Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Citrate synthase 5, mitochondrial

Gene

CSY5

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathway:itricarboxylic 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. Citrate synthase 5, mitochondrial (CSY5), Citrate synthase 1, peroxisomal (CSY1), Citrate synthase 2, peroxisomal (CSY2), Citrate synthase 3, peroxisomal (CSY3), Citrate synthase 4, mitochondrial (CSY4)
  2. Aconitate hydratase 2, mitochondrial (ACO2), Aconitate hydratase 1 (ACO1), Aconitate hydratase 3, mitochondrial (ACO3)
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 sitei300 – 3001PROSITE-ProRule annotation
Active sitei346 – 3461PROSITE-ProRule annotation
Active sitei401 – 4011PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciARA:AT3G60100-MONOMER.
ReactomeiREACT_289406. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase 5, mitochondrial (EC:2.3.3.16)
Gene namesi
Name:CSY5
Ordered Locus Names:At3g60100
ORF Names:T2O9.80
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G60100.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionSequence AnalysisAdd
BLAST
Chaini26 – 464439Citrate synthase 5, mitochondrialPRO_0000005485Add
BLAST

Proteomic databases

PaxDbiQ9M1D3.
PRIDEiQ9M1D3.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT3G60100.1.

Structurei

3D structure databases

ProteinModelPortaliQ9M1D3.
SMRiQ9M1D3. Positions 36-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000130831.
InParanoidiQ9M1D3.
KOiK01647.
OMAiSYVYRRM.

Family and domain databases

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase.
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]

Sequencei

Sequence statusi: Complete.

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

Q9M1D3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVFFRSVSAI SRLRSRAVQQ SSLSNSVRWL HSSELDLKSQ MQEIIPEQQD
60 70 80 90 100
RLKKLKSEQG KVPVGNITVD MVLGGMRGMT GLLWETSLLD ADEGIRFRGM
110 120 130 140 150
SIPECQKILP SAESGEEPLP ESLLWLLLTG KVPTKEQANA LSTELAHRAA
160 170 180 190 200
VPAIDALPST AHPMTQFASG VMALQVQSEF QKAYEQGDIS KSKYWEPTFE
210 220 230 240 250
DALNLIARVP VVASYVYRRM YKDGSIIPLD DSLDYGANFS HMLGFDSPQM
260 270 280 290 300
KELMRLYVTI HSDHEGGNVS AHAGHLVGSA LSDPYLSFAA ALNGLAGPLH
310 320 330 340 350
GLANQEVLLW IKLVVEECGE SISKEQLKDY VWKTLNSGKV VPGYGHGVLR
360 370 380 390 400
KTDPRYICQR EFALKHLPDD PLFQLVSKLY EVVPPILTEL GKVKNPWPNV
410 420 430 440 450
DAHSGVLLNY YGLTEARYYT VLFGVSRSLG ICSQLIWDRA LGLPLERPKS
460
VNMDWLDNFT RLNR
Length:464
Mass (Da):51,724
Last modified:February 22, 2012 - v2
Checksum:i2D2AE88A6AA29BB2
GO

Sequence cautioni

The sequence CAB75925.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL138658 Genomic DNA. Translation: CAB75925.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE80011.1.
PIRiT47834.
RefSeqiNP_191569.2. NM_115873.3.
UniGeneiAt.70776.

Genome annotation databases

EnsemblPlantsiAT3G60100.1; AT3G60100.1; AT3G60100.
GeneIDi825180.
KEGGiath:AT3G60100.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL138658 Genomic DNA. Translation: CAB75925.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE80011.1.
PIRiT47834.
RefSeqiNP_191569.2. NM_115873.3.
UniGeneiAt.70776.

3D structure databases

ProteinModelPortaliQ9M1D3.
SMRiQ9M1D3. Positions 36-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G60100.1.

Proteomic databases

PaxDbiQ9M1D3.
PRIDEiQ9M1D3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G60100.1; AT3G60100.1; AT3G60100.
GeneIDi825180.
KEGGiath:AT3G60100.

Organism-specific databases

GeneFarmi4305.
TAIRiAT3G60100.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000130831.
InParanoidiQ9M1D3.
KOiK01647.
OMAiSYVYRRM.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BioCyciARA:AT3G60100-MONOMER.
ReactomeiREACT_289406. Citric acid cycle (TCA cycle).

Miscellaneous databases

PROiQ9M1D3.

Family and domain databases

Gene3Di1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR002020. Citrate_synthase.
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. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
    Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
    Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.

Entry informationi

Entry nameiCISY5_ARATH
AccessioniPrimary (citable) accession number: Q9M1D3
Secondary accession number(s): F4JAL9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 22, 2012
Last modified: July 22, 2015
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  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.