ID   CISY_DEIRA              Reviewed;         377 AA.
AC   Q9RWB2;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Citrate synthase;
DE            EC=2.3.3.16;
GN   Name=gltA; OrderedLocusNames=DR_0757;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS   27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-14.
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 /
RC   NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX   PubMed=15249204; DOI=10.1016/j.bbrc.2004.06.062;
RA   Joshi B.S., Schmid R., Altendorf K., Apte S.K.;
RT   "Protein recycling is a major component of post-irradiation recovery in
RT   Deinococcus radiodurans strain R1.";
RL   Biochem. Biophys. Res. Commun. 320:1112-1117(2004).
CC   -!- FUNCTION: Might regulate the synthesis and function of enzymes involved
CC       in later enzymatic steps of Krebs cycle. Loss in activity results in
CC       sporulation defect (By similarity). {ECO:0000250|UniProtKB:P39120}.
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;
CC         Evidence={ECO:0000250|UniProtKB:P39120, ECO:0000255|PROSITE-
CC         ProRule:PRU10117, ECO:0000255|RuleBase:RU000441};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 1/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q53554}.
CC   -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC       oxidative metabolism. {ECO:0000250|UniProtKB:P39120}.
CC   -!- SIMILARITY: Belongs to the citrate synthase family.
CC       {ECO:0000255|RuleBase:RU000441, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF10336.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000513; AAF10336.1; ALT_INIT; Genomic_DNA.
DR   PIR; A75479; A75479.
DR   RefSeq; NP_294481.1; NC_001263.1.
DR   RefSeq; WP_027479989.1; NZ_JMLF01000005.1.
DR   AlphaFoldDB; Q9RWB2; -.
DR   SMR; Q9RWB2; -.
DR   STRING; 243230.DR_0757; -.
DR   PaxDb; 243230-DR_0757; -.
DR   EnsemblBacteria; AAF10336; AAF10336; DR_0757.
DR   GeneID; 69517002; -.
DR   KEGG; dra:DR_0757; -.
DR   PATRIC; fig|243230.17.peg.937; -.
DR   eggNOG; COG0372; Bacteria.
DR   HOGENOM; CLU_025068_2_1_0; -.
DR   InParanoid; Q9RWB2; -.
DR   OrthoDB; 9800864at2; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   CDD; cd06118; citrate_synt_like_1; 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; 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   NCBIfam; TIGR01800; cit_synth_II; 1.
DR   PANTHER; PTHR11739; CITRATE SYNTHASE; 1.
DR   PANTHER; PTHR11739:SF4; CITRATE SYNTHASE, PEROXISOMAL; 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   1: Evidence at protein level;
KW   Allosteric enzyme; Direct protein sequencing; Reference proteome;
KW   Transferase; Tricarboxylic acid cycle.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:15249204"
FT   CHAIN           2..377
FT                   /note="Citrate synthase"
FT                   /id="PRO_0000169942"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        259
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        313
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   377 AA;  41628 MW;  268F74D5B8EC37DA CRC64;
     MSNIAKGLEG VLFTESKLTF INGSEGILTH LGIPIQEWAE KSTFEELSLA LLDAKLPTAE
     ELAKFDAELK ANRAIPDQLV GIIRDMPKGV HPMQALRTAV SYLGLLDPQA EDITPEARRA
     ISTRMIAQFS TIIAAINRAQ EGQDIVAPRA DLTHAGNFLY MLTGNEPTPE QARLFDIALV
     LHADHGMNAS TFTAIATSST LSDMYSCMVS AIGALKGPLH GGANEAVMTM LDEIGTVDKA
     EAYITGKLDN KEKIMGVGHR VYKYFDPRSR VLRDYAEHVA NKEGKSNYYQ ILEAIEKIIV
     DRMGAKGIYP NVDFYSGTVY SDLGIKKEYF TPIFALARIS GWCASVIEYS QDNRLLRPDA
     EYTGARDQHY VDIKDRQ
//