Reviewed, UniProtKB/Swiss-Prot P07139 (LEU3_CANMA)

Names and origin

Protein names

Recommended name:
    3-isopropylmalate dehydrogenase
      Short name=3-IPM-DH
      Short name=IMDH
    EC=1.1.1.85
Alternative name(s):
    Beta-IPM dehydrogenase

Gene names

Name:

LEU2

Organism

Candida maltosa (Yeast)

Taxonomic identifier

5479 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	373 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.
Catalytic activity	(2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + 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	Cytoplasm.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

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
Gene Ontology (GO)
Biological process	leucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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: EC 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 – 373	373	3-isopropylmalate dehydrogenase		PRO_0000083604
Regions
	Nucleotide binding	82 – 93	12	NAD By similarity
	Nucleotide binding	295 – 306	12	NAD By similarity
Sites
	Metal binding	231	1	Magnesium or manganese By similarity
	Metal binding	256	1	Magnesium or manganese By similarity
	Metal binding	260	1	Magnesium or manganese By similarity
	Binding site	100	1	Substrate By similarity
	Binding site	110	1	Substrate By similarity
	Binding site	139	1	Substrate By similarity
	Binding site	231	1	Substrate By similarity
	Site	146	1	Important for catalysis By similarity
	Site	198	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	P07139-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 256E9886219BA529	FASTA	373	40,173
	10 20 30 40 50 60 MSVKTKTITI LPGDHVGTEI VNEAIKVLEA IEAATPYQKI HFDFKHHLIG GAAIDATGVP 70 80 90 100 110 120 LPDDALESAK NSDAVLLGAV GGPKWGTGAL RPEQGLLKIR KELNLYANIR PCNFASDSLL 130 140 150 160 170 180 ELSPLRPEVV KGTNLIIVRE LVGGIYFGDR EEQEESADKQ TAWDTEKYTV DEVTRITRMA 190 200 210 220 230 240 AFMALQHTPP LPIWSLDKAN VLASSRLWRR TVDKVISEEF PTLSVQHQLI DSAAMILIQN 250 260 270 280 290 300 PTKLNGIIIT SNMFGDIISD EASVIPGSLG LLPSASLASL PDTNTAFGLY EPCHGSAPDL 310 320 330 340 350 360 PANKVNPIAT ILSAASMLRL SLDCVKEAEA LEEAVKQVLD KGIRTADLRG TSSTTEVGDA 370 IVEAVTKILK EKA

References

[1]	"Nucleotide sequencing analysis of a LEU gene of Candida maltosa which complements leuB mutation of Escherichia coli and leu2 mutation of Saccharomyces cerevisiae." Takagi M., Kobayashi N., Sugimoto M., Fujii T., Watari J., Yano K. Curr. Genet. 11:451-457(1987) [PubMed: 2897248] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Molecular analysis of a leu2-mutant of Candida maltosa demonstrates the presence of multiple alleles." Becher D., Schulze S., Kasuske A., Schulze H., Samsonova I.A., Oliver S.G. Curr. Genet. 26:208-216(1994) [PubMed: 7859302] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: G587.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X05459 Genomic DNA. Translation: CAA29024.1. X72940 Genomic DNA. Translation: CAA51445.1.
PIR	S48228.
3D structure databases
SMR	P07139. Positions 5-365.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.85. 3846.
Family and domain databases
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_CANMA

Accession

Primary (citable) accession number: P07139

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	February 9, 2010
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)