Reviewed, UniProtKB/Swiss-Prot Q01987 (LEU3_CANBO)

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 boidinii (Yeast)

Taxonomic identifier

5477 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	365 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	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: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	3-isopropylmalate dehydrogenase activity 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 – 365	365	3-isopropylmalate dehydrogenase		PRO_0000083602
Regions
	Nucleotide binding	80 – 91	12	NAD By similarity
	Nucleotide binding	290 – 301	12	NAD By similarity
Sites
	Metal binding	226	1	Magnesium or manganese By similarity
	Metal binding	251	1	Magnesium or manganese By similarity
	Metal binding	255	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	226	1	Substrate By similarity
	Site	144	1	Important for catalysis By similarity
	Site	193	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q01987-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: D3B0B89858653BCF	FASTA	365	39,124
	10 20 30 40 50 60 MSIIEKKIVL LPGDHVGVEV VEEAVKILKS ISEVKPEIQF KFENHLIGGA AIDATGVPLP 70 80 90 100 110 120 DEALEAAKKS DAVLLGAVGG PKWGTGEVRP EQGLLKIRKE LNLYANLRPC NFASDKLLDL 130 140 150 160 170 180 SPLKSDIVKG TDFTVVRELV GGIYFGDRVE DDGSGFASDS ESYSVPEVER ITRMAAFLSL 190 200 210 220 230 240 QNDPPLPIWS LDKANVLASS RLWRKTVDRV IKEEFPKLTV QHQLIDSAAM ILVKSPTKLN 250 260 270 280 290 300 GIVITNNMFG DIISDEASVI PGSLGLLPSA SLASLPDTNQ AFGLYEPCHG SAPDLPKNKV 310 320 330 340 350 360 NPIATILSAA MMLKLSLNLV KEGNAVEEAV RKVLDQGIMT GDLGGNNSTT EVGDAIAKEV KLLLA

References

[1]

"Directed mutagenesis in an asporogenous methylotrophic yeast: cloning, sequencing, and one-step gene disruption of the 3-isopropylmalate dehydrogenase gene (LEU2) of Candida boidinii to derive doubly auxotrophic marker strains." Sakai Y., Tani Y. J. Bacteriol. 174:5988-5993(1992) [PubMed: 1522074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M98832 Genomic DNA. Translation: AAA34349.1.
PIR	A43324.
3D structure databases
HSSP	HSSP built from PDB template 2AYQ based on UniProtKB P12010.
ModBase	Search...
Family and domain databases
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_CANBO

Accession

Primary (citable) accession number: Q01987

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	November 25, 2008
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)