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F1PZA1

- F1PZA1_CANFA

UniProt

F1PZA1 - F1PZA1_CANFA

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Protein

Isocitrate dehydrogenase [NADP]

Gene

IDH1

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.UniRule annotation

Cofactori

Note: Binds 1 magnesium or manganese ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821NADPUniRule annotation
Binding sitei132 – 1321SubstrateUniRule annotation
Sitei139 – 1391Critical for catalysisUniRule annotation
Sitei212 – 2121Critical for catalysisUniRule annotation
Metal bindingi252 – 2521Magnesium or manganeseUniRule annotation
Binding sitei260 – 2601NADPUniRule annotation
Metal bindingi275 – 2751Magnesium or manganeseUniRule annotation
Binding sitei328 – 3281NADP; via amide nitrogen and carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi75 – 773NADPUniRule annotation
Nucleotide bindingi310 – 3156NADPUniRule annotation

GO - Molecular functioni

  1. isocitrate dehydrogenase (NADP+) activity Source: UniProtKB-EC
  2. magnesium ion binding Source: Ensembl
  3. NAD binding Source: InterPro

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: Ensembl
  2. glutathione metabolic process Source: Ensembl
  3. isocitrate metabolic process Source: InterPro
  4. response to oxidative stress Source: Ensembl
  5. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

Tricarboxylic acid cycleUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, ManganeseUniRule annotation, Metal-bindingUniRule annotation, NADPUniRule annotation

Enzyme and pathway databases

ReactomeiREACT_182561. Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate.
REACT_244678. NADPH regeneration.

Names & Taxonomyi

Protein namesi
Recommended name:
Isocitrate dehydrogenase [NADP]UniRule annotation (EC:1.1.1.42UniRule annotation)
Gene namesi
Name:IDH1Imported
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)Imported
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Chromosome 37

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. mitochondrion Source: Ensembl
  4. peroxisome Source: Ensembl
Complete GO annotation...

Family & Domainsi

Sequence similaritiesi

Belongs to the isocitrate and isopropylmalate dehydrogenases family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000012547.
InParanoidiF1PZA1.
KOiK00031.
OMAiCVNTVET.
OrthoDBiEOG7QNVKS.
TreeFamiTF300428.

Family and domain databases

Gene3Di3.40.718.10. 1 hit.
InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]
PANTHERiPTHR11822. PTHR11822. 1 hit.
PfamiPF00180. Iso_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsiTIGR00127. nadp_idh_euk. 1 hit.
PROSITEiPS00470. IDH_IMDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

F1PZA1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSQKIRGGSV VEMQGDEMTR IIWELIKEKL IFPYVELDLH SYDLGIENRD
60 70 80 90 100
ATNDQVTKDA AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR
110 120 130 140 150
NILGGTVFRE AIICKNIPRL VSGWVKPIII GRHAYGDQYR ATDFVVPGPG
160 170 180 190 200
KVEITYTPSD GSEKMTYLVH NFEEGGGVAM GMYNQDKSIE DFAHSSFQMA
210 220 230 240 250
LSKSWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE AQNIWYEHRL
260 270 280 290 300
IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG
310 320 330 340 350
KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWTRGL AHRAKLDNNK
360 370 380 390 400
ELSFFAKALE EVCVETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK
410
LGENLNIKLA QAKL
Length:414
Mass (Da):46,807
Last modified:May 3, 2011 - v1
Checksum:i9B607A90F0C7F387
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03018076 Genomic DNA. No translation available.
RefSeqiXP_536047.2. XM_536047.4.

Genome annotation databases

EnsembliENSCAFT00000021588; ENSCAFP00000020046; ENSCAFG00000013617.
GeneIDi478889.
KEGGicfa:478889.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAEX03018076 Genomic DNA. No translation available.
RefSeqi XP_536047.2. XM_536047.4.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSCAFT00000021588 ; ENSCAFP00000020046 ; ENSCAFG00000013617 .
GeneIDi 478889.
KEGGi cfa:478889.

Organism-specific databases

CTDi 3417.

Phylogenomic databases

GeneTreei ENSGT00390000012547.
InParanoidi F1PZA1.
KOi K00031.
OMAi CVNTVET.
OrthoDBi EOG7QNVKS.
TreeFami TF300428.

Enzyme and pathway databases

Reactomei REACT_182561. Abnormal conversion of 2-oxoglutarate to 2-hydroxyglutarate.
REACT_244678. NADPH regeneration.

Miscellaneous databases

NextBioi 20854158.

Family and domain databases

Gene3Di 3.40.718.10. 1 hit.
InterProi IPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view ]
PANTHERi PTHR11822. PTHR11822. 1 hit.
Pfami PF00180. Iso_dh. 1 hit.
[Graphical view ]
PIRSFi PIRSF000108. IDH_NADP. 1 hit.
TIGRFAMsi TIGR00127. nadp_idh_euk. 1 hit.
PROSITEi PS00470. IDH_IMDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence, comparative analysis and haplotype structure of the domestic dog."
    Broad Sequencing Platform
    Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R.
    , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
    Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BoxerImported.
  2. Ensembl
    Submitted (JUL-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: BoxerImported.

Entry informationi

Entry nameiF1PZA1_CANFA
AccessioniPrimary (citable) accession number: F1PZA1
Entry historyi
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: November 26, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.Imported

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3