Reviewed, UniProtKB/Swiss-Prot Q5LAB4 (LEU3_BACFN)

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:	BF3263

Organism

Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]

Taxonomic identifier

272559 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

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.
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 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 – 353	353	3-isopropylmalate dehydrogenase		PRO_0000083645
Sites
	Metal binding	219	1	Magnesium or manganese By similarity
	Metal binding	243	1	Magnesium or manganese By similarity
	Metal binding	247	1	Magnesium or manganese By similarity
	Binding site	97	1	Substrate By similarity
	Binding site	107	1	Substrate By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	219	1	Substrate By similarity
	Site	142	1	Important for catalysis By similarity
	Site	187	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5LAB4-1 [UniParc]. Last modified June 21, 2005. Version 1. Checksum: 355259EA221F4A84	FASTA	353	39,098
	10 20 30 40 50 60 MDFKIAVLAG DGIGPEISVQ GVEVMSAVCE KFGHKVNYEY AICGADAIDK VGDPFPEETY 70 80 90 100 110 120 RVCKNADAVL FSAVGDPKFD NDPTAKVRPE QGLLAMRKKL GLFANIRPVQ TFKCLVHKSP 130 140 150 160 170 180 LRAELVEGAD FLCIRELTGG MYFGEKYQDN DKAYDTNMYT RPEIERILKV GFEYAMKRRK 190 200 210 220 230 240 HLTVVDKANV LASSRLWRQI AQEMAPQYPE VTTDYMFVDN AAMKMIQEPK FFDVMVTENT 250 260 270 280 290 300 FGDILTDEGS VISGSMGLLP SASTGESTPV FEPIHGSWPQ AKGLNIANPL AQILSVAMLF 310 320 330 340 350 EYFDCKAEGA LIRKAVDASL DANVRTPEIQ VEGGEKFGTK EVGAWIVDYI RKA

References

[1]

"Extensive DNA inversions in the B. fragilis genome control variable gene expression." Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A. , Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J. Science 307:1463-1465(2005) [PubMed: 15746427] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR626927 Genomic DNA. Translation: CAH08959.1.
RefSeq	YP_212877.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3287842.
GenomeReviews	Gene locus BF3263 in contig CR626927_GR.
KEGG	bfs:BF3263.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5LAB4.
Enzyme and pathway databases
BioCyc	BFRA272559:BF3263-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

LEU3_BACFN

Accession

Primary (citable) accession number: Q5LAB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	June 21, 2005
Last modified:	November 4, 2008
This is version 27 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)