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Protein

Citrate synthase

Gene

gltA

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
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

Enzyme regulationi

Allosterically inhibited by NADH.

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 (gltA)
  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 sitei258PROSITE-ProRule annotation1
Active sitei313PROSITE-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

BRENDAi2.3.3.16. 6163.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase (EC:2.3.3.16)
Gene namesi
Name:gltA
Ordered Locus Names:SSO2589
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001974 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001699771 – 377Citrate synthaseAdd BLAST377

Post-translational modificationi

The N-terminus is blocked by acetylation.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP80148.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi273057.SSO2589.

Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 8Combined sources3
Beta strandi12 – 22Combined sources11
Turni23 – 26Combined sources4
Beta strandi27 – 30Combined sources4
Helixi35 – 41Combined sources7
Helixi44 – 53Combined sources10
Helixi59 – 70Combined sources12
Helixi77 – 85Combined sources9
Helixi92 – 106Combined sources15
Beta strandi112 – 115Combined sources4
Helixi116 – 138Combined sources23
Helixi152 – 161Combined sources10
Helixi167 – 180Combined sources14
Helixi187 – 197Combined sources11
Helixi202 – 213Combined sources12
Turni216 – 220Combined sources5
Helixi221 – 232Combined sources12
Helixi235 – 237Combined sources3
Helixi238 – 245Combined sources8
Turni246 – 249Combined sources4
Helixi266 – 279Combined sources14
Helixi283 – 303Combined sources21
Turni304 – 307Combined sources4
Turni312 – 315Combined sources4
Helixi316 – 323Combined sources8
Helixi327 – 329Combined sources3
Helixi330 – 352Combined sources23
Beta strandi360 – 363Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O7XX-ray2.70A/B/C/D1-377[»]
ProteinModelPortaliP80148.
SMRiP80148.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80148.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiarCOG04237. Archaea.
COG0372. LUCA.
HOGENOMiHOG000021225.
InParanoidiP80148.
KOiK01647.
OMAiNKEDGVR.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR011278. 2-MeCitrate/Citrate_synth_II.
IPR016142. 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.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01800. cit_synth_II. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80148-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVVSKGLEN VIIKVTNLTF IDGEKGILRY RGYNIEDLVN YGSYEETIYL
60 70 80 90 100
MLYGKLPTKK ELNDLKAKLN EEYEVPQEVL DTIYLMPKEA DAIGLLEVGT
110 120 130 140 150
AALASIDKNF KWKENDKEKA ISIIAKMATL VANVYRRKEG NKPRIPEPSD
160 170 180 190 200
SFAKSFLLAS FAREPTTDEI NAMDKALILY TDHEVPASTT AALVAASTLS
210 220 230 240 250
DMYSSLTAAL AALKGPLHGG AAEEAFKQFI EIGDPNRVQN WFNDKVVNQK
260 270 280 290 300
NRLMGFGHRV YKTYDPRAKI FKKLALTLIE RNADARRYFE IAQKLEELGI
310 320 330 340 350
KQFSSKGIYP NTDFYSGIVF YALGFPVYMF TALFALSRTL GWLAHIIEYV
360 370
EEQHRLIRPR ALYVGPEYQE YVSIDKR
Length:377
Mass (Da):42,752
Last modified:June 1, 2001 - v3
Checksum:iE3036E232F134F11
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10N → D AA sequence (PubMed:1521537).Curated1
Sequence conflicti12I → Y AA sequence (PubMed:1521537).Curated1
Sequence conflicti15V → S AA sequence (PubMed:1521537).Curated1
Sequence conflicti17N → S AA sequence (PubMed:1521537).Curated1
Sequence conflicti20F → Y AA sequence (PubMed:1521537).Curated1
Sequence conflicti24 – 25EK → VN AA sequence (PubMed:1521537).Curated2
Sequence conflicti27I → V AA sequence (PubMed:1521537).Curated1
Sequence conflicti57P → R in AAB09594 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70879 Genomic DNA. Translation: AAB09594.1.
AE006641 Genomic DNA. Translation: AAK42713.1.
PIRiB90432.
RefSeqiWP_009989299.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK42713; AAK42713; SSO2589.
GeneIDi27428887.
KEGGisso:SSO2589.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70879 Genomic DNA. Translation: AAB09594.1.
AE006641 Genomic DNA. Translation: AAK42713.1.
PIRiB90432.
RefSeqiWP_009989299.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O7XX-ray2.70A/B/C/D1-377[»]
ProteinModelPortaliP80148.
SMRiP80148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO2589.

Proteomic databases

PRIDEiP80148.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK42713; AAK42713; SSO2589.
GeneIDi27428887.
KEGGisso:SSO2589.

Phylogenomic databases

eggNOGiarCOG04237. Archaea.
COG0372. LUCA.
HOGENOMiHOG000021225.
InParanoidiP80148.
KOiK01647.
OMAiNKEDGVR.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BRENDAi2.3.3.16. 6163.

Miscellaneous databases

EvolutionaryTraceiP80148.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR011278. 2-MeCitrate/Citrate_synth_II.
IPR016142. 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.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01800. cit_synth_II. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCISY_SULSO
AccessioniPrimary (citable) accession number: P80148
Secondary accession number(s): P77979
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 120 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

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.