ID CISY_PYRFU Reviewed; 377 AA. AC Q53554; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 146. DE RecName: Full=Citrate synthase; DE EC=2.3.3.16; GN Name=gltA; OrderedLocusNames=PF0203; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=186497; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. RX PubMed=8532683; DOI=10.1093/protein/8.6.583; RA Muir J.M., Russell R.J., Hough D.W., Danson M.J.; RT "Citrate synthase from the hyperthermophilic Archaeon, Pyrococcus RT furiosus."; RL Protein Eng. 8:583-592(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. RT horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX PubMed=9254593; DOI=10.1021/bi9705321; RA Russell R.J., Ferguson J.M., Hough D.W., Danson M.J., Taylor G.L.; RT "The crystal structure of citrate synthase from the hyperthermophilic RT archaeon Pyrococcus furiosus at 1.9-A resolution."; RL Biochemistry 36:9983-9994(1997). CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); CC Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10117}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate CC from oxaloacetate: step 1/2. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; S81109; AAB35835.2; -; Genomic_DNA. DR EMBL; AE009950; AAL80327.1; -; Genomic_DNA. DR RefSeq; WP_011011316.1; NZ_CP023154.1. DR PDB; 1AJ8; X-ray; 1.90 A; A/B=7-377. DR PDBsum; 1AJ8; -. DR AlphaFoldDB; Q53554; -. DR SMR; Q53554; -. DR STRING; 186497.PF0203; -. DR PaxDb; 186497-PF0203; -. DR GeneID; 41711994; -. DR KEGG; pfu:PF0203; -. DR PATRIC; fig|186497.12.peg.211; -. DR eggNOG; arCOG04237; Archaea. DR HOGENOM; CLU_025068_2_1_2; -. DR OrthoDB; 21302at2157; -. DR PhylomeDB; Q53554; -. DR BRENDA; 2.3.3.1; 5243. DR BRENDA; 2.3.3.16; 5243. DR UniPathway; UPA00223; UER00717. DR EvolutionaryTrace; Q53554; -. DR Proteomes; UP000001013; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR CDD; cd06118; citrate_synt_like_1; 1. DR Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1. DR Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 1. DR InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II. DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub. DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub. DR InterPro; IPR002020; Citrate_synthase. DR InterPro; IPR019810; Citrate_synthase_AS. DR InterPro; IPR024176; Citrate_synthase_bac-typ. DR InterPro; IPR036969; Citrate_synthase_sf. DR NCBIfam; TIGR01800; cit_synth_II; 1. DR PANTHER; PTHR11739; CITRATE SYNTHASE; 1. DR PANTHER; PTHR11739:SF4; CITRATE SYNTHASE, PEROXISOMAL; 1. DR Pfam; PF00285; Citrate_synt; 1. DR PIRSF; PIRSF001369; Citrate_synth; 1. DR PRINTS; PR00143; CITRTSNTHASE. DR SUPFAM; SSF48256; Citrate synthase; 1. DR PROSITE; PS00480; CITRATE_SYNTHASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Direct protein sequencing; KW Reference proteome; Transferase; Tricarboxylic acid cycle. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..377 FT /note="Citrate synthase" FT /id="PRO_0000169976" FT ACT_SITE 263 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" FT ACT_SITE 313 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" FT HELIX 9..11 FT /evidence="ECO:0007829|PDB:1AJ8" FT STRAND 15..25 FT /evidence="ECO:0007829|PDB:1AJ8" FT TURN 26..29 FT /evidence="ECO:0007829|PDB:1AJ8" FT STRAND 30..33 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 38..44 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 47..56 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 62..73 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 80..88 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 95..109 FT /evidence="ECO:0007829|PDB:1AJ8" FT TURN 111..114 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 119..144 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 158..167 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 173..186 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 193..202 FT /evidence="ECO:0007829|PDB:1AJ8" FT TURN 203..205 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 208..220 FT /evidence="ECO:0007829|PDB:1AJ8" FT TURN 222..226 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 227..238 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 241..243 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 244..254 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 271..283 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 286..302 FT /evidence="ECO:0007829|PDB:1AJ8" FT TURN 303..307 FT /evidence="ECO:0007829|PDB:1AJ8" FT TURN 312..315 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 316..321 FT /evidence="ECO:0007829|PDB:1AJ8" FT TURN 322..324 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 330..350 FT /evidence="ECO:0007829|PDB:1AJ8" FT STRAND 359..362 FT /evidence="ECO:0007829|PDB:1AJ8" FT HELIX 373..375 FT /evidence="ECO:0007829|PDB:1AJ8" SQ SEQUENCE 377 AA; 43050 MW; A73E70EF123BE44B CRC64; MNTEKYLAKG LEDVYIDQTN ICYIDGKEGK LYYRGYSVEE LAELSTFEEV VYLLWWGKLP SLSELENFKK ELAKSRGLPK EVIEIMEALP KNTHPMGALR TIISYLGNID DSGDIPVTPE EVYRIGISVT AKIPTIVANW YRIKNGLEYV PPKEKLSHAA NFLYMLHGEE PPKEWEKAMD VALILYAEHE INASTLAVMT VGSTLSDYYS AILAGIGALK GPIHGGAVEE AIKQFMEIGS PEKVEEWFFK ALQQKRKIMG AGHRVYKTYD PRARIFKKYA SKLGDKKLFE IAERLERLVE EYLSKKGISI NVDYWSGLVF YGMKIPIELY TTIFAMGRIA GWTAHLAEYV SHNRIIRPRL QYVGEIGKKY LPIELRR //