ID   PRPC_MYCTE              Reviewed;         393 AA.
AC   H8F0D7;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=2-methylcitrate synthase {ECO:0000303|PubMed:16689789};
DE            Short=2-MCS {ECO:0000303|PubMed:16689789};
DE            Short=MCS {ECO:0000303|PubMed:16689789};
DE            EC=2.3.3.5 {ECO:0000269|PubMed:16689789};
DE   AltName: Full=Citrate synthase {ECO:0000303|PubMed:16689789};
DE            Short=CS {ECO:0000303|PubMed:16689789};
DE            EC=2.3.3.16 {ECO:0000269|PubMed:16689789};
GN   Name=gltA1; OrderedLocusNames=ERDMAN_1267; ORFNames=Q643_01184;
OS   Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=652616;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=22535945; DOI=10.1128/jb.00353-12;
RA   Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT   "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL   J. Bacteriol. 194:2770-2770(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Hung D., Gomez D., Hsueh P.R., Rozo J.C., Zambrano M.M.,
RA   Desjardins C., Abeel T., Young S., Zeng Q., Gargeya S., Abouelleil A.,
RA   Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., Murphy C.,
RA   Naylor J., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Mycobacterium tuberculosis Erdman.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, INDUCTION, AND
RP   SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX   PubMed=16689789; DOI=10.1111/j.1365-2958.2006.05155.x;
RA   Munoz-Elias E.J., Upton A.M., Cherian J., McKinney J.D.;
RT   "Role of the methylcitrate cycle in Mycobacterium tuberculosis metabolism,
RT   intracellular growth, and virulence.";
RL   Mol. Microbiol. 60:1109-1122(2006).
CC   -!- FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA)
CC       via the tricarboxylic acid (TCA)(acetyl degradation route) and via the
CC       2-methylcitrate cycle I (propionate degradation route). Catalyzes the
CC       Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield
CC       2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of
CC       oxaloacetate with acetyl-CoA. {ECO:0000269|PubMed:16689789}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + oxaloacetate + propanoyl-CoA = (2S,3S)-2-methylcitrate +
CC         CoA + H(+); Xref=Rhea:RHEA:23780, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57392, ChEBI:CHEBI:58853; EC=2.3.3.5;
CC         Evidence={ECO:0000269|PubMed:16689789};
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:0000269|PubMed:16689789};
CC   -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC       {ECO:0000305|PubMed:16689789}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 1/2. {ECO:0000305|PubMed:16689789}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:I6Y9Q3}.
CC   -!- INDUCTION: By propionate, but not by glucose.
CC       {ECO:0000269|PubMed:16689789}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking both prpC and prpD are unable to
CC       grow on propionate media in vitro or in murine bone marrow-derived
CC       macrophages infected ex vivo. Paradoxically, bacterial growth and
CC       persistence, and tissue pathology, are indistinguishable in mice
CC       infected with wild-type. {ECO:0000269|PubMed:16689789}.
CC   -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR   EMBL; AP012340; BAL65070.1; -; Genomic_DNA.
DR   EMBL; JLBG01000002; KBK19227.1; -; Genomic_DNA.
DR   RefSeq; WP_003405909.1; NZ_KK339487.1.
DR   AlphaFoldDB; H8F0D7; -.
DR   SMR; H8F0D7; -.
DR   EnsemblBacteria; BAL65070; BAL65070; ERDMAN_1267.
DR   GeneID; 45425104; -.
DR   KEGG; mtn:ERDMAN_1267; -.
DR   PATRIC; fig|652616.3.peg.1285; -.
DR   HOGENOM; CLU_025068_2_1_11; -.
DR   UniPathway; UPA00223; UER00717.
DR   UniPathway; UPA00946; -.
DR   Proteomes; UP000007568; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0050440; F:2-methylcitrate synthase activity; IDA:UniProtKB.
DR   GO; GO:0036440; F:citrate synthase activity; IDA:UniProtKB.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..393
FT                   /note="2-methylcitrate synthase"
FT                   /id="PRO_0000432970"
FT   ACT_SITE        242
FT                   /evidence="ECO:0000250|UniProtKB:O34002"
FT   ACT_SITE        281
FT                   /evidence="ECO:0000250|UniProtKB:O34002"
FT   ACT_SITE        332
FT                   /evidence="ECO:0000250|UniProtKB:O34002"
FT   BINDING         92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT   BINDING         275..279
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:O34002"
FT   BINDING         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT   BINDING         357
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT   BINDING         376
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
SQ   SEQUENCE   393 AA;  42969 MW;  5591E9F482CF1232 CRC64;
     MTGPLAAARS VAATKSMTAP TVDERPDIKK GLAGVVVDTT AISKVVPQTN SLTYRGYPVQ
     DLAARCSFEQ VAFLLWRGEL PTDAELALFS QRERASRRVD RSMLSLLAKL PDNCHPMDVV
     RTAISYLGAE DPDEDDAAAN RAKAMRMMAV LPTIVAIDMR RRRGLPPIAP HSGLGYAQNF
     LHMCFGEVPE TAVVSAFEQS MILYAEHGFN ASTFAARVVT STQSDIYSAV TGAIGALKGR
     LHGGANEAVM HDMIEIGDPA NAREWLRAKL ARKEKIMGFG HRVYRHGDSR VPTMKRALER
     VGTVRDGQRW LDIYQVLAAE MASATGILPN LDFPTGPAYY LMGFDIASFT PIFVMSRITG
     WTAHIMEQAT ANALIRPLSA YCGHEQRVLP GTF