ID   CISY_CORGL              Reviewed;         437 AA.
AC   P42457;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Citrate synthase;
DE            EC=2.3.3.16;
GN   Name=gltA; OrderedLocusNames=Cgl0829, cg0949;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=7522844; DOI=10.1099/13500872-140-8-1817;
RA   Eikmanns B.J., Thum-Schmitz N., Eggeling L., Luedtke K.U., Sahm H.;
RT   "Nucleotide sequence, expression and transcriptional analysis of the
RT   Corynebacterium glutamicum gltA gene encoding citrate synthase.";
RL   Microbiology 140:1817-1828(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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: Weakly inhibited by ATP (apparent Ki = 10 mm).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 1/2.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
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; X66112; CAA46902.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB98222.1; -; Genomic_DNA.
DR   EMBL; BX927150; CAF19535.1; -; Genomic_DNA.
DR   PIR; I40717; I40717.
DR   RefSeq; NP_600058.1; NC_003450.3.
DR   RefSeq; WP_011013914.1; NC_006958.1.
DR   AlphaFoldDB; P42457; -.
DR   SMR; P42457; -.
DR   STRING; 196627.cg0949; -.
DR   KEGG; cgb:cg0949; -.
DR   KEGG; cgl:Cgl0829; -.
DR   PATRIC; fig|196627.13.peg.813; -.
DR   eggNOG; COG0372; Bacteria.
DR   HOGENOM; CLU_025068_0_0_11; -.
DR   OMA; TVGWCAQ; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000000582; 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..437
FT                   /note="Citrate synthase"
FT                   /id="PRO_0000169940"
FT   ACT_SITE        316
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        372
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   437 AA;  48929 MW;  921780BF2C59676B CRC64;
     MFERDIVATD NNKAVLHYPG GEFEMDIIEA SEGNNGVVLG KMLSETGLIT FDPGYVSTGS
     TESKITYIDG DAGILRYRGY DIADLAENAT FNEVSYLLIN GELPTPDELH KFNDEIRHHT
     LLDEDFKSQF NVFPRDAHPM ATLASSVNIL STYYQDQLNP LDEAQLDKAT VRLMAKVPML
     AAYAHRARKG APYMYPDNSL NARENFLRMM FGYPTEPYEI DPIMVKALDK LLILHADHEQ
     NCSTSTVRMI GSAQANMFVS IAGGINALSG PLHGGANQAV LEMLEDIKSN HGGDATEFMN
     KVKNKEDGVR LMGFGHRVYK NYDPRAAIVK ETAHEILEHL GGDDLLDLAI KLEEIALADD
     YFISRKLYPN VDFYTGLIYR AMGFPTDFFT VLFAIGRLPG WIAHYREQLG AAGNKINRPR
     QVYTGNESRK LVPREER