ID   CISY2_MYCTO             Reviewed;         373 AA.
AC   P9WPD2; L0T808; P63777; Q10529;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Putative citrate synthase 2;
DE            EC=2.3.3.16;
GN   Name=citA; OrderedLocusNames=MT0912;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45158.1; -; Genomic_DNA.
DR   PIR; F70781; F70781.
DR   RefSeq; WP_003898633.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPD2; -.
DR   SMR; P9WPD2; -.
DR   EnsemblBacteria; AAK45158; AAK45158; MT0912.
DR   KEGG; mtc:MT0912; -.
DR   PATRIC; fig|83331.31.peg.981; -.
DR   HOGENOM; CLU_025068_2_1_11; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000001020; Chromosome.
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; -; 2.
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; IPR036969; Citrate_synthase_sf.
DR   PANTHER; PTHR11739; PTHR11739; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; SSF48256; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..373
FT                   /note="Putative citrate synthase 2"
FT                   /id="PRO_0000426972"
FT   ACT_SITE        250
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
SQ   SEQUENCE   373 AA;  40147 MW;  AABF5238CB79B54D CRC64;
     MTVVPENFVP GLDGVVAFTT EIAEPDKDGG ALRYRGVDIE DLVSQRVTFG DVWALLVDGN
     FGSGLPPAEP FPLPIHSGDV RVDVQAGLAM LAPIWGYAPL LDIDDATARQ QLARASVMAL
     SYVAQSARGI YQPAVPQRII DECSTVTARF MTRWQGEPDP RHIEAIDAYW VSAAEHGMNA
     STFTARVIAS TGADVAAALS GAIGAMSGPL HGGAPARVLP MLDEVERAGD ARSVVKGILD
     RGEKLMGFGH RVYRAEDPRA RVLRAAAERL GAPRYEVAVA VEQAALSELR ERRPDRAIET
     NVEFWAAVVL DFARVPANMM PAMFTCGRTA GWCAHILEQK RLGKLVRPSA IYVGPGPRSP
     ESVDGWERVL TTA