Reviewed, UniProtKB/Swiss-Prot O66607 (LEU3_AQUAE)

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:	aq_244

Organism

Aquifex aeolicus [Complete proteome] [HAMAP]

Taxonomic identifier

63363 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	364 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	Cytoplasm.
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 – 364	364	3-isopropylmalate dehydrogenase		PRO_0000083629
Regions
	Nucleotide binding	77 – 90	14	NAD By similarity
	Nucleotide binding	281 – 293	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	135	1	Substrate By similarity
	Binding site	224	1	Substrate By similarity
	Site	142	1	Important for catalysis By similarity
	Site	192	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	O66607-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 56B528C760712FAC	FASTA	364	40,714
	10 20 30 40 50 60 MKKYKIAVLK GDGIGPEIVE QALRVLDKIG EIYGVEFEYR EGLIGGEAID KTGDPLPEET 70 80 90 100 110 120 LKICKESDAI LLGAVGGPKW DNLPTDKRPE KGLLRIRKEL DLYANLRPAK VWDALISSSP 130 140 150 160 170 180 LKEEVVKGTD MIVIRELTSG IYYGEPRGIF EENGKRYAIN TMKYTEDEIR RIVRKGFEIA 190 200 210 220 230 240 RKRRKKLTSV DKANVLEVSA LWRQIVEEEK ENYPDVELEH LYIDNCAMQL VRRPTSFDVI 250 260 270 280 290 300 VTGNIFGDIL SDEAGVVVGS LGMLPSASIG DRYALYEPVH GSAPDIAGKG IANPIATILS 310 320 330 340 350 360 AAMMLKYSFN MDKAHDLIEK AIEETLNQGY RTPDIYSEGC IKVGTKEITD KILENLERLK DAYT

References

[1]

"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000657 Genomic DNA. Translation: AAC06564.1.
PIR	C70322.
RefSeq	NP_213167.1.
3D structure databases
HSSP	HSSP built from PDB template 1DPZ based on UniProtKB P00351.
ModBase	Search...
Genome annotation databases
GeneID	1192841.
GenomeReviews	Gene locus aq_244 in contig AE000657_GR.
KEGG	aae:aq_244.
NMPDR	fig|224324.1.peg.182.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O66607.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_244-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_AQUAE

Accession

Primary (citable) accession number: O66607

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	November 4, 2008
This is version 59 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)