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Protein

Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial

Gene

idh1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH.

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 1 Mg(2+) or Mn2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061SubstrateBy similarity
Binding sitei137 – 1371SubstrateBy similarity
Sitei144 – 1441Critical for catalysisBy similarity
Sitei191 – 1911Critical for catalysisBy similarity
Metal bindingi224 – 2241Magnesium or manganeseBy similarity
Binding sitei224 – 2241SubstrateBy similarity

GO - Molecular functioni

  1. isocitrate dehydrogenase (NAD+) activity Source: PomBase
  2. magnesium ion binding Source: InterPro
  3. NAD binding Source: InterPro
  4. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. glutamate biosynthetic process Source: PomBase
  2. isocitrate metabolic process Source: PomBase
  3. tricarboxylic acid cycle Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, NAD, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_276964. Citric acid cycle (TCA cycle).

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial (EC:1.1.1.41)
Alternative name(s):
Isocitric dehydrogenase
NAD(+)-specific ICDH
Gene namesi
Name:idh1
ORF Names:SPAC11G7.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

PomBaseiSPAC11G7.03.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. mitochondrial matrix Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 356Isocitrate dehydrogenase [NAD] subunit 1, mitochondrialPRO_0000014430
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiO13696.
PaxDbiO13696.
PRIDEiO13696.

Interactioni

Subunit structurei

Octamer of two non-identical subunits IDH1 and IDH2.By similarity

Protein-protein interaction databases

BioGridi278384. 4 interactions.
MINTiMINT-4667242.
STRINGi4896.SPAC11G7.03-1.

Structurei

3D structure databases

ProteinModelPortaliO13696.
SMRiO13696. Positions 17-356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0473.
HOGENOMiHOG000021113.
InParanoidiO13696.
KOiK00030.
OMAiKGQNTAN.
OrthoDBiEOG75XGWZ.
PhylomeDBiO13696.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00175. mito_nad_idh. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O13696-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKSLVRKSS AFQPLKYGGK YTVTLIPGDG IGRETSNAVT EIFKTANVPI
60 70 80 90 100
EFEEIDVTGM EKNNKSSGDA LHEAIQSLKR NKVGLKGILF TPFEKGGHTS
110 120 130 140 150
FNVALRKELD IYASLVLIKN IPGFKTRHDN VDFAIIRENT EGEYSGLEHQ
160 170 180 190 200
SVPGVVESLK IITEYKSKRI AQFAFDFALQ NGRKSVTCIH KANIMKLADG
210 220 230 240 250
LFRRTFYDVA NGYDAITPKD LIVDNASMQA VSRPQQFDVL VMPNLYGSIL
260 270 280 290 300
SNIGSALVGG PGVIPGANFG RDYALFEPGC RHVGLSITGR GEANPTAAIL
310 320 330 340 350
SACLMLRHLG LKDYADLINA ATYSVIEEGK TLTKDLGGSA STGDFTHAIL

ERMESL
Length:356
Mass (Da):38,758
Last modified:January 1, 1998 - v1
Checksum:i11B482F42B467AAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16208.1.
PIRiT37546.
RefSeqiNP_594397.1. NM_001019820.2.

Genome annotation databases

EnsemblFungiiSPAC11G7.03.1; SPAC11G7.03.1:pep; SPAC11G7.03.
GeneIDi2541894.
KEGGispo:SPAC11G7.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16208.1.
PIRiT37546.
RefSeqiNP_594397.1. NM_001019820.2.

3D structure databases

ProteinModelPortaliO13696.
SMRiO13696. Positions 17-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278384. 4 interactions.
MINTiMINT-4667242.
STRINGi4896.SPAC11G7.03-1.

Proteomic databases

MaxQBiO13696.
PaxDbiO13696.
PRIDEiO13696.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC11G7.03.1; SPAC11G7.03.1:pep; SPAC11G7.03.
GeneIDi2541894.
KEGGispo:SPAC11G7.03.

Organism-specific databases

PomBaseiSPAC11G7.03.

Phylogenomic databases

eggNOGiCOG0473.
HOGENOMiHOG000021113.
InParanoidiO13696.
KOiK00030.
OMAiKGQNTAN.
OrthoDBiEOG75XGWZ.
PhylomeDBiO13696.

Enzyme and pathway databases

ReactomeiREACT_276964. Citric acid cycle (TCA cycle).

Miscellaneous databases

NextBioi20802981.
PROiO13696.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERiPTHR11835. PTHR11835. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00175. mito_nad_idh. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2001) [PubMed] [Europe PMC] [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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.

Entry informationi

Entry nameiIDH1_SCHPO
AccessioniPrimary (citable) accession number: O13696
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 1, 1998
Last modified: April 1, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.