Reviewed, UniProtKB/Swiss-Prot Q6FEV6 (LEU3_ACIAD)

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:	ACIAD0469

Organism

Acinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]

Taxonomic identifier

62977 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	359 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. HAMAP MF_01033
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: HAMAP oxidation reduction 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: HAMAP NAD or NADH binding Inferred from electronic annotation. Source: InterPro 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 – 359	359	3-isopropylmalate dehydrogenase HAMAP MF_01033		PRO_0000083626
Regions
	Nucleotide binding	76 – 89	14	NAD By similarity
	Nucleotide binding	283 – 295	13	NAD By similarity
Sites
	Metal binding	225	1	Magnesium or manganese By similarity
	Metal binding	249	1	Magnesium or manganese By similarity
	Metal binding	253	1	Magnesium or manganese By similarity
	Binding site	96	1	Substrate By similarity
	Binding site	106	1	Substrate By similarity
	Binding site	134	1	Substrate By similarity
	Binding site	225	1	Substrate By similarity
	Site	141	1	Important for catalysis By similarity
	Site	192	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6FEV6-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 8C8A50F44C9A791B	FASTA	359	38,544
	10 20 30 40 50 60 MSKQILILAG DGIGPEIVGA AEQVLTKVNE KFELGLTWEH GLLGGSAIDA HGEPYPAVTS 70 80 90 100 110 120 EQAKKADAIL LGAVGGPKWD TIERSIRPER GLLKIRSELN LFANLRPALL YPQLADASSL 130 140 150 160 170 180 KPEIVAGLDI LIVRELTGGI YFGQPRGIRE LENGEKQGYN TDVYSESEIK RIAKVAFELA 190 200 210 220 230 240 ALRGSKVCSV DKANVLEVTE LWKQTVTELQ QAQYPNIQLS HMYVDNAAMQ LVRAPKQFDV 250 260 270 280 290 300 IVTGNLFGDI LSDEAAMLTG SIGMLPSASL DENGKGMYEP CHGSAPDIAG QNVANPLATI 310 320 330 340 350 LSVAMMLRYT FREEAAAKAI EDAVGQVLDQ GLRTADIMSE GMQRVGTVEM GQAVVAALA

References

[1]

"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium." Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C. Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR543861 Genomic DNA. Translation: CAG67402.1.
RefSeq	YP_045224.1.
3D structure databases
SMR	Q6FEV6. Positions 3-358.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6FEV6.
Genome annotation databases
GeneID	2880113.
GenomeReviews	Gene locus ACIAD0469 in contig CR543861_GR.
KEGG	aci:ACIAD0469.
NMPDR	fig|62977.3.peg.1122.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0473.
HOGENOM	HBG518924.
OMA	MSYQIAV.
PhylomeDB	Q6FEV6.
Enzyme and pathway databases
BioCyc	ASP62977:ACIAD0469-MONOMER.
Family and domain databases
HAMAP	MF_01033. LeuB_type1. [Tree]
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004429. Isopropylmalate_DH. [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_ACIAD

Accession

Primary (citable) accession number: Q6FEV6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
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)