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 01-MAY-2013, entry version 89.
DE RecName: Full=2-methylcitrate synthase;
DE EC=2.3.3.5;
DE AltName: Full=Citrate synthase 2;
DE AltName: Full=Methylcitrate synthase;
GN Name=prpC; OrderedLocusNames=STM0369;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=9006051;
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
RT encodes a member of the sigma-54 family of activators, and the prpBCDE
RT genes 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.,
RA Waterston R., Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, AND PATHWAY.
RX PubMed=10482501;
RA Horswill A.R., Escalante-Semerena J.C.;
RT "Salmonella typhimurium LT2 catabolizes propionate via the 2-
RT methylcitric acid cycle.";
RL J. Bacteriol. 181:5615-5623(1999).
CC -!- FUNCTION: Catalyzes the synthesis of 2-methylcitrate from
CC propionyl-CoA and oxaloacetate. Also catalyzes the condensation of
CC oxaloacetate with acetyl-CoA but with a lower specificity.
CC -!- CATALYTIC ACTIVITY: Propanoyl-CoA + H(2)O + oxaloacetate =
CC (2R,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA.
CC -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC -!- SUBUNIT: Homodimer (Probable).
CC -!- SIMILARITY: Belongs to the citrate synthase family.
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DR EMBL; U51879; AAC44815.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19323.1; -; Genomic_DNA.
DR RefSeq; NP_459364.1; NC_003197.1.
DR PDB; 3O8J; X-ray; 2.41 A; A/B/C/D/E/F/G/H/I/J=1-389.
DR PDBsum; 3O8J; -.
DR ProteinModelPortal; 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; 32379059; VBISalEnt20916_0391.
DR eggNOG; COG0372; -.
DR HOGENOM; HOG000021225; -.
DR KO; K01659; -.
DR OMA; HVIEYVE; -.
DR ProtClustDB; PRK12351; -.
DR BioCyc; MetaCyc:MONOMER-63; -.
DR BRENDA; 2.3.3.5; 2169.
DR UniPathway; UPA00946; -.
DR EvolutionaryTrace; Q56063; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0050440; F:2-methylcitrate synthase activity; IEA:EC.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR InterPro; IPR011278; 2-MeCitrate/Citrate_synth_I.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase-like.
DR InterPro; IPR016141; Citrate_synthase-like_core.
DR InterPro; IPR019810; Citrate_synthase_AS.
DR InterPro; IPR024176; Citrate_synthase_bac-typ.
DR PANTHER; PTHR11739; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PIRSF; PIRSF001369; Citrate_synth; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; Citrate_synthase_core; 1.
DR TIGRFAMs; TIGR01800; cit_synth_II; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Reference proteome; Transferase.
FT CHAIN 1 389 2-methylcitrate synthase.
FT /FTId=PRO_0000169982.
FT ACT_SITE 274 274 By similarity.
FT ACT_SITE 325 325 By similarity.
FT CONFLICT 144 144 S -> N (in Ref. 1; AAC44815).
FT STRAND 29 35
FT STRAND 42 44
FT HELIX 49 55
FT HELIX 58 66
FT STRAND 67 69
FT HELIX 73 84
FT HELIX 91 98
FT HELIX 106 120
FT HELIX 129 156
FT HELIX 169 178
FT HELIX 184 196
FT STRAND 201 203
FT HELIX 204 213
FT TURN 214 216
FT HELIX 219 230
FT TURN 233 235
FT HELIX 238 246
FT HELIX 252 264
FT HELIX 282 298
FT HELIX 302 318
FT TURN 324 326
FT HELIX 327 334
FT HELIX 339 341
FT HELIX 342 363
FT STRAND 372 374
FT HELIX 385 387
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
//
