PRPC_SALTY
ID PRPC_SALTY Reviewed; 389 AA.
AC Q56063;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=2-methylcitrate synthase {ECO:0000303|PubMed:10482501};
DE Short=2-MCS {ECO:0000303|PubMed:20970504};
DE Short=mcs {ECO:0000303|PubMed:10482501};
DE EC=2.3.3.5 {ECO:0000269|PubMed:10482501, ECO:0000269|PubMed:20970504};
DE AltName: Full=Citrate synthase {ECO:0000303|PubMed:10482501};
DE EC=2.3.3.16 {ECO:0000269|PubMed:10482501, ECO:0000269|PubMed:20970504};
GN Name=prpC {ECO:0000303|PubMed:9006051}; OrderedLocusNames=STM0369;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=9006051; DOI=10.1128/jb.179.3.928-940.1997;
RA Horswill A.R., Escalante-Semerena J.C.;
RT "Propionate catabolism in Salmonella typhimurium LT2: two divergently
RT transcribed units comprise the prp locus at 8.5 centisomes, prpR encodes a
RT member of the sigma-54 family of activators, and the prpBCDE genes
RT constitute an operon.";
RL J. Bacteriol. 179:928-940(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=10482501; DOI=10.1128/jb.181.18.5615-5623.1999;
RA Horswill A.R., Escalante-Semerena J.C.;
RT "Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric
RT acid cycle.";
RL J. Bacteriol. 181:5615-5623(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=20970504; DOI=10.1016/j.jsb.2010.10.008;
RA Chittori S., Savithri H.S., Murthy M.R.;
RT "Crystal structure of Salmonella typhimurium 2-methylcitrate synthase:
RT Insights on domain movement and substrate specificity.";
RL J. Struct. Biol. 174:58-68(2011).
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 or butyryl-CoA but with a lower
CC specificity. {ECO:0000269|PubMed:10482501,
CC ECO:0000269|PubMed:20970504}.
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:10482501, ECO:0000269|PubMed:20970504};
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:10482501, ECO:0000269|PubMed:20970504};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 uM for oxaloacetate (with propionyl-CoA)
CC {ECO:0000269|PubMed:10482501};
CC KM=13 uM for oxaloacetate (with propionyl-CoA at pH 8 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:20970504};
CC KM=14 uM for oxaloacetate (with acetyl-CoA)
CC {ECO:0000269|PubMed:10482501};
CC KM=15 uM for oxaloacetate (with acetyl-CoA at pH 8 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:20970504};
CC KM=45 uM for propionyl-CoA (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:20970504};
CC KM=48 uM for propionyl-CoA {ECO:0000269|PubMed:10482501};
CC KM=265 uM for acetyl-CoA (at pH 8 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:20970504};
CC KM=285 uM for acetyl-CoA {ECO:0000269|PubMed:10482501};
CC Vmax=2 umol/min/mg enzyme with acetyl-CoA as substrate
CC {ECO:0000269|PubMed:10482501};
CC Vmax=2.5 umol/min/mg enzyme with acetyl-CoA as substrate (at pH 8 and
CC 30 degrees Celsius) {ECO:0000269|PubMed:20970504};
CC Vmax=10 umol/min/mg enzyme with propionyl-CoA as substrate
CC {ECO:0000269|PubMed:10482501};
CC Vmax=11 umol/min/mg enzyme with propionyl-CoA as substrate (at pH 8
CC and 30 degrees Celsius) {ECO:0000269|PubMed:20970504};
CC Note=kcat is 1.4 sec(-1) for citrate synthase activity with acetyl-
CC CoA as substrate. kcat is 1.87 sec(-1) for citrate synthase activity
CC with acetyl-CoA as substrate (at pH 8 and 30 degrees Celsius). kcat
CC is 7.4 sec(-1) for 2-methylcitrate synthase activity with propionyl-
CC CoA as substrate. kcat is 8.25 sec(-1) for 2-methylcitrate synthase
CC activity with propionyl-CoA as substrate (at pH 8 and 30 degrees
CC Celsius). {ECO:0000269|PubMed:10482501, ECO:0000269|PubMed:20970504};
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000305|PubMed:9006051}.
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2. {ECO:0000305|PubMed:9006051}.
CC -!- SUBUNIT: Homodimer at low concentrations and converted to a larger
CC oligomers at higher concentrations. {ECO:0000269|PubMed:10482501,
CC ECO:0000269|PubMed:20970504}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to accumulate
CC propionyl-CoA. {ECO:0000269|PubMed:10482501}.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; U51879; AAC44815.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19323.1; -; Genomic_DNA.
DR RefSeq; NP_459364.1; NC_003197.2.
DR RefSeq; WP_000132749.1; NC_003197.2.
DR PDB; 3O8J; X-ray; 2.41 A; A/B/C/D/E/F/G/H/I/J=1-389.
DR PDBsum; 3O8J; -.
DR AlphaFoldDB; Q56063; -.
DR SMR; Q56063; -.
DR STRING; 99287.STM0369; -.
DR PaxDb; Q56063; -.
DR PRIDE; Q56063; -.
DR EnsemblBacteria; AAL19323; AAL19323; STM0369.
DR GeneID; 1251888; -.
DR KEGG; stm:STM0369; -.
DR PATRIC; fig|99287.12.peg.391; -.
DR HOGENOM; CLU_025068_2_1_6; -.
DR OMA; NEAVMHM; -.
DR PhylomeDB; Q56063; -.
DR BioCyc; MetaCyc:MON-63; -.
DR BioCyc; SENT99287:STM0369-MON; -.
DR BRENDA; 2.3.3.5; 5542.
DR UniPathway; UPA00223; UER00717.
DR UniPathway; UPA00946; -.
DR EvolutionaryTrace; Q56063; -.
DR Proteomes; UP000001014; 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; IBA:GO_Central.
DR GO; GO:0036440; F:citrate 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 3D-structure; Reference proteome; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1..389
FT /note="2-methylcitrate synthase"
FT /id="PRO_0000169982"
FT ACT_SITE 235
FT /evidence="ECO:0000250|UniProtKB:O34002,
FT ECO:0000305|PubMed:20970504"
FT ACT_SITE 274
FT /evidence="ECO:0000250|UniProtKB:O34002,
FT ECO:0000305|PubMed:20970504"
FT ACT_SITE 325
FT /evidence="ECO:0000250|UniProtKB:O34002,
FT ECO:0000305|PubMed:20970504"
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"
FT CONFLICT 144
FT /note="S -> N (in Ref. 1; AAC44815)"
FT /evidence="ECO:0000305"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:3O8J"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:3O8J"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 106..120
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 129..156
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 169..178
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:3O8J"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:3O8J"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:3O8J"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 252..264
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 282..298
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 302..318
FT /evidence="ECO:0007829|PDB:3O8J"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 342..363
FT /evidence="ECO:0007829|PDB:3O8J"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:3O8J"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:3O8J"
SQ SEQUENCE 389 AA; 43173 MW; 0927008F1E5F38D4 CRC64;
MTDTTILQNN THVIKPKKSV ALSGVPAGNT ALCTVGKSGN DLHYRGYDIL DLAEHCEFEE
VAHLLIHGKL PTRDELNAYK SKLKALRGLP ANVRTVLEAL PAASHPMDVM RTGVSALGCT
LPEKEGHTVS GARDIADKLL ASLSSILLYW YHYSHNGERI QPETDDDSIG GHFLHLLHGE
KPTQSWEKAM HISLVLYAEH EFNASTFTSR VIAGTGSDVY SAIIGAIGAL RGPKHGGANE
VSLEIQQRYE TPDEAEADIR KRVENKEVVI GFGHPVYTIA DPRHQVIKRV AKQLSEEGGS
LKMYHIADRL ETVMWETKKM FPNLDWFSAV SYNMMGVPTE MFTPLFVIAR VTGWAAHIIE
QRQDNKIIRP SANYTGPEDR PFVSIDDRC
