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Protein

Citrate synthase, mitochondrial

Gene

CIT

Organism
Candida tropicalis (Yeast)
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, mitochondrial (CIT)
  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 sitei301 – 3011PROSITE-ProRule annotation
Active sitei347 – 3471PROSITE-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

UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase, mitochondrial (EC:2.3.3.16)
Gene namesi
Name:CIT
OrganismiCandida tropicalis (Yeast)
Taxonomic identifieri5482 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 467Citrate synthase, mitochondrialPRO_0000005476
Transit peptidei1 – ?MitochondrionSequence Analysis

Interactioni

Protein-protein interaction databases

STRINGi294747.XP_002545966.1.

Structurei

3D structure databases

ProteinModelPortaliP79024.
SMRiP79024. Positions 32-463.
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.

P79024-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSALRSFQRS SNVAKSTLKN SVRTYATAEP TLKQRLEEIL PAKAEEVKQL
60 70 80 90 100
KKDYGKTVIG EVLLEQAYGG MRGIKGLVWE GSVLDPIEGI RFRGRTIPDI
110 120 130 140 150
QKELPKAPGG EEPLPEALFW LLLTGEVPTE AQTRALSEEF AARSALPKHV
160 170 180 190 200
EELIDRSPSH LHPMAQFSIA VTALESESQF AKAYAKGVHK SEYWKYTYED
210 220 230 240 250
SIELLAKLPT IAAKIYRNVF HDGKLPAQID SKLDYGANLA SLLGFGENKE
260 270 280 290 300
FLELMRLYLT IHSDHEGGNV SAHTTHLVGS ALSSPFLSLA AGLNGLAGPL
310 320 330 340 350
HGRANQEVLE WLFKLREELN GDYSKEAIEK YLWDTLNAGR VGPGYGHAVL
360 370 380 390 400
RKTDPRYTAQ REFALKHMPD YELFKLVSNI YEVAPGVFDQ HGMTKNPWPN
410 420 430 440 450
VGSHSGVLLQ YYGLTEESFY TVLFGVSRAF GVLPQLILDR GLGMPIERPK
460
SFSTEKYIEL VKSIGKN
Length:467
Mass (Da):52,004
Last modified:May 1, 1997 - v1
Checksum:i4B194132C4198CA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001565 Genomic DNA. Translation: BAA19410.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB001565 Genomic DNA. Translation: BAA19410.1.

3D structure databases

ProteinModelPortaliP79024.
SMRiP79024. Positions 32-463.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi294747.XP_002545966.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.

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. Ueda M., Sanuki S., Kawachi H., Shimizu K., Atomi H., Tanaka A.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 20336 / pK233 / NCYC 997.

Entry informationi

Entry nameiCISY_CANTR
AccessioniPrimary (citable) accession number: P79024
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: July 22, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Caution

The conserved active site Asp residue in position 402 is replaced by a Gly.Curated

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.