3-isopropylmalate dehydrogenase - Ashbya gossypii (Yeast)

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Reviewed, UniProtKB/Swiss-Prot O60027 (LEU3_ASHGO)

Last modified June 16, 2009. Version 60. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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:	AAL012C

Organism

Ashbya gossypii (Yeast) (Eremothecium gossypii) [Complete proteome]

Taxonomic identifier

33169 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium

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Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 372

372

3-isopropylmalate dehydrogenase

PRO_0000083598

Regions

Nucleotide binding

79 – 90

NAD By similarity

Nucleotide binding

289 – 300

NAD By similarity

Sites

Metal binding

225

Magnesium or manganese By similarity

Metal binding

250

Magnesium or manganese By similarity

Metal binding

254

Magnesium or manganese By similarity

Binding site

Substrate By similarity

Binding site

107

Substrate By similarity

Binding site

136

Substrate By similarity

Binding site

225

Substrate By similarity

Site

143

Important for catalysis By similarity

Site

192

Important for catalysis By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

O60027-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 84C96C221B0C438D
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FASTA

372

39,309

        10         20         30         40         50         60 
MAAVKRIVVL PGDHIGREVV EEAVKVLGAV EQSLSDVHFD FQYHLVGGAA IDATGSALPD 

        70         80         90        100        110        120 
EALGAAKEAD AVLLGAVGGP KWQGGAVRPE QGLLKLRQEL GVYANLRPCN FAADSLLELS 

       130        140        150        160        170        180 
PLRPEIARDT DIMVVRELLG GSYFGERHED EGDGVAWDTD KYTVKEVQRI ARMAGFLALQ 

       190        200        210        220        230        240 
HDPPLPVWSL DKANVLASSR LWRKTVEETF QSEFPNVQLQ HQLIDSAAMI LVKNPRAFNG 

       250        260        270        280        290        300 
VVVTSNMFGD IISDEASVIP GSLGLLPSAS LASLPDSKSA FGLYEPCHGS APDLPAGKAN 

       310        320        330        340        350        360 
PIGCILSAAM MLKLSLNMVA AGEAVEQAVQ EVLDSGVRTG DLLGSSSTSE VGDAIALAVK 

       370 
EALRRQSAAG LS

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of the Ashbya gossypii LEU2 gene and its use as a marker gene in transformation experiments." Mohr C., Philippsen P. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10895 / NRRL Y-1056 / CBS 109.51.
[2]	"AgLEU2 gene." Revuelta J.L. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10895 / NRRL Y-1056 / CBS 109.51.
[3]	"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed: 15001715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / NRRL Y-1056 / CBS 109.51.

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Cross-references

Sequence databases
	AJ006406 Genomic DNA. Translation: CAA07006.1. AJ001115 Genomic DNA. Translation: CAA04541.1. AE016814 Genomic DNA. Translation: AAS50354.1.
RefSeq	NP_982530.1.
3D structure databases
HSSP	HSSP built from PDB template 2AYQ based on UniProtKB P12010.
ModBase	Search...
Genome annotation databases
GeneID	4618651.
KEGG	ago:AGOS_AAL012C.
NMPDR	fig\|33169.1.peg.175.
Organism-specific databases
AGD	AAL012C.
Phylogenomic databases
HOGENOM	O60027.
OMA	O60027. LPGDHIG.
Enzyme and pathway databases
BioCyc	AGOS-XXX-01:AGOS-XXX-01-000175-MON.
BRENDA	1.1.1.85. 279361.
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...

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Entry information

Entry name

LEU3_ASHGO

Accession

Primary (citable) accession number: O60027

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	August 1, 1998
Last modified:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents