
ModBase	Search...
Genome annotation databases
GeneID	1119353.
GenomeReviews	Gene locus CA_C3171 in contig AE001437_GR.
KEGG	cac:CAC3171.
NMPDR	fig|272562.1.peg.3297.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q97EE2.
Enzyme and pathway databases
BioCyc	CACE272562:CAC3171-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_CLOAB

Accession

Primary (citable) accession number: Q97EE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	October 1, 2001
Last modified:	November 4, 2008
This is version 48 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)