P51553 (IDH3G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

IDH3G

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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

General annotation (Comments)

Catalytic activity	Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Enzyme regulation	Activated by increasing ADP/ATP ratios and by Ca2+ By similarity.
Subunit structure	Heterooligomer of subunits alpha, beta, and gamma in the apparent ratio of 2:1:1 By similarity.
Subcellular location	Mitochondrion Ref.5.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Non-traceable author statement Ref.1. Source: ProtInc isocitrate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB tricarboxylic acid cycle Traceable author statement. Source: Reactome
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome nucleolus Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NAD binding Inferred from electronic annotation. Source: InterPro isocitrate dehydrogenase (NAD+) activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 39	39	Mitochondrion By similarity
	Chain	40 – 393	354	Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial		PRO_0000014449
Regions
	Nucleotide binding	56 – 84	29	NAD Potential
	Nucleotide binding	309 – 316	8	ATP Potential
Sites
	Metal binding	254	1	Magnesium or manganese By similarity
	Binding site	136	1	Substrate By similarity
	Binding site	167	1	Substrate By similarity
	Binding site	254	1	Substrate By similarity
	Site	174	1	Critical for catalysis By similarity
	Site	221	1	Critical for catalysis By similarity
Experimental info
	Sequence conflict	267	1	F → L in AAH01902. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P51553 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: A0870F2B7D228A37	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

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[3]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta and Skin.
[5]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00220150.
RefSeq	NP_004126.1. NM_004135.3. NP_777358.1. NM_174869.2.
UniGene	Hs.410197.
3D structure databases
ProteinModelPortal	P51553.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51553. 2 interactions.
MINT	MINT-3018829.
STRING	9606.ENSP00000217901.
PTM databases
PhosphoSite	P51553.
Polymorphism databases
DMDM	1708404.
Proteomic databases
PaxDb	P51553.
PRIDE	P51553.
Protocols and materials databases
DNASU	3421.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000217901; ENSP00000217901; ENSG00000067829. ENST00000593996; ENSP00000473196; ENSG00000267989.
GeneID	3421.
KEGG	hsa:3421.
UCSC	uc004fip.3. human.
Organism-specific databases
CTD	3421.
GeneCards	GC0XM153051.
HGNC	HGNC:5386. IDH3G.
HPA	HPA000425. HPA002017.
MIM	300089. gene.
neXtProt	NX_P51553.
PharmGKB	PA29634.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0473.
HOGENOM	HOG000021113.
HOVERGEN	HBG052080.
InParanoid	P51553.
KO	K00030.
OMA	SGSERIC.
OrthoDB	EOG4M0F21.
PhylomeDB	P51553.
Enzyme and pathway databases
BioCyc	MetaCyc:ENSG00000067829-MONOMER.
Reactome	REACT_111217. Metabolism. REACT_17015. Metabolism of proteins.
SABIO-RK	P51553.
Gene expression databases
ArrayExpress	P51553.
Bgee	P51553.
CleanEx	HS_IDH3G.
Genevestigator	P51553.
GermOnline	ENSG00000067829. Homo sapiens.
Family and domain databases
Gene3D	3.40.718.10. 1 hit.
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004434. Isocitrate_DH_NAD. IPR024084. IsoPropMal-DH-like_dom. [Graphical view]
PANTHER	PTHR11835. PTHR11835. 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
DrugBank	DB00157. NADH.
GenomeRNAi	3421.
NextBio	13490.
SOURCE	Search...

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:	May 29, 2013
This is version 140 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.