ID CISY_HELPJ Reviewed; 426 AA. AC Q9ZN37; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 123. DE RecName: Full=Citrate synthase; DE EC=2.3.3.16; GN Name=gltA; OrderedLocusNames=jhp_0022; OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=J99 / ATCC 700824; RX PubMed=9923682; DOI=10.1038/16495; RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D., RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.; RT "Genomic sequence comparison of two unrelated isolates of the human gastric RT pathogen Helicobacter pylori."; RL Nature 397:176-180(1999). 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 -!- 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; AE001439; AAD05606.1; -; Genomic_DNA. DR PIR; D71982; D71982. DR RefSeq; WP_000117349.1; NC_000921.1. DR AlphaFoldDB; Q9ZN37; -. DR SMR; Q9ZN37; -. DR IntAct; Q9ZN37; 2. DR KEGG; hpj:jhp_0022; -. DR eggNOG; COG0372; Bacteria. DR UniPathway; UPA00223; UER00717. DR Proteomes; UP000000804; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway. DR CDD; cd06114; EcCS_like; 1. DR Gene3D; 2.20.28.60; -; 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; 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 InterPro; IPR010953; Citrate_synthase_typ-I. DR PANTHER; PTHR42871; CITRATE SYNTHASE; 1. DR PANTHER; PTHR42871:SF1; CITRATE SYNTHASE; 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 3: Inferred from homology; KW Transferase; Tricarboxylic acid cycle. FT CHAIN 1..426 FT /note="Citrate synthase" FT /id="PRO_0000169947" FT ACT_SITE 314 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" FT ACT_SITE 372 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117" SQ SEQUENCE 426 AA; 48262 MW; 373FEE23B1C6239A CRC64; MSVTLINNEN NARYEFETIE CTRGPKAVDF SKLFETTGFF SYDPGYSSTA GCQSKISYIN GKKGELYYRG HRIEDLVAKY KYVDVCRLLL TGELPKNQDE SLEFELELRH RSFVHESLLN MFSAFPSNAH PMAKLSSGVS ILSTLYSTHQ NMHTEEDYQT MARRIVAKIP TLAAICYRNE VGAPIIYPDI ARSYVENILF MLRGYPYSRL KHTTQGEVGI TPLEVEAFDK ILTLHADHGQ NASSTTVRNV ASTGVHPYAA ISAGISALWG HLHGGANEKV LLQLEEIGDV KNVDKYIARV KDKNDNFKLM GFGHRVYKSY DPRAKILKGL KDELHQKGVK MDERLSEIAA KVEEIALKDE YFIERNLYPN VDFYSGTILR ALKIPVRFFT PVFVIGRTVG WCAQLLEHVK SPQARITRPR QVYVGD //