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Protein

Citrate synthase

Gene

aarA

Organism
Acetobacter aceti
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: 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. Citrate synthase (aarA), Citrate synthase (aarA), Citrate synthase (aarA), Citrate synthase (aarA)
  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)DescriptionActionsGraphical viewLength
Active sitei313PROSITE-ProRule annotation1
Active sitei371PROSITE-ProRule annotation1

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-17983.
BRENDAi2.3.3.16. 33.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase (EC:2.3.3.16)
Alternative name(s):
Acetic acid resistance protein
Gene namesi
Name:aarA
OrganismiAcetobacter aceti
Taxonomic identifieri435 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeAcetobacterAcetobacter subgen. Acetobacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001699231 – 436Citrate synthaseAdd BLAST436

Proteomic databases

PRIDEiP20901.

Interactioni

Subunit structurei

Homohexamer.

Structurei

Secondary structure

1436
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 17Combined sources6
Beta strandi20 – 27Combined sources8
Beta strandi30 – 32Combined sources3
Beta strandi35 – 37Combined sources3
Helixi41 – 45Combined sources5
Beta strandi48 – 50Combined sources3
Beta strandi57 – 68Combined sources12
Turni69 – 72Combined sources4
Beta strandi73 – 76Combined sources4
Helixi81 – 87Combined sources7
Helixi90 – 99Combined sources10
Helixi105 – 116Combined sources12
Helixi123 – 125Combined sources3
Helixi126 – 129Combined sources4
Helixi138 – 149Combined sources12
Helixi150 – 152Combined sources3
Helixi155 – 158Combined sources4
Helixi165 – 188Combined sources24
Helixi201 – 210Combined sources10
Helixi221 – 234Combined sources14
Helixi241 – 250Combined sources10
Turni251 – 253Combined sources3
Helixi256 – 268Combined sources13
Turni270 – 274Combined sources5
Helixi275 – 286Combined sources12
Helixi289 – 291Combined sources3
Helixi292 – 300Combined sources9
Helixi321 – 336Combined sources16
Helixi343 – 357Combined sources15
Helixi359 – 363Combined sources5
Helixi371 – 380Combined sources10
Helixi385 – 387Combined sources3
Helixi388 – 409Combined sources22
Beta strandi419 – 422Combined sources4
Helixi433 – 435Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H12X-ray1.85A/B/C/D/E/F1-436[»]
ProteinModelPortaliP20901.
SMRiP20901.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20901.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
IPR010953. Citrate_synthase_typ-I.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01798. cit_synth_I. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20901-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSASQKEGKL STATISVDGK SAEMPVLSGT LGPDVIDIRK LPAQLGVFTF
60 70 80 90 100
DPGYGETAAC NSKITFIDGD KGVLLHRGYP IAQLDENASY EEVIYLLLNG
110 120 130 140 150
ELPNKVQYDT FTNTLTNHTL LHEQIRNFFN GFRRDAHPMA ILCGTVGALS
160 170 180 190 200
AFYPDANDIA IPANRDLAAM RLIAKIPTIA AWAYKYTQGE AFIYPRNDLN
210 220 230 240 250
YAENFLSMMF ARMSEPYKVN PVLARAMNRI LILHADHEQN ASTSTVRLAG
260 270 280 290 300
STGANPFACI AAGIAALWGP AHGGANEAVL KMLARIGKKE NIPAFIAQVK
310 320 330 340 350
DKNSGVKLMG FGHRVYKNFD PRAKIMQQTC HEVLTELGIK DDPLLDLAVE
360 370 380 390 400
LEKIALSDDY FVQRKLYPNV DFYSGIILKA MGIPTSMFTV LFAVARTTGW
410 420 430
VSQWKEMIEE PGQRISRPRQ LYIGAPQRDY VPLAKR
Length:436
Mass (Da):48,197
Last modified:February 1, 1991 - v1
Checksum:i3E6F0DD5D4216244
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34830 Genomic DNA. Translation: AAA21883.1.
PIRiA35157. YKQPC.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34830 Genomic DNA. Translation: AAA21883.1.
PIRiA35157. YKQPC.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H12X-ray1.85A/B/C/D/E/F1-436[»]
ProteinModelPortaliP20901.
SMRiP20901.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP20901.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BioCyciMetaCyc:MONOMER-17983.
BRENDAi2.3.3.16. 33.

Miscellaneous databases

EvolutionaryTraceiP20901.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
IPR010953. Citrate_synthase_typ-I.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01798. cit_synth_I. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCISY_ACEAC
AccessioniPrimary (citable) accession number: P20901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 2, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Allosteric enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.