Reviewed, UniProtKB/Swiss-Prot Q9PLW0 (LEU3_CAMJE)

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:	Cj1718c

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [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_0000083675
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)
	Q9PLW0-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 26B811645E7FFA83	FASTA	358	39,368
	10 20 30 40 50 60 MKTYKVAVLA GDGIGPLVMK EALKILTFIA 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 RIAFESARIR 190 200 210 220 230 240 KKKVHLIDKA NVLASSILWR EVVANVAKDY 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 ILKENDNG

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL35812.1.
PIR	B81270.
RefSeq	YP_002345084.1.
3D structure databases
SMR	Q9PLW0. Positions 2-354.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PLW0. 6 interactions.
Genome annotation databases
GeneID	905995.
GenomeReviews	Gene locus Cj1718c in contig AL111168_GR.
KEGG	cje:Cj1718c.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG518924.
OMA	DINLEYM.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ1718C-MONOMER.
BRENDA	1.1.1.85. 255835.
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_CAMJE

Accession

Primary (citable) accession number: Q9PLW0
Secondary accession number(s): Q0P7R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 56 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)