Reviewed, UniProtKB/Swiss-Prot Q479H7 (LEU32_DECAR)

Names and origin

Protein names

Recommended name:
    3-isopropylmalate dehydrogenase 2
    EC=1.1.1.85
Alternative name(s):
    Beta-IPM dehydrogenase 2
      Short name=IMDH 2
    3-IPM-DH 2

Gene names

Name:	leuB2
Ordered Locus Names:	Daro_3775

Organism

Dechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]

Taxonomic identifier

159087 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Dechloromonas

Protein attributes

Sequence length	358 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. HAMAP MF_01033
Catalytic activity	(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO(2) + 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	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 – 358	358	3-isopropylmalate dehydrogenase 2 HAMAP MF_01033		PRO_0000083684
Regions
	Nucleotide binding	74 – 87	14	NAD By similarity
	Nucleotide binding	279 – 291	13	NAD By similarity
Sites
	Metal binding	221	1	Magnesium or manganese By similarity
	Metal binding	245	1	Magnesium or manganese By similarity
	Metal binding	249	1	Magnesium or manganese By similarity
	Binding site	94	1	Substrate By similarity
	Binding site	104	1	Substrate By similarity
	Binding site	132	1	Substrate By similarity
	Binding site	221	1	Substrate By similarity
	Site	139	1	Important for catalysis By similarity
	Site	189	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q479H7-1 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: CA577A4C48616AAB	FASTA	358	38,855
	10 20 30 40 50 60 MKICVIPGDG IGVEICAEAV RVIDALKDIH GLKIEYEYGL LGGAAYDQTG RPLPVETLRL 70 80 90 100 110 120 ADEANAILLG AVGGPKWDKL PAESRPERGL LGIRKYLGLN ANLRPIKVYP ELANASTLRP 130 140 150 160 170 180 EVVSGLDMMI VRELTGDIYF GQPRGIRTSG FERVGYNTME YSESEIALIA EMAFRIARQR 190 200 210 220 230 240 SGKVMSVDKM NVLECMQLWR DVVTKVGERF PDVTLDHMLV DNAAMQLVKN PKQFDVLLTG 250 260 270 280 290 300 NMFGDILSDE AAMLTGSIGM LPSASLNVED KGMYEPCHGS APDIAGQGVA NPLGMILSAA 310 320 330 340 350 MMFRYSLGRP DMADAIESAV QTVLTNGART RDIFQAGDRL VSTSEMGGLV EAALRRIS

References

[1]

"Complete sequence of Dechloromonas aromatica RCB." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S., Kellar K., Schmutz J., Larimer F., Land M., Ivanova N., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000089 Genomic DNA. Translation: AAZ48504.1.
RefSeq	YP_286974.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3567508.
GenomeReviews	Gene locus Daro_3775 in contig CP000089_GR.
KEGG	dar:Daro_3775.
NMPDR	fig|159087.4.peg.3660.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q479H7.
Enzyme and pathway databases
BioCyc	DARO159087:DARO_3775-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

LEU32_DECAR

Accession

Primary (citable) accession number: Q479H7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	September 13, 2005
Last modified:	November 4, 2008
This is version 25 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)