Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial precursor

Contribute

Send feedback

Reviewed, UniProtKB/Swiss-Prot P70404 (IDH3G_MOUSE)

Last modified November 25, 2008. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

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

Hide | Top

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial
    EC=1.1.1.41
Alternative name(s):
    Isocitric dehydrogenase
    NAD(+)-specific ICDH

Gene names

Name:

Idh3g

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Catalytic activity	Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH.
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Enzyme regulation	Activated by increasing ADP/ATP ratios and by Ca(2+) By similarity.
Subunit structure	Heterooligomer of subunits alpha, beta, and gamma in the apparent ratio of 2:1:1 By similarity.
Subcellular location	Mitochondrion.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Hide | Top

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Magnesium Manganese Metal-binding NAD Nucleotide-binding
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	isocitrate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW isocitrate dehydrogenase (NAD+) activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 39

Mitochondrion By similarity

Chain

40 – 393

354

Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial

PRO_0000014451

Regions

Nucleotide binding

56 – 84

NAD Potential

Nucleotide binding

309 – 316

ATP Potential

Sites

Metal binding

254

Magnesium or manganese By similarity

Binding site

136

Substrate By similarity

Binding site

167

Substrate By similarity

Binding site

254

Substrate By similarity

Site

174

Critical for catalysis By similarity

Site

221

Critical for catalysis By similarity

Amino acid modifications

Modified residue

363

Phosphothreonine

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P70404-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 4023560C44C1F4D3
Show »

FASTA

393

42,785

        10         20         30         40         50         60 
MALKVAIAAG GAAKAMLKPT LLCRPWEVLA AHVAPRRSIS SQQTIPPSAK YGGRHTVTMI 

        70         80         90        100        110        120 
PGDGIGPELM LHVKSVFRHA CVPVDFEEVH VSSNADEEDI RNAIMAIRRN RVALKGNIET 

       130        140        150        160        170        180 
NHNLPPSHKS RNNILRTSLD LYANVIHCKS LPGVVTRHKD IDILIVRENT EGEYSSLEHE 

       190        200        210        220        230        240 
SVAGVVESLK IITKAKSLRI AEYAFKLAQE SGRKKVTAVH KANIMKLGDG LFLQCCREVA 

       250        260        270        280        290        300 
AHYPQITFDS MIVDNTTMQL VSRPQQFDVM VMPNLYGNIV NNVCAGLVGG PGLVAGANYG 

       310        320        330        340        350        360 
HVYAVFETAT RNTGKSIANK NIANPTATLL ASCMMLDHLK LHSYATSIRK AVLASMDNEN 

       370        380        390 
MHTPDIGGQG TTSQAIQDII RHIRIINGRA VEA

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic organization of two novel genes on human Xq28: compact head to head arrangement of IDH gamma and TRAP delta is conserved in rat and mouse." Brenner V., Nyakatura G., Rosenthal A., Platzer M. Genomics 44:8-14(1997) [PubMed: 9286695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Comparative sequence analysis of the mouse L1cam locus and the corresponding region of human Xq28." Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A., Rosenthal A. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 102-108; 116-129; 150-190 AND 227-237, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[4]	"Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed: 15572359] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-363, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases
	U68564 mRNA. Translation: AAC53340.1. AF133093 Genomic DNA. No translation available.
RefSeq	NP_032349.1.
UniGene	Mm.14825
3D structure databases
HSSP	HSSP built from PDB template 1OSJ based on UniProtKB P00351.
ModBase	Search...
PTM databases
PhosphoSite	P70404.
Genome annotation databases
Ensembl	ENSMUSG00000002010. Mus musculus. [Contig view]
GeneID	15929.
KEGG	mmu:15929.
Organism-specific databases
MGI	MGI:1099463. Idh3g.
Phylogenomic databases
HOGENOM	P70404.
HOVERGEN	P70404.
Gene expression databases
ArrayExpress	P70404.
CleanEx	MM_IDH3G.
GermOnline	ENSMUSG00000002010. Mus musculus.
Family and domain databases
InterPro	IPR004434. IsoCit_DHase_NAD_mit. IPR001804. IsoCit_IM_DHase. [Graphical view]
Gene3D	G3DSA:3.40.718.10. IDH_IMDH. 1 hit.
PANTHER	PTHR11835. IDH_IMDH_dimeric. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR00175. mito_nad_idh. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	288644.
SOURCE	Search...

Hide | Top

Entry information

Entry name

IDH3G_MOUSE

Accession

Primary (citable) accession number: P70404

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	November 25, 2008
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents