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P21553

- CISY_THEAC

UniProt

P21553 - CISY_THEAC

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Protein

Citrate synthase

Gene

gltA

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed - Annotation score: 4 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei223 – 2231
Active sitei263 – 2631
Active sitei318 – 3181

GO - Molecular functioni

  1. transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer Source: InterPro

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase (EC:2.3.3.16)
Gene namesi
Name:gltA
Ordered Locus Names:Ta0169
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
ProteomesiUP000001024: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 385384Citrate synthasePRO_0000169978Add
BLAST

Proteomic databases

PRIDEiP21553.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi273075.Ta0169.

Structurei

Secondary structure

1
385
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113
Beta strandi15 – 2511
Turni26 – 294
Beta strandi30 – 334
Helixi38 – 436
Helixi48 – 5710
Helixi63 – 7412
Helixi75 – 773
Helixi81 – 888
Helixi96 – 11015
Turni118 – 1203
Helixi121 – 14323
Helixi157 – 16610
Helixi172 – 18413
Helixi192 – 20110
Turni202 – 2043
Helixi207 – 21812
Turni221 – 2233
Helixi226 – 23712
Helixi240 – 2423
Helixi243 – 2508
Turni251 – 2533
Beta strandi254 – 2563
Helixi271 – 28515
Helixi288 – 30821
Helixi309 – 3113
Turni317 – 3204
Helixi321 – 3288
Helixi333 – 3353
Helixi336 – 36025
Beta strandi367 – 3704
Helixi381 – 3833

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IFCX-ray1.70A/B/C/D1-385[»]
2R26X-ray2.50A/B/C/D2-385[»]
2R9EX-ray1.95A/B/C/D1-385[»]
ProteinModelPortaliP21553.
SMRiP21553. Positions 4-385.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21553.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021225.
KOiK01647.
OMAiSCKSRIT.

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.

P21553-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPETEEISKG LEDVNIKWTR LTTIDGNKGI LRYGGYSVED IIASGAQDEE
60 70 80 90 100
IQYLFLYGNL PTEQELRKYK ETVQKGYKIP DFVINAIRQL PRESDAVAMQ
110 120 130 140 150
MAAVAAMAAS ETKFKWNKDT DRDVAAEMIG RMSAITVNVY RHIMNMPAEL
160 170 180 190 200
PKPSDSYAES FLNAAFGRKA TKEEIDAMNT ALILYTDHEV PASTTAGLVA
210 220 230 240 250
VSTLSDMYSG ITAALAALKG PLHGGAAEAA IAQFDEIKDP AMVEKWFNDN
260 270 280 290 300
IINGKKRLMG FGHRVYKTYD PRAKIFKGIA EKLSSKKPEV HKVYEIATKL
310 320 330 340 350
EDFGIKAFGS KGIYPNTDYF SGIVYMSIGF PLRNNIYTAL FALSRVTGWQ
360 370 380
AHFIEYVEEQ QRLIRPRAVY VGPAERKYVP IAERK
Length:385
Mass (Da):43,072
Last modified:January 23, 2007 - v2
Checksum:i9B7C2C88CEBCB690
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55282 Genomic DNA. Translation: CAA38996.1.
AL445063 Genomic DNA. Translation: CAC11315.1.
PIRiS13831. YKYT.
RefSeqiNP_393647.1. NC_002578.1.
WP_010900596.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaiCAC11315; CAC11315; CAC11315.
GeneIDi1455814.
KEGGitac:Ta0169.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X55282 Genomic DNA. Translation: CAA38996.1 .
AL445063 Genomic DNA. Translation: CAC11315.1 .
PIRi S13831. YKYT.
RefSeqi NP_393647.1. NC_002578.1.
WP_010900596.1. NC_002578.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IFC X-ray 1.70 A/B/C/D 1-385 [» ]
2R26 X-ray 2.50 A/B/C/D 2-385 [» ]
2R9E X-ray 1.95 A/B/C/D 1-385 [» ]
ProteinModelPortali P21553.
SMRi P21553. Positions 4-385.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273075.Ta0169.

Proteomic databases

PRIDEi P21553.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC11315 ; CAC11315 ; CAC11315 .
GeneIDi 1455814.
KEGGi tac:Ta0169.

Phylogenomic databases

eggNOGi COG0372.
HOGENOMi HOG000021225.
KOi K01647.
OMAi SCKSRIT.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .

Miscellaneous databases

EvolutionaryTracei P21553.

Family and domain databases

Gene3Di 1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProi IPR011278. 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 ]
PANTHERi PTHR11739. PTHR11739. 1 hit.
Pfami PF00285. Citrate_synt. 1 hit.
[Graphical view ]
PIRSFi PIRSF001369. Citrate_synth. 1 hit.
PRINTSi PR00143. CITRTSNTHASE.
SUPFAMi SSF48256. SSF48256. 1 hit.
TIGRFAMsi TIGR01800. cit_synth_II. 1 hit.
PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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).

Entry informationi

Entry nameiCISY_THEAC
AccessioniPrimary (citable) accession number: P21553
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 101 of the entry and version 2 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