ID   MMGD_BACSU              Reviewed;         372 AA.
AC   P45858;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Citrate/2-methylcitrate synthase {ECO:0000303|PubMed:28956599};
DE            EC=2.3.3.- {ECO:0000269|PubMed:28956599};
DE            EC=2.3.3.16 {ECO:0000269|PubMed:28956599};
DE   AltName: Full=2-methylcitrate synthase {ECO:0000250|UniProtKB:Q8NSL1};
DE            Short=2-MCS {ECO:0000250|UniProtKB:Q8NSL1};
DE            Short=MCS {ECO:0000250|UniProtKB:Q8NSL1};
DE   AltName: Full=Citrate synthase {ECO:0000303|PubMed:8759838};
GN   Name=mmgD {ECO:0000303|PubMed:8759838}; Synonyms=yqiO;
GN   OrderedLocusNames=BSU24140;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A CITRATE SYNTHASE,
RP   DEVELOPMENTAL STAGE, AND INDUCTION.
RC   STRAIN=168 / MB24;
RX   PubMed=8759838; DOI=10.1128/jb.178.16.4778-4786.1996;
RA   Bryan E.M., Beall B.W., Moran C.P. Jr.;
RT   "A sigma E dependent operon subject to catabolite repression during
RT   sporulation in Bacillus subtilis.";
RL   J. Bacteriol. 178:4778-4786(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=168;
RX   PubMed=28956599; DOI=10.1021/acs.biochem.7b00778;
RA   Reddick J.J., Sirkisoon S., Dahal R.A., Hardesty G., Hage N.E., Booth W.T.,
RA   Quattlebaum A.L., Mills S.N., Meadows V.G., Adams S.L.H., Doyle J.S.,
RA   Kiel B.E.;
RT   "First biochemical characterization of a methylcitric acid cycle from
RT   Bacillus subtilis strain 168.";
RL   Biochemistry 56:5698-5711(2017).
CC   -!- FUNCTION: Involved in both the tricarboxylic acid (TCA) and
CC       methylcitric acid cycles (PubMed:28956599). Has both 2-methylcitrate
CC       synthase and citrate synthase activities. Catalyzes the condensation of
CC       propionyl-CoA and oxaloacetate to yield 2-methylcitrate (2-MC) and CoA,
CC       and the condensation of acetyl-CoA and oxaloacetate to yield citrate
CC       and CoA (PubMed:8759838, PubMed:28956599). Has 2.3-fold higher activity
CC       as a 2-methylcitrate synthase (PubMed:28956599). Catalyzes the
CC       formation of either (2S,3R)- or (2R,3S)-2-methylcitrate
CC       (PubMed:28956599). {ECO:0000269|PubMed:28956599,
CC       ECO:0000269|PubMed:8759838}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + oxaloacetate + propanoyl-CoA = 2-methylcitrate + CoA +
CC         H(+); Xref=Rhea:RHEA:57492, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15598, ChEBI:CHEBI:16452, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57392; Evidence={ECO:0000269|PubMed:28956599};
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:28956599};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC       from oxaloacetate: step 1/2. {ECO:0000305|PubMed:28956599}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the mother cell at intermediate
CC       stages of sporulation under the control of the sigma-E factor.
CC       {ECO:0000269|PubMed:8759838}.
CC   -!- INDUCTION: Subject to catabolite repression.
CC       {ECO:0000269|PubMed:8759838}.
CC   -!- MISCELLANEOUS: Bifunctionality as a citrate and 2-methylcitrate
CC       synthase is likely important in the mother cell's physiological milieu.
CC       {ECO:0000305|PubMed:28956599}.
CC   -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR   EMBL; U29084; AAB09616.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12590.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14345.1; -; Genomic_DNA.
DR   PIR; E69658; E69658.
DR   RefSeq; NP_390294.1; NC_000964.3.
DR   RefSeq; WP_003230298.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P45858; -.
DR   SMR; P45858; -.
DR   STRING; 224308.BSU24140; -.
DR   PaxDb; 224308-BSU24140; -.
DR   EnsemblBacteria; CAB14345; CAB14345; BSU_24140.
DR   GeneID; 938665; -.
DR   KEGG; bsu:BSU24140; -.
DR   PATRIC; fig|224308.179.peg.2628; -.
DR   eggNOG; COG0372; Bacteria.
DR   InParanoid; P45858; -.
DR   OrthoDB; 9800864at2; -.
DR   PhylomeDB; P45858; -.
DR   BioCyc; BSUB:BSU24140-MONOMER; -.
DR   BRENDA; 2.3.3.16; 658.
DR   BRENDA; 2.3.3.5; 658.
DR   UniPathway; UPA00223; UER00717.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0050440; F:2-methylcitrate synthase activity; ISS:UniProtKB.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IBA:GO_Central.
DR   GO; GO:0036440; F:citrate synthase activity; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; ISS:UniProtKB.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   CDD; cd06118; citrate_synt_like_1; 1.
DR   Gene3D; 1.10.580.10; Citrate Synthase, domain 1; 1.
DR   Gene3D; 1.10.230.10; Cytochrome P450-Terp, domain 2; 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   PANTHER; PTHR11739; CITRATE SYNTHASE; 1.
DR   PANTHER; PTHR11739:SF11; CITRATE_2-METHYLCITRATE SYNTHASE; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PIRSF; PIRSF001369; Citrate_synth; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; Citrate synthase; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Sporulation; Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..372
FT                   /note="Citrate/2-methylcitrate synthase"
FT                   /id="PRO_0000169930"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000250|UniProtKB:O34002"
FT   ACT_SITE        262
FT                   /evidence="ECO:0000250|UniProtKB:O34002"
FT   ACT_SITE        314
FT                   /evidence="ECO:0000250|UniProtKB:O34002"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT   BINDING         256..260
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:O34002"
FT   BINDING         272
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT   BINDING         339
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT   BINDING         358
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
SQ   SEQUENCE   372 AA;  42106 MW;  29FD292E27B5F9F7 CRC64;
     MEEKQHYSPG LDGVIAAETH ISYLDTQSSQ ILIRGYDLIE LSETKSYLEL VHLLLEGRLP
     EESEMETLER KINSASSLPA DHLRLLELLP EDTHPMDGLR TGLSALAGYD RQIDDRSPSA
     NKERAYQLLG KMPALTAASY RIINKKEPIL PLQTLSYSAN FLYMMTGKLP SSLEEQIFDR
     SLVLYSEHEM PNSTFAARVI ASTHSDLYGA LTGAVASLKG NLHGGANEAV MYLLLEAKTT
     SDFEQLLQTK LKRKEKIMGF GHRVYMKKMD PRALMMKEAL QQLCDKAGDH RLYEMCEAGE
     RLMEKEKGLY PNLDYYAAPV YWMLGIPIPL YTPIFFSART SGLCAHVIEQ HANNRLFRPR
     VSYMGPRYQT KS
//