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Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Daucus carota (Wild carrot)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

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, mitochondrial (CS)
  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 sitei308 – 3081PROSITE-ProRule annotation
Active sitei354 – 3541PROSITE-ProRule annotation
Active sitei409 – 4091PROSITE-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

BioCyciMetaCyc:MONOMER-15824.
BRENDAi2.3.3.16. 1841.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase, mitochondrial (EC:2.3.3.16)
Gene namesi
Name:CS
OrganismiDaucus carota (Wild carrot)
Taxonomic identifieri4039 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsApialesApiaceaeApioideaeScandiceaeDaucinaeDaucus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 472Citrate synthase, mitochondrialPRO_0000005487
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

PRIDEiO80433.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO80433.
SMRiO80433. Positions 36-464.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Keywords - Domaini

Transit peptide

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.

O80433-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVFFRSVSLL NKLRSRAVQQ SNLSNTVRWF QVQTSASDLD LRSQLKELIP
60 70 80 90 100
EQQERIKKLK AEHGKVQLGN ITVDMVLGGM RGMTGLLWET SLLDPEEGIR
110 120 130 140 150
FRGLSIPECQ KLLPGAKPGG EPLPEGLLWL LLTGKVPTKE QVDALSAELR
160 170 180 190 200
SRAAVPEHVY KTIDALPVTA HPMTQFATGV MALQVQSEFQ KAYEKGIHKT
210 220 230 240 250
KYWEPTYEDS ITLIAQLPVV AAYIYRRMYK NGQSISTDDS LDYGANFAHM
260 270 280 290 300
LGYDSPSMQE LMRLYVTIHT DHEGGNVSAH TGHLVASALS DPYLSFAAAL
310 320 330 340 350
NGLAGPLHGL ANQEVLLWIK SVVSECGENV TKEQLKDYIW KTLNSGKVVP
360 370 380 390 400
GYGHGVLRNT DPRYICQREF ALKHLPDDPL FQLVSNLFEV VPPILTELGK
410 420 430 440 450
VKNPWPNVDA HSGVLLNHYG LTEARYYTVL FGVSRAIGIC SQLVWDRALG
460 470
LPLERPKSVT MEWLENHCKK SS
Length:472
Mass (Da):52,657
Last modified:November 1, 1998 - v1
Checksum:iA6C8CFCA17142120
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017159 mRNA. Translation: BAA32557.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017159 mRNA. Translation: BAA32557.1.

3D structure databases

ProteinModelPortaliO80433.
SMRiO80433. Positions 36-464.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO80433.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BioCyciMetaCyc:MONOMER-15824.
BRENDAi2.3.3.16. 1841.

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

  1. "cDNA encoding carrot mitochondrial citrate synthase."
    Takita E., Koyama H., Shirano Y., Shibata D., Hara T.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. MS Yonsun.

Entry informationi

Entry nameiCISY_DAUCA
AccessioniPrimary (citable) accession number: O80433
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: July 22, 2015
This is version 80 of the entry and version 1 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.

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.