Reviewed, UniProtKB/Swiss-Prot Q8G500 (LEU3_BIFLO)

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:	BL1218

Organism

Bifidobacterium longum [Complete proteome] [HAMAP]

Taxonomic identifier

216816 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length	343 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	CytoplasmBy similarity.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 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 – 343	343	3-isopropylmalate dehydrogenase		PRO_0000083794
Regions
	Nucleotide binding	278 – 290	13	NAD By similarity
Sites
	Metal binding	218	1	Magnesium or manganese By similarity
	Metal binding	242	1	Magnesium or manganese By similarity
	Metal binding	246	1	Magnesium or manganese By similarity
	Binding site	94	1	Substrate By similarity
	Binding site	104	1	Substrate By similarity
	Binding site	128	1	Substrate By similarity
	Binding site	218	1	Substrate By similarity
	Site	135	1	Important for catalysis By similarity
	Site	185	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8G500-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 143417C91B926D30	FASTA	343	37,246
	10 20 30 40 50 60 MAKTYKIAVI PGDGIGKEVT PWAQKALEKA AEGVADFEYE NFDLGAERYL RDGAILPEDE 70 80 90 100 110 120 EERIKANDAI LLGAVGDPRI KAGILERGLL LKLRFDLDQY VNLRPSKLYK GVTSPLANPG 130 140 150 160 170 180 DIDFVVVREG TEGLYCGAGG AVRRNTPQEV ATEVSINTAY GVERVVRYAF KLAMKRKKHV 190 200 210 220 230 240 TLVHKKNVLV NAGDMWQRIV DKVGEEYPEV THDYQHIDAA TIFLVSDPSR FDVILTDNLF 250 260 270 280 290 300 GDILTDEAGS VVGGVGYSAS GCINASDEFP SMFEPIHGSA PDIAGQNKAN PTAAILSAAM 310 320 330 340 LLEHLGFDDA AKKIHTAVEA DIEELGSTVR STDQVGKDIL ARM

References

[1]

"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract." Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F. Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCC 2705.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014295 Genomic DNA. Translation: AAN25025.1.
RefSeq	NP_696389.1.
3D structure databases
HSSP	HSSP built from PDB template 1IPD based on UniProtKB P61495.
ModBase	Search...
Genome annotation databases
GeneID	1022733.
GenomeReviews	Gene locus BL1218 in contig AE014295_GR.
KEGG	blo:BL1218.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8G500.
Enzyme and pathway databases
BioCyc	BLON206672:BL1218-MON.
Family and domain databases
HAMAP	MF_01035. [Tree]
InterPro	IPR001804. IsoCit_IM_DHase. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11835. IDH_IMDH_dimeric. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
PROSITE	PS00470. IDH_IMDH. False negative. [Graphical view]
BLOCKS	Search...
ProtoNet	Search...

Entry information

Entry name

LEU3_BIFLO

Accession

Primary (citable) accession number: Q8G500

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	March 1, 2003
Last modified:	November 4, 2008
This is version 31 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)