ID   SCPC_ECOLI              Reviewed;         492 AA.
AC   P52043; Q2M9S2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Propionyl-CoA:succinate CoA transferase;
DE            EC=2.8.3.-;
GN   Name=scpC; Synonyms=ygfH; OrderedLocusNames=b2920, JW2887;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=10769117; DOI=10.1021/bi992888d;
RA   Haller T., Buckel T., Retey J., Gerlt J.A.;
RT   "Discovering new enzymes and metabolic pathways: conversion of succinate to
RT   propionate by Escherichia coli.";
RL   Biochemistry 39:4622-4629(2000).
CC   -!- FUNCTION: Catalyzes the transfer of coenzyme A from propionyl-CoA to
CC       succinate. Could be part of a pathway that converts succinate to
CC       propionate. {ECO:0000269|PubMed:10769117}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=propanoyl-CoA + succinate = propanoate + succinyl-CoA;
CC         Xref=Rhea:RHEA:28010, ChEBI:CHEBI:17272, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:57392;
CC         Evidence={ECO:0000269|PubMed:10769117};
CC   -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC       {ECO:0000305}.
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DR   EMBL; U28377; AAA69087.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75957.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76984.1; -; Genomic_DNA.
DR   PIR; G65076; G65076.
DR   RefSeq; NP_417395.1; NC_000913.3.
DR   RefSeq; WP_000449965.1; NZ_SSZK01000003.1.
DR   AlphaFoldDB; P52043; -.
DR   SMR; P52043; -.
DR   BioGRID; 4262329; 6.
DR   DIP; DIP-12167N; -.
DR   IntAct; P52043; 9.
DR   STRING; 511145.b2920; -.
DR   PaxDb; P52043; -.
DR   PRIDE; P52043; -.
DR   EnsemblBacteria; AAC75957; AAC75957; b2920.
DR   EnsemblBacteria; BAE76984; BAE76984; BAE76984.
DR   GeneID; 947402; -.
DR   KEGG; ecj:JW2887; -.
DR   KEGG; eco:b2920; -.
DR   PATRIC; fig|1411691.4.peg.3812; -.
DR   EchoBASE; EB2800; -.
DR   eggNOG; COG0427; Bacteria.
DR   HOGENOM; CLU_019748_3_0_6; -.
DR   InParanoid; P52043; -.
DR   OMA; DEALSWH; -.
DR   PhylomeDB; P52043; -.
DR   BioCyc; EcoCyc:G7517-MON; -.
DR   BioCyc; MetaCyc:G7517-MON; -.
DR   PRO; PR:P52043; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008775; F:acetate CoA-transferase activity; IBA:GO_Central.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; IBA:GO_Central.
DR   GO; GO:0043821; F:propionyl-CoA:succinate CoA-transferase activity; IDA:EcoCyc.
DR   GO; GO:0006083; P:acetate metabolic process; IBA:GO_Central.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR   Gene3D; 3.40.1080.20; -; 1.
DR   InterPro; IPR026888; AcetylCoA_hyd_C.
DR   InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR   InterPro; IPR003702; ActCoA_hydro.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR017821; Succinate_CoA_transferase.
DR   Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR   Pfam; PF02550; AcetylCoA_hydro; 1.
DR   SUPFAM; SSF100950; SSF100950; 2.
DR   TIGRFAMs; TIGR03458; YgfH_subfam; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Transferase.
FT   CHAIN           1..492
FT                   /note="Propionyl-CoA:succinate CoA transferase"
FT                   /id="PRO_0000215527"
FT   ACT_SITE        286
FT                   /note="5-glutamyl coenzyme A thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         260..264
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         376
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
FT   BINDING         380
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:B3EY95"
SQ   SEQUENCE   492 AA;  53824 MW;  4C84C10B91D2CA65 CRC64;
     METQWTRMTA NEAAEIIQHN DMVAFSGFTP AGSPKALPTA IARRANEQHE AKKPYQIRLL
     TGASISAAAD DVLSDADAVS WRAPYQTSSG LRKKINQGAV SFVDLHLSEV AQMVNYGFFG
     DIDVAVIEAS ALAPDGRVWL TSGIGNAPTW LLRAKKVIIE LNHYHDPRVA ELADIVIPGA
     PPRRNSVSIF HAMDRVGTRY VQIDPKKIVA VVETNLPDAG NMLDKQNPMC QQIADNVVTF
     LLQEMAHGRI PPEFLPLQSG VGNINNAVMA RLGENPVIPP FMMYSEVLQE SVVHLLETGK
     ISGASASSLT ISADSLRKIY DNMDYFASRI VLRPQEISNN PEIIRRLGVI ALNVGLEFDI
     YGHANSTHVA GVDLMNGIGG SGDFERNAYL SIFMAPSIAK EGKISTVVPM CSHVDHSEHS
     VKVIITEQGI ADLRGLSPLQ RARTIIDNCA HPMYRDYLHR YLENAPGGHI HHDLSHVFDL
     HRNLIATGSM LG