ID   CISY_BARVI              Reviewed;         319 AA.
AC   P51036;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=Citrate synthase;
DE            EC=2.3.3.16;
DE   Flags: Fragment;
GN   Name=gltA;
OS   Bartonella vinsonii (Rochalimaea vinsonii).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=33047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC VR-152 / Baker / CIP 103738;
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 208-319.
RA   Jones D.C., Regnery R., Bowen M.;
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}.
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DR   EMBL; Z70015; CAA93837.1; -; Genomic_DNA.
DR   EMBL; U28074; AAA74979.1; -; Genomic_DNA.
DR   AlphaFoldDB; P51036; -.
DR   SMR; P51036; -.
DR   STRING; 1094497.BVwin_03910; -.
DR   UniPathway; UPA00223; UER00717.
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   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   NCBIfam; TIGR01798; cit_synth_I; 1.
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..>319
FT                   /note="Citrate synthase"
FT                   /id="PRO_0000169938"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   NON_TER         1
FT   NON_TER         319
SQ   SEQUENCE   319 AA;  36063 MW;  BEC3CDC771EE7EEF CRC64;
     DGNKGILLYR GYPIEQLAEK GDFLESCYLL LYGELPTQQE KSDFDRCIMQ HTMVHEQFAR
     FFHGFRRDSH PMAVMVACLG AMSAFYHDSI DITDPQQRMI ASVRLISKVP TLAAMAYKYS
     IGQAFVYPRN DLSYAANFLR MCFSVPCEEY KTNPVLTRAM DRIFILHADH EQNASTSTVR
     LAGSSGANPF ACIAAGVACL WGPAHGGANE ACLKMLQEIG SVKRIPEFIA RAKDKNDPFR
     LMGFGHRVYK NYDPRAKIMQ KTCHEVLKEL NIQDDPLLDI AIELEKIALN DEYFVEKKLY
     PNVDFYSGIT LKALGFPTE
//