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Protein

Probable citrate synthase, mitochondrial

Gene

kdn

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a role in controlling neuronal activity and seizure susceptibility.1 Publication

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotation

Pathway: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes isocitrate from oxaloacetate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Probable citrate synthase, mitochondrial (kdn)
  2. no protein annotated in this organism
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei302 – 3021PROSITE-ProRule annotation
Active sitei348 – 3481PROSITE-ProRule annotation
Active sitei403 – 4031PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Behavior, Tricarboxylic acid cycle

Enzyme and pathway databases

ReactomeiREACT_326398. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable citrate synthase, mitochondrial (EC:2.3.3.16)
Alternative name(s):
Protein knockdown
Gene namesi
Name:kdn
Synonyms:l(1)G0030
ORF Names:CG3861
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0261955. kdn.

Subcellular locationi

GO - Cellular componenti

  • microtubule associated complex Source: FlyBase
  • mitochondrial matrix Source: UniProtKB
  • mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 464Probable citrate synthase, mitochondrialPRO_0000291603
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

PaxDbiQ9W401.
PRIDEiQ9W401.

Expressioni

Gene expression databases

BgeeiQ9W401.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi58066. 3 interactions.
IntActiQ9W401. 24 interactions.
MINTiMINT-936064.
STRINGi7227.FBpp0070871.

Structurei

3D structure databases

ProteinModelPortaliQ9W401.
SMRiQ9W401. Positions 29-462.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0372.
GeneTreeiENSGT00390000006813.
InParanoidiQ9W401.
KOiK01647.
OMAiWLQMQSP.
OrthoDBiEOG73BVCB.
PhylomeDBiQ9W401.

Family and domain databases

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR010109. Citrate_synthase_euk.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01793. cit_synth_euk. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 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. AlignAdd to basket

Isoform A (identifier: Q9W401-1) [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

        10         20         30         40         50
MSLYRISARK LSEAQKLPNV GAYVRMIAAD GKSLRDVLAA KVPQEQERVK
60 70 80 90 100
NFRKQHGATK MGETTIDMMY GGMRGIKALV TETSVLDADE GIRFRGLSIP
110 120 130 140 150
ECQKVLPAAD GGTEPLPEGL FWLLLTGEVP TKSQVQQLSR EWAERAALPQ
160 170 180 190 200
HVVTMLNNMP TTLHPMSQFA AAVTALNHDS KFAKAYSDGV HKSKYWEYVY
210 220 230 240 250
EDSMDLIAKL PVVAATIYCN TYRGGKGSRS IDSSLDWSAN FVKMLGYDNA
260 270 280 290 300
PFTELMRLYL TIHSDHEGGN VSAHTVHLVG SALSDPYLSF AAGLNGLAGP
310 320 330 340 350
LHGLANQEVL VWLRKLQKEA GNNPSEEQLK EYIWKTLKSG QVVPGYGHAV
360 370 380 390 400
LRKTDPRYTC QREFALKHLP EDETFQLVSK IYKVVPPILT ETGKVKNPWP
410 420 430 440 450
NVDAHSGVLL QYYGMKEMNY YTVLFGVSRA LGVLASLVWD RALGLPIERP
460
KSFSTDLLVK MVQK
Note: No experimental confirmation available.
Length:464
Mass (Da):51,574
Last modified:May 1, 2000 - v1
Checksum:i57D582652931B4F9
GO
Isoform B (identifier: Q9W401-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-13: SLYRISARKLSE → FVRRFGNGSL...ETLNMPDMQD

Note: No experimental confirmation available.
Show »
Length:522
Mass (Da):58,217
Checksum:i7CA9D79350F2764D
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 1312SLYRI…RKLSE → FVRRFGNGSLGHHFAFQRRY LAKNSMWDSKSIGTPSSFRM RSKKDNVTGNLKEQQQSATP ETLNMPDMQD in isoform B. 1 PublicationVSP_027491Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF46159.1.
AE014298 Genomic DNA. Translation: AAN09169.1.
AY089318 mRNA. Translation: AAL90056.1.
RefSeqiNP_572319.2. NM_132091.3. [Q9W401-1]
NP_727091.1. NM_167072.2. [Q9W401-2]
UniGeneiDm.8.

Genome annotation databases

EnsemblMetazoaiFBtr0070907; FBpp0070872; FBgn0261955. [Q9W401-1]
GeneIDi31579.
KEGGidme:Dmel_CG3861.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF46159.1.
AE014298 Genomic DNA. Translation: AAN09169.1.
AY089318 mRNA. Translation: AAL90056.1.
RefSeqiNP_572319.2. NM_132091.3. [Q9W401-1]
NP_727091.1. NM_167072.2. [Q9W401-2]
UniGeneiDm.8.

3D structure databases

ProteinModelPortaliQ9W401.
SMRiQ9W401. Positions 29-462.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58066. 3 interactions.
IntActiQ9W401. 24 interactions.
MINTiMINT-936064.
STRINGi7227.FBpp0070871.

Proteomic databases

PaxDbiQ9W401.
PRIDEiQ9W401.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070907; FBpp0070872; FBgn0261955. [Q9W401-1]
GeneIDi31579.
KEGGidme:Dmel_CG3861.

Organism-specific databases

CTDi31579.
FlyBaseiFBgn0261955. kdn.

Phylogenomic databases

eggNOGiCOG0372.
GeneTreeiENSGT00390000006813.
InParanoidiQ9W401.
KOiK01647.
OMAiWLQMQSP.
OrthoDBiEOG73BVCB.
PhylomeDBiQ9W401.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
ReactomeiREACT_326398. Citric acid cycle (TCA cycle).

Miscellaneous databases

GenomeRNAii31579.
NextBioi774282.
PROiQ9W401.

Gene expression databases

BgeeiQ9W401.

Family and domain databases

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
IPR010109. Citrate_synthase_euk.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01793. cit_synth_euk. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 B).
    Strain: Berkeley.
    Tissue: Testis.
  4. Cited for: IDENTIFICATION.
  5. "Metabolic disruption in Drosophila bang-sensitive seizure mutants."
    Fergestad T., Bostwick B., Ganetzky B.
    Genetics 173:1357-1364(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCISY_DROME
AccessioniPrimary (citable) accession number: Q9W401
Secondary accession number(s): Q8T477
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: May 1, 2000
Last modified: April 1, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism.
Mutation of kdn causes a behavioral mutation ('bang sensitivity' = temporarily paralysis in response to a physical jolt). Flies lacking kdn exhibit alterations in neuronal firing patterns in the giant fiber (GF) pathway.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.