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Protein

2-methylcitrate synthase

Gene

prpC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

Propanoyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA.2 Publications
Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.2 Publications

Kineticsi

  1. KM=5 µM for oxaloacetate (at pH 8 and 35 degrees Celsius)1 Publication
  2. KM=17 µM for propionyl-CoA (at pH 7.4)1 Publication
  3. KM=37 µM for propionyl-CoA (at pH 8 and 35 degrees Celsius)1 Publication
  4. KM=101 µM for acetyl-CoA (at pH 8 and 35 degrees Celsius)1 Publication
  1. Vmax=0.11 µmol/min/mg enzyme with acetyl-CoA as substrate (at pH 8 and 35 degrees Celsius)1 Publication
  2. Vmax=0.33 µmol/min/mg enzyme with propionyl-CoA as substrate (at pH 8 and 35 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 9.1 Publication

Temperature dependencei

Optimum temperature is between 45 and 50 degrees Celsius.1 Publication

Pathwayi: propanoate degradation

This protein is involved in the pathway propanoate degradation, which is part of Organic acid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway propanoate degradation and in Organic acid metabolism.

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 2 of the subpathway that synthesizes isocitrate from oxaloacetate.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Citrate synthase (gltA)
  2. Aconitate hydratase B (acnB), 2-methylcitrate dehydratase (prpD), Aconitate hydratase A (acnA), 2-methylcitrate synthase (prpC)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei82 – 821SubstrateBy similarity
Binding sitei200 – 2001SubstrateBy similarity
Active sitei235 – 2351By similarity
Active sitei274 – 2741By similarity
Binding sitei283 – 2831SubstrateBy similarity
Active sitei325 – 3251By similarity
Binding sitei350 – 3501SubstrateBy similarity
Binding sitei369 – 3691SubstrateBy similarity

GO - Molecular functioni

  • 2-methylcitrate synthase activity Source: UniProtKB
  • citrate (Si)-synthase activity Source: UniProtKB

GO - Biological processi

  • propionate metabolic process, methylcitrate cycle Source: UniProtKB
  • tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciEcoCyc:G6198-MONOMER.
ECOL316407:JW0324-MONOMER.
MetaCyc:G6198-MONOMER.
BRENDAi2.3.3.5. 2026.
UniPathwayiUPA00223; UER00718.
UPA00946.

Names & Taxonomyi

Protein namesi
Recommended name:
2-methylcitrate synthase1 Publication (EC:2.3.3.52 Publications)
Short name:
2-MCS1 Publication
Short name:
MCS1 Publication
Alternative name(s):
(2S,3S)-2-methylcitrate synthase1 Publication
Citrate synthase1 Publication (EC:2.3.3.162 Publications)
Gene namesi
Name:prpC1 Publication
Synonyms:yahS, yzzD
Ordered Locus Names:b0333, JW0324
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11756. prpC.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3893892-methylcitrate synthasePRO_0000169981Add
BLAST

Proteomic databases

PaxDbiP31660.

Expressioni

Inductioni

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.5 Publications

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4259809. 8 interactions.
DIPiDIP-10579N.
IntActiP31660. 2 interactions.
STRINGi511145.b0333.

Structurei

3D structure databases

ProteinModelPortaliP31660.
SMRiP31660. Positions 26-388.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni268 – 2725Coenzyme A bindingBy similarity

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105BZN. Bacteria.
COG0372. LUCA.
HOGENOMiHOG000021225.
InParanoidiP31660.
KOiK01659.
OMAiPSEEWIQ.
OrthoDBiEOG6P8TP4.
PhylomeDBiP31660.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR011278. 2-MeCitrate/Citrate_synth_II.
IPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01800. cit_synth_II. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31660-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDTTILQNS THVIKPKKSV ALSGVPAGNT ALCTVGKSGN DLHYRGYDIL
60 70 80 90 100
DLAKHCEFEE VAHLLIHGKL PTRDELAAYK TKLKALRGLP ANVRTVLEAL
110 120 130 140 150
PAASHPMDVM RTGVSALGCT LPEKEGHTVS GARDIADKLL ASLSSILLYW
160 170 180 190 200
YHYSHNGERI QPETDDDSIG GHFLHLLHGE KPSQSWEKAM HISLVLYAEH
210 220 230 240 250
EFNASTFTSR VIAGTGSDMY SAIIGAIGAL RGPKHGGANE VSLEIQQRYE
260 270 280 290 300
TPDEAEADIR KRVENKEVVI GFGHPVYTIA DPRHQVIKRV AKQLSQEGGS
310 320 330 340 350
LKMYNIADRL ETVMWESKKM FPNLDWFSAV SYNMMGVPTE MFTPLFVIAR
360 370 380
VTGWAAHIIE QRQDNKIIRP SANYVGPEDR PFVALDKRQ
Length:389
Mass (Da):43,102
Last modified:November 1, 1997 - v2
Checksum:i02B779E7AD4581C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73857 Genomic DNA. Translation: AAB18057.1.
U00096 Genomic DNA. Translation: AAC73436.1.
AP009048 Genomic DNA. Translation: BAE76115.1.
PIRiE64760.
RefSeqiNP_414867.1. NC_000913.3.
WP_001285927.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73436; AAC73436; b0333.
BAE76115; BAE76115; BAE76115.
GeneIDi947528.
KEGGiecj:JW0324.
eco:b0333.
PATRICi32115797. VBIEscCol129921_0340.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73857 Genomic DNA. Translation: AAB18057.1.
U00096 Genomic DNA. Translation: AAC73436.1.
AP009048 Genomic DNA. Translation: BAE76115.1.
PIRiE64760.
RefSeqiNP_414867.1. NC_000913.3.
WP_001285927.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP31660.
SMRiP31660. Positions 26-388.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259809. 8 interactions.
DIPiDIP-10579N.
IntActiP31660. 2 interactions.
STRINGi511145.b0333.

Proteomic databases

PaxDbiP31660.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73436; AAC73436; b0333.
BAE76115; BAE76115; BAE76115.
GeneIDi947528.
KEGGiecj:JW0324.
eco:b0333.
PATRICi32115797. VBIEscCol129921_0340.

Organism-specific databases

EchoBASEiEB1706.
EcoGeneiEG11756. prpC.

Phylogenomic databases

eggNOGiENOG4105BZN. Bacteria.
COG0372. LUCA.
HOGENOMiHOG000021225.
InParanoidiP31660.
KOiK01659.
OMAiPSEEWIQ.
OrthoDBiEOG6P8TP4.
PhylomeDBiP31660.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00718.
UPA00946.
BioCyciEcoCyc:G6198-MONOMER.
ECOL316407:JW0324-MONOMER.
MetaCyc:G6198-MONOMER.
BRENDAi2.3.3.5. 2026.

Miscellaneous databases

PROiP31660.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR011278. 2-MeCitrate/Citrate_synth_II.
IPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01800. cit_synth_II. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of minutes 4-25 of Escherichia coli."
    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.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Does Escherichia coli possess a second citrate synthase gene?"
    Patton A.J., Hough D.W., Towner P., Danson M.J.
    Eur. J. Biochem. 214:75-81(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 18-54, FUNCTION.
  5. "Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria."
    Textor S., Wendisch V.F., de Graaf A.A., Mueller U., Linder M.I., Linder D., Buckel W.
    Arch. Microbiol. 168:428-436(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.
  6. "Citrate synthase and 2-methylcitrate synthase: structural, functional and evolutionary relationships."
    Gerike U., Hough D.W., Russell N.J., Dyall-Smith M.L., Danson M.J.
    Microbiology 144:929-935(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, SUBSTRATE SPECIFICITY, SUBUNIT.
  7. "Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase."
    Brock M., Maerker C., Schuetz A., Voelker U., Buckel W.
    Eur. J. Biochem. 269:6184-6194(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Catabolite repression of the propionate catabolic genes in Escherichia coli and Salmonella enterica: evidence for involvement of the cyclic AMP receptor protein."
    Lee S.K., Newman J.D., Keasling J.D.
    J. Bacteriol. 187:2793-2800(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  9. "The mechanism of sugar-mediated catabolite repression of the propionate catabolic genes in Escherichia coli."
    Park J.M., Vinuselvi P., Lee S.K.
    Gene 504:116-121(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiPRPC_ECOLI
AccessioniPrimary (citable) accession number: P31660
Secondary accession number(s): P77217, Q2MC91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1997
Last modified: January 20, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.