Reviewed, UniProtKB/Swiss-Prot P50213 (IDH3A_HUMAN)

Names and origin

Protein names

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

Gene names

Name:

IDH3A

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	366 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.
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.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Non-traceable author statement. Source: ProtInc oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from Experiment. Source: Reactome
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro isocitrate dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P50213-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P50213-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 27	27	Mitochondrion By similarity
	Chain	28 – 366	339	Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial		PRO_0000014436
Sites
	Metal binding	233	1	Magnesium or manganese By similarity
	Metal binding	257	1	Magnesium or manganese By similarity
	Metal binding	261	1	Magnesium or manganese By similarity
	Binding site	115	1	Substrate By similarity
	Binding site	125	1	Substrate By similarity
	Binding site	146	1	Substrate By similarity
	Binding site	233	1	Substrate By similarity
	Site	153	1	Critical for catalysis By similarity
	Site	200	1	Critical for catalysis By similarity
Amino acid modifications
	Modified residue	343	1	N6-acetyllysine Ref.6
Natural variations
	Alternative sequence	1 – 78	78	Missing in isoform 2.		VSP_014516

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 695F6A34F97430CF	FASTA	366	39,592
	10 20 30 40 50 60 MAGPAWISKV SRLLGAFHNP KQVTRGFTGG VQTVTLIPGD GIGPEISAAV MKIFDAAKAP 70 80 90 100 110 120 IQWEERNVTA IQGPGGKWMI PSEAKESMDK NKMGLKGPLK TPIAAGHPSM NLLLRKTFDL 130 140 150 160 170 180 YANVRPCVSI EGYKTPYTDV NIVTIRENTE GEYSGIEHVI VDGVVQSIKL ITEGASKRIA 190 200 210 220 230 240 EFAFEYARNN HRSNVTAVHK ANIMRMSDGL FLQKCREVAE SCKDIKFNEM YLDTVCLNMV 250 260 270 280 290 300 QDPSQFDVLV MPNLYGDILS DLCAGLIGGL GVTPSGNIGA NGVAIFESVH GTAPDIAGKD 310 320 330 340 350 360 MANPTALLLS AVMMLRHMGL FDHAARIEAA CFATIKDGKS LTKDLGGNAK CSDFTEEICR RVKDLD
	Isoform 2. Checksum: BF8327BD4AA7D3EC	FASTA	288	31,381
	10 20 30 40 50 60 MIPSEAKESM DKNKMGLKGP LKTPIAAGHP SMNLLLRKTF DLYANVRPCV SIEGYKTPYT 70 80 90 100 110 120 DVNIVTIREN TEGEYSGIEH VIVDGVVQSI KLITEGASKR IAEFAFEYAR NNHRSNVTAV 130 140 150 160 170 180 HKANIMRMSD GLFLQKCREV AESCKDIKFN EMYLDTVCLN MVQDPSQFDV LVMPNLYGDI 190 200 210 220 230 240 LSDLCAGLIG GLGVTPSGNI GANGVAIFES VHGTAPDIAG KDMANPTALL LSAVMMLRHM 250 260 270 280 GLFDHAARIE AACFATIKDG KSLTKDLGGN AKCSDFTEEI CRRVKDLD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a cDNA clone for human NAD(+)-specific isocitrate dehydrogenase alpha-subunit and structural comparison with its isoenzymes from different species." Kim Y.O., Oh I.U., Park H.S., Jeng J., Song B.J., Huh T.L. Biochem. J. 308:63-68(1995) [PubMed: 7755589] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Heart.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain cortex.
[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] (ISOFORM 1). Tissue: Lymph.
[4]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 135-146; 179-188 AND 300-316, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-343, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U07681 mRNA. Translation: AAA85639.1. AL442090 mRNA. Translation: CAC09449.1. BC021967 mRNA. Translation: AAH21967.1.
IPI	IPI00030702. IPI00792971.
PIR	S55282.
RefSeq	NP_005521.1.
UniGene	Hs.591110
3D structure databases
SMR	P50213. Positions 28-362.
ModBase	Search...
Protein-protein interaction databases
IntAct	P50213. 6 interactions.
STRING	P50213.
PTM databases
PhosphoSite	P50213.
2-D gel databases
OGP	P50213.
REPRODUCTION-2DPAGE	IPI00030702.
Proteomic databases
PRIDE	P50213.
Genome annotation databases
Ensembl	ENST00000299518; ENSP00000299518; ENSG00000166411; Homo sapiens. [Genome view]
GeneID	3419.
KEGG	hsa:3419.
NMPDR	fig|9606.3.peg.11057.
UCSC	uc002bdd.1. human. uc002bde.1. human.
Organism-specific databases
CTD	3419.
GeneCards	GC15P076228.
HGNC	HGNC:5384. IDH3A.
MIM	601149. gene.
PharmGKB	PA29632.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11254.
HOGENOM	HBG518924.
HOVERGEN	P50213.
InParanoid	P50213.
OMA	ITTFAYE.
OrthoDB	EOG9B2WGN.
PhylomeDB	P50213.
Enzyme and pathway databases
BRENDA	1.1.1.41. 247.
Reactome	REACT_1046. Pyruvate metabolism and TCA cycle. REACT_1505. Integration of energy metabolism. REACT_15380. Diabetes pathways.
Gene expression databases
ArrayExpress	P50213.
Bgee	P50213.
CleanEx	HS_IDH3A.
Genevestigator	P50213.
GermOnline	ENSG00000166411. Homo sapiens.
Family and domain databases
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR001804. Isocitrate/isopropylmalate_DH. IPR004434. Isocitrate_DH_NAD_mit. [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.
NextBio	13478.
SOURCE	Search...

Entry information

Entry name

IDH3A_HUMAN

Accession

Primary (citable) accession number: P50213
Secondary accession number(s): Q9H3X0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	February 9, 2010
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.