ID   CISY2_MYCTU             Reviewed;         373 AA.
AC   P9WPD3; L0T808; P63777; Q10529;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Putative citrate synthase 2;
DE            EC=2.3.3.16;
GN   Name=citA; OrderedLocusNames=Rv0889c; ORFNames=MTCY31.17c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP43637.1; -; Genomic_DNA.
DR   PIR; F70781; F70781.
DR   RefSeq; NP_215404.1; NC_000962.3.
DR   RefSeq; WP_003898633.1; NZ_NVQJ01000001.1.
DR   AlphaFoldDB; P9WPD3; -.
DR   SMR; P9WPD3; -.
DR   STRING; 83332.Rv0889c; -.
DR   iPTMnet; P9WPD3; -.
DR   PaxDb; P9WPD3; -.
DR   DNASU; 885466; -.
DR   GeneID; 885466; -.
DR   KEGG; mtu:Rv0889c; -.
DR   TubercuList; Rv0889c; -.
DR   eggNOG; COG0372; Bacteria.
DR   OMA; YWTSAAE; -.
DR   PhylomeDB; P9WPD3; -.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
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   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   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; Reference proteome; Transferase;
KW   Tricarboxylic acid cycle.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:21969609"
FT   CHAIN           2..373
FT                   /note="Putative citrate synthase 2"
FT                   /id="PRO_0000169949"
FT   ACT_SITE        250
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0007744|PubMed:21969609"
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