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Protein

3-isopropylmalate dehydrogenase

Gene

leu1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

(2R,3S)-3-isopropylmalate + NAD+ = 4-methyl-2-oxopentanoate + CO2 + NADH.

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg2+ or Mn2+ ion per subunit.By similarity

Pathwayi: L-leucine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 2-isopropylmalate synthase (leu3)
  2. 3-isopropylmalate dehydratase (leu2)
  3. 3-isopropylmalate dehydrogenase (leu1)
  4. no protein annotated in this organism
This subpathway is part of the pathway L-leucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate, the pathway L-leucine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei96 – 961SubstrateBy similarity
Binding sitei106 – 1061SubstrateBy similarity
Binding sitei135 – 1351SubstrateBy similarity
Sitei142 – 1421Important for catalysisBy similarity
Sitei191 – 1911Important for catalysisBy similarity
Metal bindingi224 – 2241Magnesium or manganeseBy similarity
Binding sitei224 – 2241SubstrateBy similarity
Metal bindingi249 – 2491Magnesium or manganeseBy similarity
Metal bindingi253 – 2531Magnesium or manganeseBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi78 – 8912NADBy similarityAdd
BLAST
Nucleotide bindingi290 – 30213NADBy similarityAdd
BLAST

GO - Molecular functioni

  • 3-isopropylmalate dehydrogenase activity Source: PomBase
  • magnesium ion binding Source: InterPro
  • NAD binding Source: InterPro

GO - Biological processi

  • leucine biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesis

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, NAD

Enzyme and pathway databases

UniPathwayiUPA00048; UER00072.

Names & Taxonomyi

Protein namesi
Recommended name:
3-isopropylmalate dehydrogenase (EC:1.1.1.85)
Short name:
3-IPM-DH
Short name:
IMDH
Alternative name(s):
Beta-IPM dehydrogenase
Gene namesi
Name:leu1
ORF Names:SPBC1A4.02c, SPBC1E8.07c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1A4.02c.
PomBaseiSPBC1A4.02c. leu1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3713713-isopropylmalate dehydrogenasePRO_0000083618Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP18869.
PRIDEiP18869.

PTM databases

iPTMnetiP18869.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi276814. 17 interactions.
MINTiMINT-4687541.

Structurei

3D structure databases

ProteinModelPortaliP18869.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000021112.
InParanoidiP18869.
KOiK00052.
OMAiHCGPEVV.
OrthoDBiEOG092C306Q.
PhylomeDBiP18869.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR004429. Isopropylmalate_DH.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
SMARTiSM01329. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00169. leuB. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18869-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCAKKIVVLP GDHIGPEIVA SALEVLKVVE KKRPELKLEF EEHKIGGASI
60 70 80 90 100
DAYGTPLTDE TVKACLEADG VLLGAVGGPE WTNPNCRPEQ GLLKLRKSMG
110 120 130 140 150
VWANLRPCNF ASKSLVKYSP LKPEIVEGVD FCVVRELTGG CYFGERTEDN
160 170 180 190 200
GSGYAMDTWP YSLEEVSRIA RLAAWLAETS NPPAPVTLLD KANVLATSRL
210 220 230 240 250
WRKTVAKIFK EEYPHLTLKN QLIDSAAMLL VKSPRTLNGV VLTDNLFGDI
260 270 280 290 300
ISDEASVIPG SLGLLPSASL SGVVGKSEEK VHCLVEPIHG SAPDIAGKGI
310 320 330 340 350
VNPVGTILSA SLLLRYGLNA PKEAEAIEAA VRKVLDDTSI GGRGLYTRDL
360 370
GGEASTADIT KAVVEELEKI L
Length:371
Mass (Da):39,733
Last modified:November 1, 1990 - v1
Checksum:i65AA2E6AA94D45EE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36910 Genomic DNA. Translation: AAA35316.1.
CU329671 Genomic DNA. Translation: CAA16840.1.
PIRiT43407.
RefSeqiNP_595804.2. NM_001021706.3.

Genome annotation databases

EnsemblFungiiSPBC1A4.02c.1; SPBC1A4.02c.1:pep; SPBC1A4.02c.
GeneIDi2540283.
KEGGispo:SPBC1A4.02c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36910 Genomic DNA. Translation: AAA35316.1.
CU329671 Genomic DNA. Translation: CAA16840.1.
PIRiT43407.
RefSeqiNP_595804.2. NM_001021706.3.

3D structure databases

ProteinModelPortaliP18869.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276814. 17 interactions.
MINTiMINT-4687541.

PTM databases

iPTMnetiP18869.

Proteomic databases

MaxQBiP18869.
PRIDEiP18869.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1A4.02c.1; SPBC1A4.02c.1:pep; SPBC1A4.02c.
GeneIDi2540283.
KEGGispo:SPBC1A4.02c.

Organism-specific databases

EuPathDBiFungiDB:SPBC1A4.02c.
PomBaseiSPBC1A4.02c. leu1.

Phylogenomic databases

HOGENOMiHOG000021112.
InParanoidiP18869.
KOiK00052.
OMAiHCGPEVV.
OrthoDBiEOG092C306Q.
PhylomeDBiP18869.

Enzyme and pathway databases

UniPathwayiUPA00048; UER00072.

Miscellaneous databases

PROiP18869.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
IPR004429. Isopropylmalate_DH.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
SMARTiSM01329. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00169. leuB. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLEU3_SCHPO
AccessioniPrimary (citable) accession number: P18869
Secondary accession number(s): Q76PD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: September 7, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.