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Protein

Citrate synthase

Gene

gltA

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
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

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 sitei263 – 2631PROSITE-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

BRENDAi2.3.3.16. 5243.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase (EC:2.3.3.16)
Gene namesi
Name:gltA
Ordered Locus Names:PF0203
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 377376Citrate synthasePRO_0000169976Add
BLAST

Proteomic databases

PRIDEiQ53554.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi186497.PF0203.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113Combined sources
Beta strandi15 – 2511Combined sources
Turni26 – 294Combined sources
Beta strandi30 – 334Combined sources
Helixi38 – 447Combined sources
Helixi47 – 5610Combined sources
Helixi62 – 7312Combined sources
Helixi80 – 889Combined sources
Helixi95 – 10915Combined sources
Turni111 – 1144Combined sources
Helixi119 – 14426Combined sources
Helixi158 – 16710Combined sources
Helixi173 – 18614Combined sources
Helixi193 – 20210Combined sources
Turni203 – 2053Combined sources
Helixi208 – 22013Combined sources
Turni222 – 2265Combined sources
Helixi227 – 23812Combined sources
Helixi241 – 2433Combined sources
Helixi244 – 25411Combined sources
Helixi271 – 28313Combined sources
Helixi286 – 30217Combined sources
Turni303 – 3075Combined sources
Turni312 – 3154Combined sources
Helixi316 – 3216Combined sources
Turni322 – 3243Combined sources
Helixi327 – 3293Combined sources
Helixi330 – 35021Combined sources
Beta strandi359 – 3624Combined sources
Helixi373 – 3753Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ8X-ray1.90A/B7-377[»]
ProteinModelPortaliQ53554.
SMRiQ53554. Positions 7-377.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53554.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
KOiK01647.
OMAiDNRLLRP.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q53554-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTEKYLAKG LEDVYIDQTN ICYIDGKEGK LYYRGYSVEE LAELSTFEEV
60 70 80 90 100
VYLLWWGKLP SLSELENFKK ELAKSRGLPK EVIEIMEALP KNTHPMGALR
110 120 130 140 150
TIISYLGNID DSGDIPVTPE EVYRIGISVT AKIPTIVANW YRIKNGLEYV
160 170 180 190 200
PPKEKLSHAA NFLYMLHGEE PPKEWEKAMD VALILYAEHE INASTLAVMT
210 220 230 240 250
VGSTLSDYYS AILAGIGALK GPIHGGAVEE AIKQFMEIGS PEKVEEWFFK
260 270 280 290 300
ALQQKRKIMG AGHRVYKTYD PRARIFKKYA SKLGDKKLFE IAERLERLVE
310 320 330 340 350
EYLSKKGISI NVDYWSGLVF YGMKIPIELY TTIFAMGRIA GWTAHLAEYV
360 370
SHNRIIRPRL QYVGEIGKKY LPIELRR
Length:377
Mass (Da):43,050
Last modified:January 23, 2007 - v2
Checksum:iA73E70EF123BE44B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S81109 Genomic DNA. Translation: AAB35835.2.
AE009950 Genomic DNA. Translation: AAL80327.1.
RefSeqiNP_577932.1. NC_003413.1.
WP_011011316.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL80327; AAL80327; PF0203.
GeneIDi1468035.
KEGGipfu:PF0203.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S81109 Genomic DNA. Translation: AAB35835.2.
AE009950 Genomic DNA. Translation: AAL80327.1.
RefSeqiNP_577932.1. NC_003413.1.
WP_011011316.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ8X-ray1.90A/B7-377[»]
ProteinModelPortaliQ53554.
SMRiQ53554. Positions 7-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF0203.

Proteomic databases

PRIDEiQ53554.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL80327; AAL80327; PF0203.
GeneIDi1468035.
KEGGipfu:PF0203.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
KOiK01647.
OMAiDNRLLRP.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BRENDAi2.3.3.16. 5243.

Miscellaneous databases

EvolutionaryTraceiQ53554.

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. "Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus furiosus."
    Muir J.M., Russell R.J., Hough D.W., Danson M.J.
    Protein Eng. 8:583-592(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  3. "The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9-A resolution."
    Russell R.J., Ferguson J.M., Hough D.W., Danson M.J., Taylor G.L.
    Biochemistry 36:9983-9994(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiCISY_PYRFU
AccessioniPrimary (citable) accession number: Q53554
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.