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P21553 (CISY_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Citrate synthase

EC=2.3.3.1
Gene names
Name:gltA
Ordered Locus Names:Ta0169
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length385 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.

Enzyme regulation

Allosterically inhibited by NADH.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.

Subunit structure

Homodimer.

Miscellaneous

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

Sequence similarities

Belongs to the citrate synthase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 385384Citrate synthase
PRO_0000169978

Sites

Active site2231
Active site2631
Active site3181

Secondary structure

...................................................... 385
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21553 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9B7C2C88CEBCB690

FASTA38543,072
        10         20         30         40         50         60 
MPETEEISKG LEDVNIKWTR LTTIDGNKGI LRYGGYSVED IIASGAQDEE IQYLFLYGNL 

        70         80         90        100        110        120 
PTEQELRKYK ETVQKGYKIP DFVINAIRQL PRESDAVAMQ MAAVAAMAAS ETKFKWNKDT 

       130        140        150        160        170        180 
DRDVAAEMIG RMSAITVNVY RHIMNMPAEL PKPSDSYAES FLNAAFGRKA TKEEIDAMNT 

       190        200        210        220        230        240 
ALILYTDHEV PASTTAGLVA VSTLSDMYSG ITAALAALKG PLHGGAAEAA IAQFDEIKDP 

       250        260        270        280        290        300 
AMVEKWFNDN IINGKKRLMG FGHRVYKTYD PRAKIFKGIA EKLSSKKPEV HKVYEIATKL 

       310        320        330        340        350        360 
EDFGIKAFGS KGIYPNTDYF SGIVYMSIGF PLRNNIYTAL FALSRVTGWQ AHFIEYVEEQ 

       370        380 
QRLIRPRAVY VGPAERKYVP IAERK 

« Hide

References

« Hide 'large scale' references
[1]"Citrate synthase from the thermophilic archaebacterium Thermoplasma acidophilium. Cloning and sequencing of the gene."
Sutherland K.J., Henneke C.M., Towner P., Hough D.W., Danson M.J.
Eur. J. Biochem. 194:839-844(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
[2]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
[3]"Citrate synthase from the thermophilic archaebacteria Thermoplasma acidophilum and Sulfolobus acidocaldarius."
Smith L.D., Stevenson K.J., Hough D.W., Danson M.J.
FEBS Lett. 225:277-281(1987)
Cited for: PROTEIN SEQUENCE OF 2-17.
[4]"The crystal structure of citrate synthase from the thermophilic archaeon, Thermoplasma acidophilum."
Russel R.J.M., Hough D.W., Danson M.J., Taylor G.L.
Structure 2:1157-1167(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55282 Genomic DNA. Translation: CAA38996.1.
AL445063 Genomic DNA. Translation: CAC11315.1.
PIRYKYT. S13831.
RefSeqNP_393647.1. NC_002578.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IFCX-ray1.70A/B/C/D1-385[»]
2R26X-ray2.50A/B/C/D2-385[»]
2R9EX-ray1.95A/B/C/D1-385[»]
ProteinModelPortalP21553.
SMRP21553. Positions 4-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta0169.

Proteomic databases

PRIDEP21553.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC11315; CAC11315; CAC11315.
GeneID1455814.
KEGGtac:Ta0169.

Phylogenomic databases

eggNOGCOG0372.
HOGENOMHOG000021225.
KOK01647.
OMAPRSDIIK.
ProtClustDBPRK14037.

Enzyme and pathway databases

UniPathwayUPA00223; UER00717.

Family and domain databases

Gene3D1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProIPR011278. 2-MeCitrate/Citrate_synth_I.
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]
PANTHERPTHR11739. PTHR11739. 1 hit.
PfamPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFPIRSF001369. Citrate_synth. 1 hit.
PRINTSPR00143. CITRTSNTHASE.
SUPFAMSSF48256. SSF48256. 1 hit.
TIGRFAMsTIGR01800. cit_synth_II. 1 hit.
PROSITEPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21553.

Entry information

Entry nameCISY_THEAC
AccessionPrimary (citable) accession number: P21553
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways