ID   CISY_MYCSM              Reviewed;         375 AA.
AC   P26491;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Citrate synthase;
DE            EC=2.3.3.16;
GN   Name=gltA;
OS   Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 607 / DSM 43465 / JCM 20379 / NBRC 3207 / NRRL B-692;
RX   PubMed=1883331; DOI=10.1042/bj2780225;
RA   David M., Lubinsky-Mink S., Benzvi A., Suissa M., Unitzur S., Kuhn J.C.;
RT   "Citrate synthase from Mycobacterium smegmatis. Cloning, sequence
RT   determination and expression in Escherichia coli.";
RL   Biochem. J. 278:225-234(1991).
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; X60513; CAA43028.1; -; Genomic_DNA.
DR   PIR; S17168; YKMY.
DR   AlphaFoldDB; P26491; -.
DR   SMR; P26491; -.
DR   UniPathway; UPA00223; UER00717.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0036440; F:citrate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.230.10; -; 1.
DR   Gene3D; 1.10.580.10; -; 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   PANTHER; PTHR11739; PTHR11739; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PIRSF; PIRSF001369; Citrate_synth; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; SSF48256; 1.
DR   TIGRFAMs; TIGR01800; cit_synth_II; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..375
FT                   /note="Citrate synthase"
FT                   /id="PRO_0000169951"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        317
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   375 AA;  41501 MW;  95D6D4E0C954C994 CRC64;
     MTTATESEAP RIHKGLAGVV VDTTAISKVV PETNSLTYRG YPVQDLAAQC SFEQVAYLLW
     HGELPTDQLA LFSQRERASR RIDRSMQALL AKLPDNCHPM DVVRTAISYL GAEDLEEDVD
     TAEANYAKSL RMFAVLPTIV ATDIRRRQGL TPIPPHSQLG YAQNFLNMCF GEVPEPVVVR
     AFEQSMVLYA EHSFNASTFA ARVVTSTQSD IYSAVTAAIG ALKGSLHGGA NEAVMHDMLE
     IGSAEKAPEW LHGKLSRKEK VMGFGHRVYK NGDSRVPTMK VALEQVAQVR DGQRWLDIYN
     TLESAMFAAT RIKPNLDFPT GPAYYLMDFP IESFTPLFVM SRITGWTAHI MEQAASNALI
     RPLSEYSGQP QRSLV