Reviewed, UniProtKB/Swiss-Prot Q9HDQ5 (LEU3_CANRU)

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 rugosa (Yeast) (Candida cylindracea)

Taxonomic identifier

5481 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	359 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 – 359	359	3-isopropylmalate dehydrogenase		PRO_0000083606
Regions
	Nucleotide binding	77 – 88	12	NAD By similarity
	Nucleotide binding	287 – 298	12	NAD By similarity
Sites
	Metal binding	223	1	Magnesium or manganese By similarity
	Metal binding	248	1	Magnesium or manganese By similarity
	Metal binding	252	1	Magnesium or manganese By similarity
	Binding site	95	1	Substrate By similarity
	Binding site	105	1	Substrate By similarity
	Binding site	134	1	Substrate By similarity
	Binding site	223	1	Substrate By similarity
	Site	141	1	Important for catalysis By similarity
	Site	190	1	Important for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9HDQ5-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 1E888608B8C732F0	FASTA	359	37,728
	10 20 30 40 50 60 MSKSIVLLPG DHVGTEVVAE AVKVLKAIER TTPGTSFSFS THLIGGAAID ATGVPLPDEA 70 80 90 100 110 120 LEAAKASDAV LLGAVGGPKW GTGDVRPEQG LLKIRKELGL YANLRPCSFA SSKLVDLSPL 130 140 150 160 170 180 KREIVEGTDF VVVRELVGGI YFGERKEDDG SGVASDTETY SVPEVERITR MAAFLALQHN 190 200 210 220 230 240 PPQTVWSLDK ANVLASSRLW RKTVTRVMTE EFPTVPFQHQ LIDSAAMILV QKPTKLNGVV 250 260 270 280 290 300 LTSNMFGDII SDEASVIPGS LGLLPSASLA SLPDTNTAFG LYEPCHGSAP DLPAGKVNPL 310 320 330 340 350 ACILSAAMML RLSLDNAAAA DRIEQAVREV IDSGVATADL GGSSSTGEVG DAIVKALEK

References

[1]	Biasio W. Thesis (2000), University of Vienna, Austria Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 14830 / CBS 6330 / DSM 2031 / MS-5 / NRRL Y-17506.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ279020 Genomic DNA. Translation: CAC10274.1.
3D structure databases
SMR	Q9HDQ5. Positions 1-358.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.85. 3604.
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_CANRU

Accession

Primary (citable) accession number: Q9HDQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	March 1, 2001
Last modified:	February 9, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)