PRPC_CUPNE
ID PRPC_CUPNE Reviewed; 385 AA.
AC Q937N9;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=2-methylcitrate synthase {ECO:0000303|PubMed:11495997};
DE Short=2-MCS {ECO:0000303|PubMed:11495997};
DE Short=MCS {ECO:0000303|PubMed:11495997};
DE EC=2.3.3.5 {ECO:0000269|PubMed:11495997};
DE AltName: Full=Citrate synthase {ECO:0000303|PubMed:11495997};
DE EC=2.3.3.16 {ECO:0000269|PubMed:11495997};
GN Name=prpC {ECO:0000303|PubMed:11495997};
OS Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=106590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=HF39;
RX PubMed=11495997; DOI=10.1099/00221287-147-8-2203;
RA Bramer C.O., Steinbuchel A.;
RT "The methylcitric acid pathway in Ralstonia eutropha: new genes identified
RT involved in propionate metabolism.";
RL Microbiology 147:2203-2214(2001).
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 but with a lower efficiency.
CC {ECO:0000269|PubMed:11495997}.
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:11495997};
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:11495997};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305|PubMed:11495997}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2. {ECO:0000305|PubMed:11495997}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P31660}.
CC -!- INDUCTION: By propionate. {ECO:0000305|PubMed:11495997}.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; AF325554; AAL03989.1; -; Genomic_DNA.
DR AlphaFoldDB; Q937N9; -.
DR SMR; Q937N9; -.
DR UniPathway; UPA00223; UER00717.
DR UniPathway; UPA00946; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0050440; F:2-methylcitrate synthase activity; IDA:UniProtKB.
DR GO; GO:0036440; F:citrate synthase activity; IDA:UniProtKB.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IDA:UniProtKB.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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 Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..385
FT /note="2-methylcitrate synthase"
FT /id="PRO_0000432968"
FT ACT_SITE 231
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT ACT_SITE 270
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT ACT_SITE 321
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 264..268
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:O34002"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
FT BINDING 365
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:I6Y9Q3"
SQ SEQUENCE 385 AA; 42508 MW; 5B2D9DE0230D7E19 CRC64;
MSEAQPLVTP KPKKSVALSG VTAGNTALCT VGRTGNDLHY RGYDILDIAE TCEFEEIAHL
LVHGKLPTKS ELAAYKAKLK SLRGLPANVK AALEWVPASA HPMDVMRTGV SVLGTVLPEK
EDHNTPGARD IADRLMASLG SMLLYWYHYS HNGRRIEVET DDDSIGGHFL HLLHGEKPSA
LWERAMNTSL NLYAEHEFNA STFTARVIAG TGSDMYSSIS GAIGALRGPK HGGANEVAFE
IQKRYDNPDE AQADITRRVE NKEVVIGFGH PVYTTGDPRN QVIKEVAKKL SKDAGSMKMF
DIAEALETVM WDIKKMFPNL DWFSAVSYHM MGVPTAMFTA LFVIARTSGW AAHIIEQRID
NKIIRQSANY TGPENLKFVP LKDRK
