MMGD_BACSU
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 03-AUG-2022, entry version 144.
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; Firmicutes; 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; P45858; -.
DR PRIDE; P45858; -.
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 OMA; LTYCGYD; -.
DR PhylomeDB; P45858; -.
DR BioCyc; BSUB:BSU24140-MON; -.
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 Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 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; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 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
