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2-methylcitrate synthase (2-MCS) (MCS) (EC 2.3.3.5) ((2S,3S)-2-methylcitrate synthase) (Citrate synthase) (EC 2.3.3.16)

 PRPC_ECOLI              Reviewed;         389 AA.
P31660; P77217; Q2MC91;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
28-MAR-2018, entry version 135.
RecName: Full=2-methylcitrate synthase {ECO:0000303|PubMed:9579066};
Short=2-MCS {ECO:0000303|PubMed:9579066};
Short=MCS {ECO:0000303|PubMed:9579066};
EC=2.3.3.5 {ECO:0000269|PubMed:9325432, ECO:0000269|PubMed:9579066};
AltName: Full=(2S,3S)-2-methylcitrate synthase {ECO:0000305|PubMed:12473114};
AltName: Full=Citrate synthase {ECO:0000303|PubMed:8508809};
EC=2.3.3.16 {ECO:0000269|PubMed:9325432, ECO:0000269|PubMed:9579066};
Name=prpC {ECO:0000303|PubMed:9579066}; Synonyms=yahS, yzzD;
OrderedLocusNames=b0333, JW0324;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
PROTEIN SEQUENCE OF 18-54, AND FUNCTION.
PubMed=8508809; DOI=10.1111/j.1432-1033.1993.tb17898.x;
Patton A.J., Hough D.W., Towner P., Danson M.J.;
"Does Escherichia coli possess a second citrate synthase gene?";
Eur. J. Biochem. 214:75-81(1993).
[5]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
INDUCTION.
PubMed=9325432; DOI=10.1007/s002030050518;
Textor S., Wendisch V.F., de Graaf A.A., Mueller U., Linder M.I.,
Linder D., Buckel W.;
"Propionate oxidation in Escherichia coli: evidence for operation of a
methylcitrate cycle in bacteria.";
Arch. Microbiol. 168:428-436(1997).
[6]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
INDUCTION, SUBSTRATE SPECIFICITY, AND SUBUNIT.
PubMed=9579066; DOI=10.1099/00221287-144-4-929;
Gerike U., Hough D.W., Russell N.J., Dyall-Smith M.L., Danson M.J.;
"Citrate synthase and 2-methylcitrate synthase: structural, functional
and evolutionary relationships.";
Microbiology 144:929-935(1998).
[7]
INDUCTION.
PubMed=12473114; DOI=10.1046/j.1432-1033.2002.03336.x;
Brock M., Maerker C., Schuetz A., Voelker U., Buckel W.;
"Oxidation of propionate to pyruvate in Escherichia coli. Involvement
of methylcitrate dehydratase and aconitase.";
Eur. J. Biochem. 269:6184-6194(2002).
[8]
INDUCTION.
PubMed=15805526; DOI=10.1128/JB.187.8.2793-2800.2005;
Lee S.K., Newman J.D., Keasling J.D.;
"Catabolite repression of the propionate catabolic genes in
Escherichia coli and Salmonella enterica: evidence for involvement of
the cyclic AMP receptor protein.";
J. Bacteriol. 187:2793-2800(2005).
[9]
INDUCTION.
PubMed=22579471; DOI=10.1016/j.gene.2012.04.074;
Park J.M., Vinuselvi P., Lee S.K.;
"The mechanism of sugar-mediated catabolite repression of the
propionate catabolic genes in Escherichia coli.";
Gene 504:116-121(2012).
-!- FUNCTION: Involved in the catabolism of short chain fatty acids
(SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route)
and via the 2-methylcitrate cycle I (propionate degradation
route). Catalyzes the Claisen condensation of propionyl-CoA and
oxaloacetate (OAA) to yield (2S,3S)-2-methylcitrate (2-MC) and
CoA. Also catalyzes the condensation of oxaloacetate with acetyl-
CoA to yield citrate but with a lower specificity.
{ECO:0000269|PubMed:8508809, ECO:0000269|PubMed:9325432,
ECO:0000269|PubMed:9579066}.
-!- CATALYTIC ACTIVITY: Propanoyl-CoA + H(2)O + oxaloacetate =
(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA.
{ECO:0000269|PubMed:9325432, ECO:0000269|PubMed:9579066}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + oxaloacetate = citrate +
CoA. {ECO:0000269|PubMed:9325432, ECO:0000269|PubMed:9579066}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5 uM for oxaloacetate (at pH 8 and 35 degrees Celsius)
{ECO:0000269|PubMed:9579066};
KM=17 uM for propionyl-CoA (at pH 7.4)
{ECO:0000269|PubMed:9325432};
KM=37 uM for propionyl-CoA (at pH 8 and 35 degrees Celsius)
{ECO:0000269|PubMed:9579066};
KM=101 uM for acetyl-CoA (at pH 8 and 35 degrees Celsius)
{ECO:0000269|PubMed:9579066};
Vmax=0.11 umol/min/mg enzyme with acetyl-CoA as substrate (at pH
8 and 35 degrees Celsius) {ECO:0000269|PubMed:9579066};
Vmax=0.33 umol/min/mg enzyme with propionyl-CoA as substrate (at
pH 8 and 35 degrees Celsius) {ECO:0000269|PubMed:9579066};
pH dependence:
Optimum pH is 9. {ECO:0000269|PubMed:9325432};
Temperature dependence:
Optimum temperature is between 45 and 50 degrees Celsius.
{ECO:0000269|PubMed:9325432};
-!- PATHWAY: Organic acid metabolism; propanoate degradation.
{ECO:0000305|PubMed:9325432}.
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
isocitrate from oxaloacetate: step 2/2.
{ECO:0000305|PubMed:9325432}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9579066}.
-!- INDUCTION: By propionate, but not acetate or glucose. Expression
of prpBCDE operon is regulated by PrpR, CRP and a variety of
sugars such as arabinose, galactose, glucose mannose and xylose.
{ECO:0000269|PubMed:12473114, ECO:0000269|PubMed:15805526,
ECO:0000269|PubMed:22579471, ECO:0000269|PubMed:9325432,
ECO:0000269|PubMed:9579066}.
-!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U73857; AAB18057.1; -; Genomic_DNA.
EMBL; U00096; AAC73436.1; -; Genomic_DNA.
EMBL; AP009048; BAE76115.1; -; Genomic_DNA.
PIR; E64760; E64760.
RefSeq; NP_414867.1; NC_000913.3.
RefSeq; WP_001285927.1; NZ_LN832404.1.
ProteinModelPortal; P31660; -.
SMR; P31660; -.
BioGrid; 4259809; 8.
DIP; DIP-10579N; -.
IntAct; P31660; 2.
STRING; 316407.85674475; -.
PaxDb; P31660; -.
PRIDE; P31660; -.
EnsemblBacteria; AAC73436; AAC73436; b0333.
EnsemblBacteria; BAE76115; BAE76115; BAE76115.
GeneID; 947528; -.
KEGG; ecj:JW0324; -.
KEGG; eco:b0333; -.
PATRIC; fig|1411691.4.peg.1944; -.
EchoBASE; EB1706; -.
EcoGene; EG11756; prpC.
eggNOG; ENOG4105BZN; Bacteria.
eggNOG; COG0372; LUCA.
HOGENOM; HOG000021225; -.
InParanoid; P31660; -.
KO; K01659; -.
OMA; LNKADYW; -.
PhylomeDB; P31660; -.
BioCyc; EcoCyc:G6198-MONOMER; -.
BioCyc; MetaCyc:G6198-MONOMER; -.
BRENDA; 2.3.3.5; 2026.
UniPathway; UPA00223; UER00718.
UniPathway; UPA00946; -.
PRO; PR:P31660; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:InterPro.
GO; GO:0050440; F:2-methylcitrate synthase activity; IDA:UniProtKB.
GO; GO:0004108; F:citrate (Si)-synthase activity; IDA:UniProtKB.
GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IDA:UniProtKB.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.230.10; -; 1.
Gene3D; 1.10.580.10; -; 2.
InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II.
InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
InterPro; IPR002020; Citrate_synthase.
InterPro; IPR019810; Citrate_synthase_AS.
InterPro; IPR024176; Citrate_synthase_bac-typ.
InterPro; IPR036969; Citrate_synthase_sf.
PANTHER; PTHR11739; PTHR11739; 1.
Pfam; PF00285; Citrate_synt; 1.
PIRSF; PIRSF001369; Citrate_synth; 1.
PRINTS; PR00143; CITRTSNTHASE.
SUPFAM; SSF48256; SSF48256; 1.
TIGRFAMs; TIGR01800; cit_synth_II; 1.
PROSITE; PS00480; CITRATE_SYNTHASE; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Reference proteome;
Transferase; Tricarboxylic acid cycle.
CHAIN 1 389 2-methylcitrate synthase.
/FTId=PRO_0000169981.
REGION 268 272 Coenzyme A binding.
{ECO:0000250|UniProtKB:O34002}.
ACT_SITE 235 235 {ECO:0000250|UniProtKB:O34002}.
ACT_SITE 274 274 {ECO:0000250|UniProtKB:O34002}.
ACT_SITE 325 325 {ECO:0000250|UniProtKB:O34002}.
BINDING 82 82 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 200 200 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 283 283 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 350 350 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
BINDING 369 369 Substrate.
{ECO:0000250|UniProtKB:I6Y9Q3}.
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


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