ID   CISY_ACIFI              Reviewed;         386 AA.
AC   P51045;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Citrate synthase;
DE            EC=2.3.3.16;
GN   Name=gltA;
OS   Acidithiobacillus ferridurans.
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=1232575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 11Fe;
RX   PubMed=8828222; DOI=10.1099/00221287-142-9-2543;
RA   Powles R.E., Deane S.M., Rawlings D.E.;
RT   "The gene for gamma-glutamylcysteine synthetase from Thiobacillus
RT   ferrooxidans has low homology to its Escherichia coli equivalent and is
RT   linked to the gene for citrate synthase.";
RL   Microbiology 142:2543-2548(1996).
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}.
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DR   EMBL; U81808; AAB41629.1; -; Genomic_DNA.
DR   PIR; D59237; D59237.
DR   AlphaFoldDB; P51045; -.
DR   SMR; P51045; -.
DR   STRING; 380394.Lferr_2672; -.
DR   PRIDE; P51045; -.
DR   UniPathway; UPA00223; UER00717.
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   Gene3D; 1.10.230.10; -; 1.
DR   Gene3D; 1.10.580.10; -; 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   PANTHER; PTHR11739; PTHR11739; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PIRSF; PIRSF001369; Citrate_synth; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; SSF48256; 1.
DR   TIGRFAMs; TIGR01800; cit_synth_II; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..386
FT                   /note="Citrate synthase"
FT                   /id="PRO_0000169975"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        322
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   386 AA;  42689 MW;  5BD23A43016A6B89 CRC64;
     MAEPNFAPGL EGVAATQSSI SNIDGAAGLL SYRGFAIADL AAHSSFEEVA LLLLDGVLPG
     AADLERFDHG LRAHRQVKYN VREIMKFMPV TGHPMDMLHC AVASLGMFYP QQELSDAERG
     NTLHLDAMAM RIIARMPTIV AMWEQMRFGN DPISPRPDLS HAANFLYMLS GREPDPAHTK
     ILDSCLILHA EHTINASTFS VLVTGSTLTN PYHVIGGAIG TLAGPLHGGA NQKVVEMLEE
     ISSVQQVGAY LDRKMANKEK IWGFGHRIYK TRDPRAVILK GMMEDMASHG NLRHSSLFEI
     AIEVERQATE RLGAQGIHAN VDFYSGVLYH EMGIKADLFT PIFAMARSAG WLAHWREQLA
     DNRIFRPTQV YTGEQDRRYV PVAQRT