Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial precursor

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Reviewed, UniProtKB/Swiss-Prot P51553 (IDH3G_HUMAN)

Last modified November 25, 2008. Version 90. 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:
    Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial
    EC=1.1.1.41
Alternative name(s):
    Isocitric dehydrogenase
    NAD(+)-specific ICDH

Gene names

Name:

IDH3G

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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 transcript level.

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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.

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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
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Ref.1 Non-traceable author statement. Source: ProtInc 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	mitochondrial matrix Inferred from Experiment. Source: Reactome nucleolus Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW isocitrate dehydrogenase (NAD+) activity Ref.1 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...

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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_0000014449

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 By similarity

Experimental info

Sequence conflict

267

F → L in AAH01902. Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P51553-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: A0870F2B7D228A37
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FASTA

393

42,794

        10         20         30         40         50         60 
MALKVATVAG SAAKAVLGPA LLCRPWEVLG AHEVPSRNIF SEQTIPPSAK 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 
ARYPQITFEN MIVDNTTMQL VSRPQQFDVM VMPNLYGNIV NNVCAGLVGG PGLVAGANYG 

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

       370        380        390 
MHTPDIGGQG TTSEAIQDVI RHIRVINGRA VEA

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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 [GENOMIC DNA / MRNA]. Tissue: Brain.
[2]	"Identification and functional characterization of a novel, tissue-specific NAD+-dependent isocitrate dehydrogenase beta subunit isoform." Kim Y.-O., Koh H.-J., Kim S.-H., Jo S.-H., Huh J.-W., Jeong K.-S., Lee I.J., Song B.J., Huh T.-L. J. Biol. Chem. 274:36866-36875(1999) [PubMed: 10601238] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta and Skin.
[4]	"Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing." Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S. EMBO Rep. 1:287-292(2000) [PubMed: 11256614] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	Z68907 mRNA. Translation: CAA93143.1. Z68129 Genomic DNA. Translation: CAA92214.1. U52111 Genomic DNA. No translation available. U40272 mRNA. Translation: AAD09357.1. BC000933 mRNA. Translation: AAH00933.1. BC001902 mRNA. Translation: AAH01902.1.
RefSeq	NP_004126.1.
UniGene	Hs.410197
3D structure databases
HSSP	HSSP built from PDB template 1XAA based on UniProtKB P00351.
ModBase	Search...
PTM databases
PhosphoSite	P51553.
Genome annotation databases
Ensembl	ENSG00000067829. Homo sapiens. [Contig view]
GeneID	3421.
KEGG	hsa:3421.
Organism-specific databases
H-InvDB	HIX0017139.
HGNC	HGNC:5386. IDH3G.
HPA	HPA000425. HPA002017.
MIM	300089. gene.
PharmGKB	PA29634.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P51553.
HOVERGEN	P51553.
Enzyme and pathway databases
Reactome	REACT_1046. Pyruvate metabolism and TCA cycle.
Gene expression databases
CleanEx	HS_IDH3G.
GermOnline	ENSG00000067829. Homo sapiens.
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
DrugBank	DB00157. NADH.
LinkHub	P51553.
NextBio	13490.
SOURCE	Search...

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Entry information

Entry name

IDH3G_HUMAN

Accession

Primary (citable) accession number: P51553
Secondary accession number(s): Q9BUU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) 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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents