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Protein

Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial

Gene

IDH3G

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.

Enzyme regulationi

Activated by increasing ADP/ATP ratios and by Ca2+.

GO - Molecular functioni

  • isocitrate dehydrogenase (NAD+) activity Source: UniProtKB
  • magnesium ion binding Source: InterPro
  • NAD binding Source: InterPro

GO - Biological processi

  • isocitrate metabolic process Source: UniProtKB
  • tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial (EC:1.1.1.41)
Alternative name(s):
Isocitric dehydrogenase subunit gamma
NAD(+)-specific ICDH subunit gamma
Gene namesi
Name:IDH3G
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›106›106Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrialPRO_0000083592Add
BLAST

Proteomic databases

PaxDbiP41566.

Interactioni

Subunit structurei

Heterooligomer of subunits alpha, beta, and gamma in the apparent ratio of 2:1:1.

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000013592.

Structurei

3D structure databases

ProteinModelPortaliP41566.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0473.
InParanoidiP41566.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.

Sequencei

Sequence statusi: Fragments.

P41566-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
FSQQTIPPSA KYGGILTVTM SPGDGDGPEL MLTVXXXXXS ACVPVDFEEV
60 70 80 90 100
VVSSNADEED IRTSLDLYAN VIHCKLGDGL FLQCCKNIAN PTATLLASCM

MLDHLK
Length:106
Mass (Da):11,334
Last modified:November 1, 1995 - v1
Checksum:iAB0A66AB845C49AB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-adjacent residuesi62 – 632Curated
Non-adjacent residuesi75 – 762Curated
Non-adjacent residuesi86 – 872Curated
Non-terminal residuei106 – 1061

Sequence databases

PIRiC35834.

Cross-referencesi

Sequence databases

PIRiC35834.

3D structure databases

ProteinModelPortaliP41566.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000013592.

Proteomic databases

PaxDbiP41566.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG0473.
InParanoidiP41566.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR001804. Isocitrate/isopropylmalate_DH.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Subunit location and sequences of the cysteinyl peptides of pig heart NAD-dependent isocitrate dehydrogenase."
    Huang Y.C., Colman R.F.
    Biochemistry 29:8266-8273(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Heart.
  2. "Cysteinyl peptide labeled by 3-bromo-2-ketoglutarate in the active site of pig heart NAD+-dependent isocitrate dehydrogenase."
    Saha A., Huang Y.C., Colman R.F.
    Biochemistry 28:8425-8431(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 40-62.
    Tissue: Heart.
  3. "Aspartyl peptide labeled by 2-(4-bromo-2,3-dioxobutylthio)adenosine 5'-diphosphate in the allosteric ADP site of pig heart NAD+-dependent isocitrate dehydrogenase."
    Huang Y.C., Colman R.F.
    J. Biol. Chem. 264:12208-12214(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 76-86.
    Tissue: Heart.

Entry informationi

Entry nameiIDH3G_PIG
AccessioniPrimary (citable) accession number: P41566
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.