ID   CISY_BARQU              Reviewed;         438 AA.
AC   P51034; Q6FZN8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 3.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Citrate synthase;
DE            EC=2.3.3.16;
GN   Name=gltA; OrderedLocusNames=BQ06850;
OS   Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-379.
RC   STRAIN=ATCC VR-358 / Fuller / CIP 107027;
RX   PubMed=8863415; DOI=10.1099/00207713-46-4-891;
RA   Birtles R.J., Raoult D.;
RT   "Comparison of partial citrate synthase gene (gltA) sequences for
RT   phylogenetic analysis of Bartonella species.";
RL   Int. J. Syst. Bacteriol. 46:891-897(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 268-379.
RC   STRAIN=ATCC VR-358 / Fuller / CIP 107027;
RA   Jones D.C., Regnery R., Bowen M.;
RT   "Bartonella species characterization: citrate synthase (gltA) PCR product
RT   sequence analysis.";
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
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; BX897700; CAF26174.1; -; Genomic_DNA.
DR   EMBL; Z70014; CAA93836.1; -; Genomic_DNA.
DR   EMBL; U28073; AAA74978.1; -; Genomic_DNA.
DR   RefSeq; WP_011179429.1; NC_005955.1.
DR   AlphaFoldDB; P51034; -.
DR   SMR; P51034; -.
DR   STRING; 283165.BQ06850; -.
DR   EnsemblBacteria; CAF26174; CAF26174; BQ06850.
DR   KEGG; bqu:BQ06850; -.
DR   eggNOG; COG0372; Bacteria.
DR   HOGENOM; CLU_025068_0_0_5; -.
DR   OMA; TVGWCAQ; -.
DR   OrthoDB; 1412360at2; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000000597; 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   Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..438
FT                   /note="Citrate synthase"
FT                   /id="PRO_0000169935"
FT   ACT_SITE        306
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   CONFLICT        117
FT                   /note="Q -> R (in Ref. 2; CAA93836)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="F -> C (in Ref. 2; CAA93836)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   438 AA;  49464 MW;  98ED2C4A41ACD5E4 CRC64;
     MSENKAHITV NNKKIELSVR KGTLGPGVIE IASLYKETDT FTYDPGFTST ASCESKITYI
     DGDKGILLYC GYPIDQLAEK GDFLESCYLL LYGELPTKQE KIDFDRCIMQ HMMVHEQFTR
     FFHGFRRDSH PMAVMVACLG AMSAFYHDSI DIKDAQQRMI AAIRLISKVP TLAAMAYKYS
     IGQAFVYPRN DLSYAANFLH MCFSVPCEEY KINPVLSRAM DRIFTLHADH EQNASTSTVR
     LVGSSGANPF ACIAAGVACL WGPAHGGANE ACLKMLQKIG SVERIPEFIA RAKDKNDPFR
     LMGFGHRVYK NYDPRAKIMQ QTCHEVLKEL NIQDDPLLDI AIALENTALN DEYFIEKKLY
     PNVDFYSGIT LKALGFPTEM FTVLFALARS IGWVAQWKEM IEDPAQKIGR PRQLYTGYAA
     REYVSIDKRI SKNKMTTQ