A0BPK2 (A0BPK2_PARTE) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Isocitrate dehydrogenase [NADP] PIRNR PIRNR000108
EC=1.1.1.42 PIRNR PIRNR000108

Gene names

ORF Names:

GSPATT00005218001 EMBL CAK60469.1, GSPATT00009194001 EMBL CAK72802.1

Organism

Paramecium tetraurelia [Reference proteome]

Taxonomic identifier

5888 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Alveolata › Ciliophora › Intramacronucleata › Oligohymenophorea › Peniculida › Parameciidae › Paramecium

Protein attributes

Sequence length	423 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH. PIRNR PIRNR000108
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity. PIRNR PIRNR000108 PIRSR PIRSR000108-3
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family. RuleBase RU004443 PIRNR PIRNR000108

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle PIRNR PIRNR000108
Ligand	Magnesium PIRNR PIRNR000108 PIRSR PIRSR000108-3 Manganese PIRNR PIRNR000108 PIRSR PIRSR000108-3 Metal-binding PIRNR PIRNR000108 PIRSR PIRSR000108-3 NADP PIRNR PIRNR000108
Molecular function	Oxidoreductase RuleBase RU004444 PIRNR PIRNR000108
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	isocitrate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro isocitrate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC 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
Regions
	Region	107 – 113	7	Substrate binding By similarity PIRSR PIRSR000108-2
Sites
	Metal binding	264	1	Magnesium or manganese By similarity PIRSR PIRSR000108-3
	Metal binding	287	1	Magnesium or manganese By similarity PIRSR PIRSR000108-3
	Binding site	90	1	Substrate By similarity PIRSR PIRSR000108-2
	Binding site	122	1	Substrate By similarity PIRSR PIRSR000108-2
	Binding site	145	1	Substrate By similarity PIRSR PIRSR000108-2
	Site	152	1	Critical for catalysis By similarity
	Site	224	1	Critical for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0BPK2 [UniParc]. Last modified November 28, 2006. Version 1. Checksum: EA4191BF7E845BF0	FASTA	423	48,091
	10 20 30 40 50 60 MSGPVFKAAA KWTGRKINVK NTVVELDGDE QARIIWKMIR ERLVLPYLNV NLEYYDLSME 70 80 90 100 110 120 HRDKTDDKVT FDSGYAILKH KVGVKCATIT ADEARVEEFK LKKMWPSPNG SIRAILDGTV 130 140 150 160 170 180 FREPIICKNI PRLVPGWTQP IVIGRHSYGD QYKCQDVKLP GPGKLELIYT PTQGEQVKRT 190 200 210 220 230 240 IFEFKGKGGV GLGMYNTYES IVNFAHQSFQ YALMRKYPLM LGTKNTILKQ YDGYFKDIFQ 250 260 270 280 290 300 EIFETKYKKD FDANKLWYEH RLIDDLVAQM MKSSGGFVLA LKNYDGDVQS DIVAQGYGSL 310 320 330 340 350 360 GMMTSELVAN DGVYESEAAH GTITRHYREH QKGKETSTNS VASIYAWTRG LRHRGRLDNN 370 380 390 400 410 420 QELIKFAETI ESSIIQTIES GLFTKDLALI VHGPKADRST YLNTEQFIDA VNGKLQSNLG FLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia." Genoscope Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R. , Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F., Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H., Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M., Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E., Cohen J., Wincker P. Nature 444:171-178(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Stock d4-2 EMBL CAK60469.1.
[2]	Genoscope Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: Stock d4-2 EMBL CAK60469.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CT868008 Genomic DNA. Translation: CAK60469.1. CT868130 Genomic DNA. Translation: CAK72802.1.
RefSeq	XP_001427867.1. XM_001427830.1. XP_001440199.1. XM_001440162.1.
UniGene	Pte.19384. Pte.59.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5013651. 5025984.
KEGG	ptm:GSPATT00005218001. ptm:GSPATT00009194001.
Phylogenomic databases
KO	K00031.
ProtClustDB	PTZ00435.
Family and domain databases
Gene3D	3.40.718.10. 1 hit.
InterPro	IPR019818. IsoCit/isopropylmalate_DH_CS. IPR004790. Isocitrate_DH_NADP. IPR024084. IsoPropMal-DH-like_dom. [Graphical view]
PANTHER	PTHR11822. PTHR11822. 1 hit.
Pfam	PF00180. Iso_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000108. IDH_NADP. 1 hit.
TIGRFAMs	TIGR00127. nadp_idh_euk. 1 hit.
PROSITE	PS00470. IDH_IMDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A0BPK2_PARTE

Accession

Primary (citable) accession number: A0BPK2

Entry history

Integrated into UniProtKB/TrEMBL:	November 28, 2006
Last sequence update:	November 28, 2006
Last modified:	April 3, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)