Reviewed, UniProtKB/Swiss-Prot O14429 (LEU3_CANGA)

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
Ordered Locus Names:	CAGL0H03795g

Organism

Candida glabrata (Yeast) (Torulopsis glabrata) [Complete proteome]

Taxonomic identifier

5478 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces

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 + 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
Technical term	Complete proteome
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 – 365	365	3-isopropylmalate dehydrogenase		PRO_0000083603
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
Experimental info
	Sequence conflict	10	1	L → P in AAB62089. Ref.1
	Sequence conflict	24	1	I → N in AAB62089. Ref.1
	Sequence conflict	51	1	A → P in AAB62089. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O14429-1 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: 05D59E0986360B82	FASTA	365	39,305
	10 20 30 40 50 60 MAVTKTIVVL PGDHVGQEIT EEAIKVLNAI QECRPDKVNF KFDHHLIGGA AIDATGVPLP 70 80 90 100 110 120 DEALEASKKA DAVLLGAVGG PKWGTGAVRP EQGLLKIRKE LQLYANLRPC NFASDSLLDL 130 140 150 160 170 180 SPLKPEIARG TDFVVVRELV GGIYFGERKE DEGDGVAWDS EKYSVPEVQR ITRMAAFMAL 190 200 210 220 230 240 QHNPPLPIWS LDKANVLASS RLWRKTVEET IKNEFPQLTV QHQLIDSAAM ILVKNPTHLN 250 260 270 280 290 300 GIIITNNMFG DIISDEASVI PGSLGLLPSA SLASLPDKNT AFGLYEPCHG SAPDLPKGKV 310 320 330 340 350 360 NPVATILSAA MMLKLSLDLF EEGEIIEQAV KKVLDSGIRT ADLKGTNSTT EVGDAVAKAV RELLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Kitada K. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.
[2]	"Genome evolution in yeasts." Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L. Nature 430:35-44(2004) [PubMed: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 2001 / CBS 138 / IFO 0622 / NRRL Y-65.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U90626 Genomic DNA. Translation: AAB62089.1. CR380954 Genomic DNA. Translation: CAG59892.1.
RefSeq	XP_446959.1.
3D structure databases
HSSP	HSSP built from PDB template 2AYQ based on UniProtKB P12010.
ModBase	Search...
Genome annotation databases
GeneID	2888798.
KEGG	cgr:CAGL0H03795g.
Phylogenomic databases
HOGENOM	O14429.
OMA	O14429. NTAFGLY.
Enzyme and pathway databases
BRENDA	1.1.1.85. 189220.
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_CANGA

Accession

Primary (citable) accession number: O14429
Secondary accession number(s): Q6FS35

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	August 16, 2004
Last modified:	June 16, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)