Reviewed, UniProtKB/Swiss-Prot O13696 (IDH1_SCHPO)

Names and origin

Protein names

Recommended name:
    Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial
    EC=1.1.1.41
Alternative name(s):
    Isocitric dehydrogenase
    NAD(+)-specific ICDH

Gene names

Name:	idh1
ORF Names:	SPAC11G7.03

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	356 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)

Function	Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs.
Catalytic activity	Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Subunit structure	Octamer of two non-identical subunits IDH1 and IDH2 By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Magnesium Manganese Metal-binding NAD RNA-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutamate biosynthetic process Inferred from mutant phenotype. Source: GeneDB_SPombe isocitrate metabolic process Inferred from mutant phenotype. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW isocitrate dehydrogenase (NAD+) activity Ref.2 Inferred from mutant phenotype. Source: GeneDB_SPombe magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 356		Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial		PRO_0000014430
Sites
	Metal binding	224	1	Magnesium or manganese By similarity
	Binding site	106	1	Substrate By similarity
	Binding site	137	1	Substrate By similarity
	Binding site	224	1	Substrate By similarity
	Site	144	1	Critical for catalysis By similarity
	Site	191	1	Critical for catalysis By similarity

Sequences

	Sequence		Length	Mass (Da)
	O13696-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 11B482F42B467AAC	FASTA	356	38,758
	10 20 30 40 50 60 MFKSLVRKSS AFQPLKYGGK YTVTLIPGDG IGRETSNAVT EIFKTANVPI EFEEIDVTGM 70 80 90 100 110 120 EKNNKSSGDA LHEAIQSLKR NKVGLKGILF TPFEKGGHTS FNVALRKELD IYASLVLIKN 130 140 150 160 170 180 IPGFKTRHDN VDFAIIRENT EGEYSGLEHQ SVPGVVESLK IITEYKSKRI AQFAFDFALQ 190 200 210 220 230 240 NGRKSVTCIH KANIMKLADG LFRRTFYDVA NGYDAITPKD LIVDNASMQA VSRPQQFDVL 250 260 270 280 290 300 VMPNLYGSIL SNIGSALVGG PGVIPGANFG RDYALFEPGC RHVGLSITGR GEANPTAAIL 310 320 330 340 350 SACLMLRHLG LKDYADLINA ATYSVIEEGK TLTKDLGGSA STGDFTHAIL ERMESL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"Isolation and RNA-binding analysis of NAD+ -isocitrate dehydrogenases from Kluyveromyces lactis and Schizosaccharomyces pombe." Elzinga S.D.J., van Oosterum K., Maat C., Grivell L.A., van der Spek H. Curr. Genet. 38:87-94(2000) [PubMed: 10975257] [Abstract] Cited for: RNA-BINDING.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB16208.1.
PIR	T37546.
RefSeq	NP_594397.1.
3D structure databases
SMR	O13696. Positions 17-356.
ModBase	Search...
Protein-protein interaction databases
STRING	O13696.
Genome annotation databases
GeneID	2541894.
GenomeReviews	Gene locus idh1 in contig CU329670_GR.
KEGG	spo:SPAC11G7.03.
NMPDR	fig|4896.1.peg.4367.
Organism-specific databases
GeneDB_Spombe	SPAC11G7.03.
Phylogenomic databases
eggNOG	fuNOG04063.
HOGENOM	HBG518924.
OMA	TAMILSS.
OrthoDB	EOG9BK6MD.
PhylomeDB	O13696.
Enzyme and pathway databases
BRENDA	1.1.1.41. 653.
Gene expression databases
ArrayExpress	O13696.
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...

Entry information

Entry name

IDH1_SCHPO

Accession

Primary (citable) accession number: O13696

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)