Reviewed, UniProtKB/Swiss-Prot Q5HS77 (LEU3_CAMJR)

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:	CJE1888

Organism

Campylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]

Taxonomic identifier

195099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	358 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. 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 – 358	358	3-isopropylmalate dehydrogenase HAMAP MF_01033		PRO_0000083676
Regions
	Nucleotide binding	77 – 90	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	98	1	Substrate By similarity
	Binding site	108	1	Substrate By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	221	1	Substrate By similarity
	Site	144	1	Important for catalysis By similarity
	Site	189	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5HS77-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 037F612953AA7A8A	FASTA	358	39,362
	10 20 30 40 50 60 MKAYKVAVLA GDGIGPLVMK EALKILTFIS QKYNFSFEFN EAKIGGASID AYGVALSDET 70 80 90 100 110 120 LKLCEQSDAI LFGSVGGPKW DNLPIDQRPE RASLLPLRKH FNLFANLRPC KIYESLTHAS 130 140 150 160 170 180 PLKNEIIQKG VDILCVRELT GGIYFGKQDL GKESAYDTEI YTKKEIERIA HIAFESARIR 190 200 210 220 230 240 KKKVHLIDKA NVLASSILWR EVVANVVKDY QDINLEYMYV DNAAMQIVKN PSIFDVMLCS 250 260 270 280 290 300 NLFGDILSDE LAAINGSLGL LSSASLNDKG FGLYEPAGGS APDIAHLNIA NPIAQILSAA 310 320 330 340 350 LMLKYSFKEE QAAQDIENAI SLALAQGKMT KDLNAKSYLN TDEMGDCILE ILKENNNG

References

[1]

"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species." Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. , Badger J.H., Fraser C.M., Nelson K.E. PLoS Biol. 3:72-85(2005) [PubMed: 15660156] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000025 Genomic DNA. Translation: AAW34488.1.
RefSeq	YP_179858.1.
3D structure databases
SMR	Q5HS77. Positions 2-355.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5HS77.
Genome annotation databases
GeneID	3230647.
GenomeReviews	Gene locus CJE1888 in contig CP000025_GR.
KEGG	cjr:CJE1888.
NMPDR	fig|195099.3.peg.1828.
TIGR	CJE1888.
Phylogenomic databases
eggNOG	COG0473.
HOGENOM	HBG518924.
OMA	DINLEYM.
Enzyme and pathway databases
BioCyc	CJEJ195099:CJE_1888-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_CAMJR

Accession

Primary (citable) accession number: Q5HS77

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	February 15, 2005
Last modified:	February 9, 2010
This is version 36 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)