Reviewed, UniProtKB/Swiss-Prot Q2IJK7 (LEU3_ANADE)

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:	Adeh_2070

Organism

Anaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]

Taxonomic identifier

290397 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

Protein attributes

Sequence length	353 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 By similarity.
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.
Subcellular location	Cytoplasm By 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: 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 – 353	353	3-isopropylmalate dehydrogenase HAMAP MF_01033		PRO_0000250101
Regions
	Nucleotide binding	76 – 89	14	NAD By similarity
	Nucleotide binding	281 – 293	13	NAD By similarity
Sites
	Metal binding	223	1	Magnesium or manganese By similarity
	Metal binding	247	1	Magnesium or manganese By similarity
	Metal binding	251	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	223	1	Substrate By similarity
	Site	141	1	Important for catalysis By similarity
	Site	191	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2IJK7-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: 088C964A71D5E7B7	FASTA	353	37,286
	10 20 30 40 50 60 MNAKIVVLPG DGIGPEVTAE AVRVLEAVAR RGGHALSFTE RLMGGCSIDA HGTALTPEVL 70 80 90 100 110 120 ADCQAADAVL LGAVGGPKWD DPRAKVRPEQ GLLGLRKGLG VFANLRPVRV HPSLLDSSPL 130 140 150 160 170 180 RPEKLRGVDI MVIRELTGGL YFGQPKGRDV KDGHARAVDT LEYQDFEVRR VVELAFRIAK 190 200 210 220 230 240 GRKKKVTSVD KANVLESSRL WRELATAIGQ ANPDVALDHM LVDTAAMRLV TSPATLDVVV 250 260 270 280 290 300 TENMFGDILT DEASVLAGSM GMLPSASIGE QGPGLYEPIH GSAPDIAGKG IANPVGTVLS 310 320 330 340 350 AALLLRHSLG LEPEAAAIER AVDQTITDGC RTADLGGKLS TRAMADEILK RLA

References

[1]

"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000251 Genomic DNA. Translation: ABC81840.1.
RefSeq	YP_465277.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q2IJK7.
Genome annotation databases
GeneID	3888347.
GenomeReviews	Gene locus Adeh_2070 in contig CP000251_GR.
KEGG	ade:Adeh_2070.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2IJK7.
OMA	EAFDTMR.
Enzyme and pathway databases
BioCyc	ADEH290397:ADEH_2070-MON.
Family and domain databases
HAMAP	MF_01033. [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_ANADE

Accession

Primary (citable) accession number: Q2IJK7

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2006
Last sequence update:	March 7, 2006
Last modified:	November 3, 2009
This is version 28 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)