Reviewed, UniProtKB/Swiss-Prot Q1QUR0 (LEU3_CHRSD)

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:	Csal_2451

Organism

Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]

Taxonomic identifier

290398 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Halomonadaceae › Chromohalobacter

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 By similarity. 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_0000250112
Regions
	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)
	Q1QUR0-1 [UniParc]. Last modified September 19, 2006. Version 2. Checksum: A6569DD652F0CF1B	FASTA	359	38,363
	10 20 30 40 50 60 MSRKILVLPG DGIGPEITRE AVKILNACRE AGLEASIEEG LVGGAGIDAH GVPLPDETLA 70 80 90 100 110 120 SAKAADAVLL GAVGGPQWDK IEDLSKRPEK GLLGLRKNLN LFGNLRPALL YPQLASASSL 130 140 150 160 170 180 KPEIVAGLDI MIVRELTGGI YFGQPRGIEE RDGERVGYNT YIYAEHEIER IGRVAFEMAR 190 200 210 220 230 240 ERGGKLCSVD KANVLEATIL WREVMERLAP EYPDVALSHM YVDNAAMQLV RAPKQFDVIV 250 260 270 280 290 300 TGNMFGDILS DAAAMLTGSI GMLPSASLNE QRQGMYEPCH GSAPDIAGQG IANPLATILS 310 320 330 340 350 VAMMLRYSLE APQLAERIER AVGTVLDQGL RTADIAFEGT APVSTQAMGD AVLAAFQAQ

References

[1]

"Complete sequence of Chromohalobacter salexigens DSM 3043." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., Canovas D., Richardson P. Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000285 Genomic DNA. Translation: ABE59798.1. Different initiation.
RefSeq	YP_574497.1.
3D structure databases
SMR	Q1QUR0. Positions 3-356.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1QUR0.
Genome annotation databases
GeneID	4026971.
GenomeReviews	Gene locus Csal_2451 in contig CP000285_GR.
KEGG	csa:Csal_2451.
NMPDR	fig|290398.4.peg.3092.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0473.
HOGENOM	HBG518924.
Enzyme and pathway databases
BioCyc	CSAL290398:CSAL_2451-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_CHRSD

Accession

Primary (citable) accession number: Q1QUR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2006
Last sequence update:	September 19, 2006
Last modified:	February 9, 2010
This is version 28 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)