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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.

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei258 – 2581PROSITE-ProRule annotation
Active sitei313 – 3131PROSITE-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

BioCyciSSOL273057:GCH2-2399-MONOMER.
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
ProteomesiUP000001974 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Citrate synthasePRO_0000169977Add
BLAST

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

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Beta strandi12 – 2211Combined sources
Turni23 – 264Combined sources
Beta strandi27 – 304Combined sources
Helixi35 – 417Combined sources
Helixi44 – 5310Combined sources
Helixi59 – 7012Combined sources
Helixi77 – 859Combined sources
Helixi92 – 10615Combined sources
Beta strandi112 – 1154Combined sources
Helixi116 – 13823Combined sources
Helixi152 – 16110Combined sources
Helixi167 – 18014Combined sources
Helixi187 – 19711Combined sources
Helixi202 – 21312Combined sources
Turni216 – 2205Combined sources
Helixi221 – 23212Combined sources
Helixi235 – 2373Combined sources
Helixi238 – 2458Combined sources
Turni246 – 2494Combined sources
Helixi266 – 27914Combined sources
Helixi283 – 30321Combined sources
Turni304 – 3074Combined sources
Turni312 – 3154Combined sources
Helixi316 – 3238Combined sources
Helixi327 – 3293Combined sources
Helixi330 – 35223Combined sources
Beta strandi360 – 3634Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O7XX-ray2.70A/B/C/D1-377[»]
ProteinModelPortaliP80148.
SMRiP80148. Positions 3-372.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80148.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0372.
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-like.
IPR016141. Citrate_synthase-like_core.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101N → D AA sequence (PubMed:1521537).Curated
Sequence conflicti12 – 121I → Y AA sequence (PubMed:1521537).Curated
Sequence conflicti15 – 151V → S AA sequence (PubMed:1521537).Curated
Sequence conflicti17 – 171N → S AA sequence (PubMed:1521537).Curated
Sequence conflicti20 – 201F → Y AA sequence (PubMed:1521537).Curated
Sequence conflicti24 – 252EK → VN AA sequence (PubMed:1521537).Curated
Sequence conflicti27 – 271I → V AA sequence (PubMed:1521537).Curated
Sequence conflicti57 – 571P → R in AAB09594 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U70879 Genomic DNA. Translation: AAB09594.1.
AE006641 Genomic DNA. Translation: AAK42713.1.
PIRiB90432.
RefSeqiNP_343923.1. NC_002754.1.
WP_009989299.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK42713; AAK42713; SSO2589.
GeneIDi1454040.
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.
RefSeqiNP_343923.1. NC_002754.1.
WP_009989299.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O7XX-ray2.70A/B/C/D1-377[»]
ProteinModelPortaliP80148.
SMRiP80148. Positions 3-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO2589.

Proteomic databases

PRIDEiP80148.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK42713; AAK42713; SSO2589.
GeneIDi1454040.
KEGGisso:SSO2589.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
InParanoidiP80148.
KOiK01647.
OMAiNKEDGVR.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BioCyciSSOL273057:GCH2-2399-MONOMER.
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-like.
IPR016141. Citrate_synthase-like_core.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Sulfolobus solfataricus citrate synthase."
    Connaris H., Danson M.J., Hough D.W.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  3. "Conversion, by limited proteolysis, of an archaebacterial citrate synthase into essentially a citryl-CoA hydrolase."
    Lill U., Lefrank S., Henschen A., Eggerer H.
    Eur. J. Biochem. 208:459-466(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 7-30, ACETYLATION.

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: May 27, 2015
This is version 113 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

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.