PRPC_ECOLI
ID PRPC_ECOLI Reviewed; 389 AA.
AC P31660; P77217; Q2MC91;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=2-methylcitrate synthase {ECO:0000303|PubMed:9579066};
DE Short=2-MCS {ECO:0000303|PubMed:9579066};
DE Short=MCS {ECO:0000303|PubMed:9579066};
DE EC=2.3.3.5 {ECO:0000269|PubMed:12473114, ECO:0000269|PubMed:9325432, ECO:0000269|PubMed:9579066};
DE AltName: Full=(2S,3S)-2-methylcitrate synthase {ECO:0000305|PubMed:12473114};
DE AltName: Full=Citrate synthase {ECO:0000303|PubMed:8508809};
DE EC=2.3.3.16 {ECO:0000269|PubMed:9325432, ECO:0000269|PubMed:9579066};
GN Name=prpC {ECO:0000303|PubMed:9579066}; Synonyms=yahS, yzzD;
GN OrderedLocusNames=b0333, JW0324;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 18-54, AND FUNCTION.
RX PubMed=8508809; DOI=10.1111/j.1432-1033.1993.tb17898.x;
RA Patton A.J., Hough D.W., Towner P., Danson M.J.;
RT "Does Escherichia coli possess a second citrate synthase gene?";
RL Eur. J. Biochem. 214:75-81(1993).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=9325432; DOI=10.1007/s002030050518;
RA Textor S., Wendisch V.F., de Graaf A.A., Mueller U., Linder M.I.,
RA Linder D., Buckel W.;
RT "Propionate oxidation in Escherichia coli: evidence for operation of a
RT methylcitrate cycle in bacteria.";
RL Arch. Microbiol. 168:428-436(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=9579066; DOI=10.1099/00221287-144-4-929;
RA Gerike U., Hough D.W., Russell N.J., Dyall-Smith M.L., Danson M.J.;
RT "Citrate synthase and 2-methylcitrate synthase: structural, functional and
RT evolutionary relationships.";
RL Microbiology 144:929-935(1998).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=12473114; DOI=10.1046/j.1432-1033.2002.03336.x;
RA Brock M., Maerker C., Schuetz A., Voelker U., Buckel W.;
RT "Oxidation of propionate to pyruvate in Escherichia coli. Involvement of
RT methylcitrate dehydratase and aconitase.";
RL Eur. J. Biochem. 269:6184-6194(2002).
RN [8]
RP INDUCTION.
RX PubMed=15805526; DOI=10.1128/jb.187.8.2793-2800.2005;
RA Lee S.K., Newman J.D., Keasling J.D.;
RT "Catabolite repression of the propionate catabolic genes in Escherichia
RT coli and Salmonella enterica: evidence for involvement of the cyclic AMP
RT receptor protein.";
RL J. Bacteriol. 187:2793-2800(2005).
RN [9]
RP INDUCTION.
RX PubMed=22579471; DOI=10.1016/j.gene.2012.04.074;
RA Park J.M., Vinuselvi P., Lee S.K.;
RT "The mechanism of sugar-mediated catabolite repression of the propionate
RT catabolic genes in Escherichia coli.";
RL Gene 504:116-121(2012).
RN [10]
RP FUNCTION, AND DISCUSSION OF STEREOCHEMISTRY.
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 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 to yield citrate but with a lower
CC specificity. {ECO:0000269|PubMed:12473114, ECO:0000269|PubMed:28956599,
CC ECO:0000269|PubMed:8508809, ECO:0000269|PubMed:9325432,
CC ECO:0000269|PubMed:9579066}.
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:12473114, ECO:0000269|PubMed:9325432,
CC ECO:0000269|PubMed:9579066};
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:0000269|PubMed:9325432,
CC ECO:0000269|PubMed:9579066};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for oxaloacetate (at pH 8 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:9579066};
CC KM=17 uM for propionyl-CoA (at pH 7.4) {ECO:0000269|PubMed:9325432};
CC KM=37 uM for propionyl-CoA (at pH 8 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:9579066};
CC KM=101 uM for acetyl-CoA (at pH 8 and 35 degrees Celsius)
CC {ECO:0000269|PubMed:9579066};
CC Vmax=0.11 umol/min/mg enzyme with acetyl-CoA as substrate (at pH 8
CC and 35 degrees Celsius) {ECO:0000269|PubMed:9579066};
CC Vmax=0.33 umol/min/mg enzyme with propionyl-CoA as substrate (at pH 8
CC and 35 degrees Celsius) {ECO:0000269|PubMed:9579066};
CC pH dependence:
CC Optimum pH is 9. {ECO:0000269|PubMed:9325432};
CC Temperature dependence:
CC Optimum temperature is between 45 and 50 degrees Celsius.
CC {ECO:0000269|PubMed:9325432};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305|PubMed:9325432}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2. {ECO:0000305|PubMed:9325432}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9579066}.
CC -!- INDUCTION: By propionate, but not acetate or glucose. Expression of
CC prpBCDE operon is regulated by PrpR, CRP and a variety of sugars such
CC as arabinose, galactose, glucose mannose and xylose.
CC {ECO:0000269|PubMed:12473114, ECO:0000269|PubMed:15805526,
CC ECO:0000269|PubMed:22579471, ECO:0000269|PubMed:9325432,
CC ECO:0000269|PubMed:9579066}.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
CC -!- CAUTION: There is uncertainty concerning the 2-methylcitrate
CC stereochemistry. Brock et al. report a (2S,3S) stereochemistry, but
CC Reddick et al. determined that the 2-methylcitrate has either (2S,3R)
CC or (2R,3S) stereochemistry. {ECO:0000305|PubMed:12473114,
CC ECO:0000305|PubMed:28956599}.
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DR EMBL; U73857; AAB18057.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73436.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76115.1; -; Genomic_DNA.
DR PIR; E64760; E64760.
DR RefSeq; NP_414867.1; NC_000913.3.
DR RefSeq; WP_001285927.1; NZ_SSZK01000063.1.
DR AlphaFoldDB; P31660; -.
DR SMR; P31660; -.
DR BioGRID; 4259809; 8.
DR DIP; DIP-10579N; -.
DR IntAct; P31660; 2.
DR STRING; 511145.b0333; -.
DR jPOST; P31660; -.
DR PaxDb; P31660; -.
DR PRIDE; P31660; -.
DR EnsemblBacteria; AAC73436; AAC73436; b0333.
DR EnsemblBacteria; BAE76115; BAE76115; BAE76115.
DR GeneID; 947528; -.
DR KEGG; ecj:JW0324; -.
DR KEGG; eco:b0333; -.
DR PATRIC; fig|1411691.4.peg.1944; -.
DR EchoBASE; EB1706; -.
DR eggNOG; COG0372; Bacteria.
DR HOGENOM; CLU_025068_2_1_6; -.
DR InParanoid; P31660; -.
DR OMA; NEAVMHM; -.
DR PhylomeDB; P31660; -.
DR BioCyc; EcoCyc:G6198-MON; -.
DR BioCyc; MetaCyc:G6198-MON; -.
DR BRENDA; 2.3.3.5; 2026.
DR UniPathway; UPA00223; UER00717.
DR UniPathway; UPA00946; -.
DR PRO; PR:P31660; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0050440; F:2-methylcitrate synthase activity; IDA:UniProtKB.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IDA:UniProtKB.
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; 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 Direct protein sequencing; Reference proteome; Transferase;
KW Tricarboxylic acid cycle.
FT CHAIN 1..389
FT /note="2-methylcitrate synthase"
FT /id="PRO_0000169981"
FT ACT_SITE 235
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT ACT_SITE 274
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT ACT_SITE 325
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 268..272
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 369
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
SQ SEQUENCE 389 AA; 43102 MW; 02B779E7AD4581C3 CRC64;
MSDTTILQNS THVIKPKKSV ALSGVPAGNT ALCTVGKSGN DLHYRGYDIL DLAKHCEFEE
VAHLLIHGKL PTRDELAAYK TKLKALRGLP ANVRTVLEAL PAASHPMDVM RTGVSALGCT
LPEKEGHTVS GARDIADKLL ASLSSILLYW YHYSHNGERI QPETDDDSIG GHFLHLLHGE
KPSQSWEKAM HISLVLYAEH EFNASTFTSR VIAGTGSDMY SAIIGAIGAL RGPKHGGANE
VSLEIQQRYE TPDEAEADIR KRVENKEVVI GFGHPVYTIA DPRHQVIKRV AKQLSQEGGS
LKMYNIADRL ETVMWESKKM FPNLDWFSAV SYNMMGVPTE MFTPLFVIAR VTGWAAHIIE
QRQDNKIIRP SANYVGPEDR PFVALDKRQ
