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O13696 (IDH1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 356Isocitrate dehydrogenase [NAD] subunit 1, mitochondrialPRO_0000014430

Sites

Metal binding2241Magnesium or manganese By similarity
Binding site1061Substrate By similarity
Binding site1371Substrate By similarity
Binding site2241Substrate By similarity
Site1441Critical for catalysis By similarity
Site1911Critical for catalysis By similarity

Sequences

Sequence LengthMass (Da)Tools
O13696 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 11B482F42B467AAC

FASTA35638,758
        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

« Hide

References

« Hide '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. expand/collapse author list , 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: 972 / ATCC 24843.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAB16208.1.
PIRT37546.
RefSeqNP_594397.1. NM_001019820.1.

3D structure databases

ProteinModelPortalO13696.
SMRO13696. Positions 17-356.
ModBaseSearch...

Protein-protein interaction databases

STRINGO13696.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC11G7.03.1; SPAC11G7.03.1:pep; SPAC11G7.03.
GeneID2541894.
GenomeReviewsGene locus idh1 in contig CU329670_GR.
KEGGspo:SPAC11G7.03.
NMPDRfig|4896.1.peg.4367.

Organism-specific databases

GeneDB_SpombeSPAC11G7.03.

Phylogenomic databases

eggNOGfuNOG04063.
GeneTreeEFGT00050000002750.
HOGENOMHBG518924.
OMAARFAFDF.
OrthoDBEOG473T12.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-002502-MONOMER.

Gene expression databases

ArrayExpressO13696.

Family and domain databases

InterProIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
Gene3DG3DSA:3.40.718.10. IDH_IMDH. 1 hit.
KOK00030.
PANTHERPTHR11835. IDH_IMDH_dimeric. 1 hit.
PTHR11835:SF5. PTHR11835:SF5. 1 hit.
PfamPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR00175. Mito_nad_idh. 1 hit.
PROSITEPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIDH1_SCHPO
AccessionPrimary (citable) accession number: O13696
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 1, 1998
Last modified: December 14, 2011
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents