ID   CISY_COXBU              Reviewed;         430 AA.
AC   P18789;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Citrate synthase;
DE            EC=2.3.3.16;
GN   Name=gltA; OrderedLocusNames=CBU_1410;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1756983; DOI=10.1016/0378-1119(91)90589-4;
RA   Heinzen R.A., Frazier M.E., Mallavia L.P.;
RT   "Sequence and linkage analysis of the Coxiella burnetii citrate synthase-
RT   encoding gene.";
RL   Gene 109:63-69(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
RC   STRAIN=Nine Mile;
RX   PubMed=7698664; DOI=10.1016/0378-1119(94)00888-y;
RA   Heinzen R.A., Mo Y.-Y., Robertson S.J., Mallavia L.P.;
RT   "Characterization of the succinate dehydrogenase-encoding gene cluster
RT   (sdh) from the rickettsia Coxiella burnetii.";
RL   Gene 155:27-34(1995).
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: Homohexamer.
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; M36338; AAA23307.1; -; Genomic_DNA.
DR   EMBL; AE016828; AAO90908.1; -; Genomic_DNA.
DR   EMBL; L33409; AAA74128.1; -; Genomic_DNA.
DR   PIR; JQ1392; JQ1392.
DR   RefSeq; NP_820394.1; NC_002971.3.
DR   RefSeq; WP_010958208.1; NC_002971.4.
DR   AlphaFoldDB; P18789; -.
DR   SMR; P18789; -.
DR   STRING; 227377.CBU_1410; -.
DR   DNASU; 1209316; -.
DR   EnsemblBacteria; AAO90908; AAO90908; CBU_1410.
DR   GeneID; 1209316; -.
DR   KEGG; cbu:CBU_1410; -.
DR   PATRIC; fig|227377.7.peg.1410; -.
DR   eggNOG; COG0372; Bacteria.
DR   HOGENOM; CLU_025068_0_0_6; -.
DR   OMA; TVGWCAQ; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000002671; 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; 1.10.230.10; -; 1.
DR   Gene3D; 1.10.580.10; -; 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   Pfam; PF00285; Citrate_synt; 1.
DR   PIRSF; PIRSF001369; Citrate_synth; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; SSF48256; 1.
DR   TIGRFAMs; TIGR01798; cit_synth_I; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Reference proteome; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..430
FT                   /note="Citrate synthase"
FT                   /id="PRO_0000169941"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   430 AA;  48633 MW;  0AA6EEE541501881 CRC64;
     MSNRKAKLSF ENQSVEFPIY SPTLGKDVID VKTLGNHGAY ALDVGFYSTA ACESKITFID
     GEKGILLYRG YPIDQLADKS DYMEVCYLLM YGELPNKGEK EKFVRTIKEH TSVYEQVTKF
     FNGFHYDAHP MAMVLSTIGA LSAFYHDALD ITKPADRELS AIRLIAKMPT LAAMSYKYSI
     GQPFMHPRRA MNYAENFLHM LFGTPYEETE PDPVLARAMD RIFILHADHE QNASTTTVRV
     AGSTGANPFA CISAGISALW GPAHGGANEA CLNMLRKIGD EKNIGQYIKK AKDKNDPFRL
     MGFGHRVYKN YDPRAKVMQK TCYEVLDAVG RHNEPLFKLA IKLEKIALED DYFIEKKLYP
     NVDFYSGLTL NAIGIPSNMF TVIFALSRTV GWISHWMEMM SSPDHRLARP RQLYTGETER
     EVISLDKRQA