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Q9VWH4

- IDH3A_DROME

UniProt

Q9VWH4 - IDH3A_DROME

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Protein

Probable isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial

Gene
l(1)G0156, CG12233
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 1 magnesium or manganese ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei131 – 1311Substrate By similarity
Binding sitei141 – 1411Substrate By similarity
Binding sitei162 – 1621Substrate By similarity
Sitei169 – 1691Critical for catalysis By similarity
Sitei216 – 2161Critical for catalysis By similarity
Metal bindingi249 – 2491Magnesium or manganese By similarity
Binding sitei249 – 2491Substrate By similarity
Metal bindingi273 – 2731Magnesium or manganese By similarity
Metal bindingi277 – 2771Magnesium or manganese By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. tricarboxylic acid cycle Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, NAD

Enzyme and pathway databases

ReactomeiREACT_218888. Citric acid cycle (TCA cycle).

Names & Taxonomyi

Protein namesi
Recommended name:
Probable isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (EC:1.1.1.41)
Alternative name(s):
Isocitric dehydrogenase subunit alpha
NAD(+)-specific ICDH subunit alpha
Gene namesi
Name:l(1)G0156
ORF Names:CG12233
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0027291. l(1)G0156.

Subcellular locationi

Mitochondrion By similarity By similarity

GO - Cellular componenti

  1. lipid particle Source: FlyBase
  2. microtubule associated complex Source: FlyBase
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 377Probable isocitrate dehydrogenase [NAD] subunit alpha, mitochondrialPRO_0000014442
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Proteomic databases

PaxDbiQ9VWH4.
PRIDEiQ9VWH4.

Expressioni

Gene expression databases

BgeeiQ9VWH4.

Interactioni

Subunit structurei

Heterooligomer of subunits alpha, beta, and gamma in the apparent ratio of 2:1:1 By similarity.By similarity

Protein-protein interaction databases

BioGridi59242. 81 interactions.
MINTiMINT-898629.

Structurei

3D structure databases

ProteinModelPortaliQ9VWH4.
SMRiQ9VWH4. Positions 50-377.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0473.
InParanoidiQ9VWH4.
KOiK00030.
OMAiLIDNMCM.
OrthoDBiEOG75B85R.
PhylomeDBiQ9VWH4.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform D (identifier: Q9VWH4-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAARFIQKIL NQLGLIAARD APAVTATPAV SQVNATPAAS RSYSSGTKKV    50
TLIPGDGIGP EISAAVQKIF TAANVPIEWE AVDVTPVRGP DGKFGIPQAA 100
IDSVNTNKIG LKGPLMTPVG KGHRSLNLAL RKEFNLYANV RPCRSLEGYK 150
TLYDDVDVVT IRENTEGEYS GIEHEIVDGV VQSIKLITEE ASKRVAEYAF 200
QYAKNNNRKK VTVVHKANIM RMSDGLFLRC VRDMAQKFPE IQFEEKYLDT 250
VCLNMVQNPG KYDVLVMPNL YGDILSDMCA GLVGGLGLTP SGNMGLNGAL 300
FESVHGTAPD IAGKDLANPT ALLLSAVMML RHMELNTYAD KIERAAFETI 350
KEGKYLTGDL GGRAKCSEFT NEICAKL 377

Note: No experimental confirmation available.

Length:377
Mass (Da):40,844
Last modified:May 1, 2000 - v1
Checksum:iFB3F30905B8939B3
GO
Isoform A1 Publication (identifier: Q9VWH4-2) [UniParc]FASTAAdd to Basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MAARFIQKILNQLGLIAARDAPAVTATPAVSQ → MAARFIQKI

Note: No experimental confirmation available.

Show »
Length:354
Mass (Da):38,584
Checksum:i64426D3BE3983BB4
GO

Sequence cautioni

The sequence AAL90367.1 differs from that shown. Reason: Frameshift at position 205.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3232MAARF…PAVSQ → MAARFIQKI in isoform A. 1 PublicationVSP_050698Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014298 Genomic DNA. Translation: AAF48965.2.
AE014298 Genomic DNA. Translation: AAN09496.1.
AE014298 Genomic DNA. Translation: AGB95545.1.
AY089629 mRNA. Translation: AAL90367.1. Frameshift.
BT125839 mRNA. Translation: ADR83724.2.
RefSeqiNP_001259705.1. NM_001272776.1. [Q9VWH4-1]
NP_573388.1. NM_133160.2. [Q9VWH4-2]
NP_728257.2. NM_167657.3. [Q9VWH4-2]
UniGeneiDm.222.

Genome annotation databases

GeneIDi32940.
KEGGidme:Dmel_CG12233.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014298 Genomic DNA. Translation: AAF48965.2 .
AE014298 Genomic DNA. Translation: AAN09496.1 .
AE014298 Genomic DNA. Translation: AGB95545.1 .
AY089629 mRNA. Translation: AAL90367.1 . Frameshift.
BT125839 mRNA. Translation: ADR83724.2 .
RefSeqi NP_001259705.1. NM_001272776.1. [Q9VWH4-1 ]
NP_573388.1. NM_133160.2. [Q9VWH4-2 ]
NP_728257.2. NM_167657.3. [Q9VWH4-2 ]
UniGenei Dm.222.

3D structure databases

ProteinModelPortali Q9VWH4.
SMRi Q9VWH4. Positions 50-377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 59242. 81 interactions.
MINTi MINT-898629.

Proteomic databases

PaxDbi Q9VWH4.
PRIDEi Q9VWH4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 32940.
KEGGi dme:Dmel_CG12233.

Organism-specific databases

FlyBasei FBgn0027291. l(1)G0156.

Phylogenomic databases

eggNOGi COG0473.
InParanoidi Q9VWH4.
KOi K00030.
OMAi LIDNMCM.
OrthoDBi EOG75B85R.
PhylomeDBi Q9VWH4.

Enzyme and pathway databases

Reactomei REACT_218888. Citric acid cycle (TCA cycle).

Miscellaneous databases

GenomeRNAii 32940.
NextBioi 781145.
PROi Q9VWH4.

Gene expression databases

Bgeei Q9VWH4.

Family and domain databases

Gene3Di 3.40.718.10. 1 hit.
InterProi IPR019818. IsoCit/isopropylmalate_DH_CS.
IPR001804. Isocitrate/isopropylmalate_DH.
IPR004434. Isocitrate_DH_NAD.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view ]
PANTHERi PTHR11835. PTHR11835. 1 hit.
Pfami PF00180. Iso_dh. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00175. mito_nad_idh. 1 hit.
PROSITEi PS00470. IDH_IMDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.
  4. Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Hoskins R., Svirskas R., Rubin G., Celniker S.
    Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
    Strain: Berkeley.
    Tissue: Larva and Pupae.

Entry informationi

Entry nameiIDH3A_DROME
AccessioniPrimary (citable) accession number: Q9VWH4
Secondary accession number(s): E4NKP2, Q8IQW9, Q8SXH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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