ID CISY_SACS2 Reviewed; 377 AA. AC P80148; P77979; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 3. DT 27-MAR-2024, entry version 150. DE RecName: Full=Citrate synthase; DE EC=2.3.3.16; GN Name=gltA; OrderedLocusNames=SSO2589; OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OS (Sulfolobus solfataricus). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Saccharolobus. OX NCBI_TaxID=273057; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1; RA Connaris H., Danson M.J., Hough D.W.; RT "Sulfolobus solfataricus citrate synthase."; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; RX PubMed=11427726; DOI=10.1073/pnas.141222098; RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.; RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2."; RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001). RN [3] RP PROTEIN SEQUENCE OF 7-30, AND ACETYLATION. RX PubMed=1521537; DOI=10.1111/j.1432-1033.1992.tb17208.x; RA Lill U., Lefrank S., Henschen A., Eggerer H.; RT "Conversion, by limited proteolysis, of an archaebacterial citrate synthase RT into essentially a citryl-CoA hydrolase."; RL Eur. J. Biochem. 208:459-466(1992). 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 -!- ACTIVITY REGULATION: Allosterically inhibited by NADH. CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate CC from oxaloacetate: step 1/2. CC -!- SUBUNIT: Homodimer. CC -!- PTM: The N-terminus is blocked by acetylation. CC {ECO:0000269|PubMed:1521537}. CC -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of CC oxidative metabolism. 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; U70879; AAB09594.1; -; Genomic_DNA. DR EMBL; AE006641; AAK42713.1; -; Genomic_DNA. DR PIR; B90432; B90432. DR RefSeq; WP_009989299.1; NC_002754.1. DR PDB; 1O7X; X-ray; 2.70 A; A/B/C/D=1-377. DR PDBsum; 1O7X; -. DR AlphaFoldDB; P80148; -. DR SMR; P80148; -. DR STRING; 273057.SSO2589; -. DR PaxDb; 273057-SSO2589; -. DR EnsemblBacteria; AAK42713; AAK42713; SSO2589. DR GeneID; 72911163; -. DR KEGG; sso:SSO2589; -. DR PATRIC; fig|273057.12.peg.2670; -. DR eggNOG; arCOG04237; Archaea. DR HOGENOM; CLU_025068_2_1_2; -. DR InParanoid; P80148; -. DR PhylomeDB; P80148; -. DR BRENDA; 2.3.3.16; 6163. DR UniPathway; UPA00223; UER00717. DR EvolutionaryTrace; P80148; -. DR Proteomes; UP000001974; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004108; F:citrate (Si)-synthase activity; IBA:GO_Central. DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. 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 NCBIfam; NF041157; Cit_synThplmales; 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; Acetylation; Allosteric enzyme; Direct protein sequencing; KW Reference proteome; Transferase; Tricarboxylic acid cycle. FT CHAIN 1..377 FT /note="Citrate synthase" FT /id="PRO_0000169977" FT ACT_SITE 258 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" FT ACT_SITE 313 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" FT CONFLICT 10 FT /note="N -> D (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 12 FT /note="I -> Y (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 15 FT /note="V -> S (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 17 FT /note="N -> S (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 20 FT /note="F -> Y (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 24..25 FT /note="EK -> VN (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 27 FT /note="I -> V (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 57 FT /note="P -> R (in Ref. 1; AAB09594)" FT /evidence="ECO:0000305" FT HELIX 6..8 FT /evidence="ECO:0007829|PDB:1O7X" FT STRAND 12..22 FT /evidence="ECO:0007829|PDB:1O7X" FT TURN 23..26 FT /evidence="ECO:0007829|PDB:1O7X" FT STRAND 27..30 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 35..41 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 44..53 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 59..70 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 77..85 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 92..106 FT /evidence="ECO:0007829|PDB:1O7X" FT STRAND 112..115 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 116..138 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 152..161 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 167..180 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 187..197 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 202..213 FT /evidence="ECO:0007829|PDB:1O7X" FT TURN 216..220 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 221..232 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 238..245 FT /evidence="ECO:0007829|PDB:1O7X" FT TURN 246..249 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 266..279 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 283..303 FT /evidence="ECO:0007829|PDB:1O7X" FT TURN 304..307 FT /evidence="ECO:0007829|PDB:1O7X" FT TURN 312..315 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 316..323 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:1O7X" FT HELIX 330..352 FT /evidence="ECO:0007829|PDB:1O7X" FT STRAND 360..363 FT /evidence="ECO:0007829|PDB:1O7X" SQ SEQUENCE 377 AA; 42752 MW; E3036E232F134F11 CRC64; MSVVSKGLEN VIIKVTNLTF IDGEKGILRY RGYNIEDLVN YGSYEETIYL MLYGKLPTKK ELNDLKAKLN EEYEVPQEVL DTIYLMPKEA DAIGLLEVGT AALASIDKNF KWKENDKEKA ISIIAKMATL VANVYRRKEG NKPRIPEPSD SFAKSFLLAS FAREPTTDEI NAMDKALILY TDHEVPASTT AALVAASTLS DMYSSLTAAL AALKGPLHGG AAEEAFKQFI EIGDPNRVQN WFNDKVVNQK NRLMGFGHRV YKTYDPRAKI FKKLALTLIE RNADARRYFE IAQKLEELGI KQFSSKGIYP NTDFYSGIVF YALGFPVYMF TALFALSRTL GWLAHIIEYV EEQHRLIRPR ALYVGPEYQE YVSIDKR //