ID   BBSF_THAAR              Reviewed;         409 AA.
AC   Q9KJE9;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Succinyl-CoA:(R)-benzylsuccinate CoA-transferase subunit BbsF;
DE            EC=2.8.3.15;
GN   Name=bbsF;
OS   Thauera aromatica.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=59405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, PATHWAY,
RP   INDUCTION, AND GENE NAME.
RC   STRAIN=DSM 6984 / CIP 107765 / K172;
RX   PubMed=10629170; DOI=10.1128/jb.182.2.272-277.2000;
RA   Leuthner B., Heider J.;
RT   "Anaerobic toluene catabolism of Thauera aromatica: the bbs operon codes
RT   for enzymes of beta-oxidation of the intermediate benzylsuccinate.";
RL   J. Bacteriol. 182:272-277(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, PATHWAY, AND SUBUNIT.
RC   STRAIN=DSM 6984 / CIP 107765 / K172;
RX   PubMed=11418570; DOI=10.1128/jb.183.14.4288-4295.2001;
RA   Leutwein C., Heider J.;
RT   "Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: an enzyme of the
RT   anaerobic toluene catabolic pathway in denitrifying bacteria.";
RL   J. Bacteriol. 183:4288-4295(2001).
CC   -!- FUNCTION: Catalyzes the reversible conversion of (R)-2-benzylsuccinate
CC       to (R)-2-benzylsuccinyl-CoA. Inactive with (S)-benzylsuccinate.
CC       {ECO:0000269|PubMed:11418570}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-benzylsuccinate + succinyl-CoA = (R)-2-benzylsuccinyl-
CC         CoA + succinate; Xref=Rhea:RHEA:16469, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:57253, ChEBI:CHEBI:57292, ChEBI:CHEBI:58692; EC=2.8.3.15;
CC         Evidence={ECO:0000269|PubMed:11418570};
CC   -!- ACTIVITY REGULATION: Inhibited by (S)-benzylsuccinyl-CoA.
CC       {ECO:0000269|PubMed:11418570}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=40 uM for (R)-2-benzylsuccinyl-CoA {ECO:0000269|PubMed:11418570};
CC         KM=160 uM for succinate {ECO:0000269|PubMed:11418570};
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC       {ECO:0000269|PubMed:10629170, ECO:0000269|PubMed:11418570}.
CC   -!- SUBUNIT: Heterotetramer composed of 2 BbsE subunits and 2 BbsF
CC       subunits. {ECO:0000269|PubMed:11418570}.
CC   -!- INDUCTION: Induced by toluene. {ECO:0000269|PubMed:10629170}.
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR   EMBL; AF173961; AAF89841.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KJE9; -.
DR   SMR; Q9KJE9; -.
DR   KEGG; ag:AAF89841; -.
DR   BioCyc; MetaCyc:MON-686; -.
DR   SABIO-RK; Q9KJE9; -.
DR   UniPathway; UPA00273; -.
DR   GO; GO:0033877; F:succinyl-CoA:(R)-benzylsuccinate CoA-transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.1540.10; -; 1.
DR   Gene3D; 3.40.50.10540; -; 1.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR   Pfam; PF02515; CoA_transf_3; 1.
DR   SUPFAM; SSF89796; SSF89796; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..409
FT                   /note="Succinyl-CoA:(R)-benzylsuccinate CoA-transferase
FT                   subunit BbsF"
FT                   /id="PRO_0000418887"
FT   ACT_SITE        178
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  44929 MW;  FE4DB50CD97C6FEA CRC64;
     MPNSIERALE GIVVCDFSWV GAGPIATSVL AQCGADVIKI ESVKRPDTLR RGEPFKDGIG
     TGLDRSGYFA ARNANKRDIA LDMSHPRARE VAVRLIEKSD IVINNFRVGQ MEKWKLGWED
     VQKINPRAIY VTMSMQGIDG PHSRYMGYGV NLNALCGLTA RAGFPGQAPF GTGTNYTDHV
     MVPTHTLFGI MAALLEREAT GRGQTVSLSQ LESAICMTPS APMAFAANGE ALGPQGYGDP
     EAAPHGVYTT LGYRKWIAIA VFDDAQWATL RRVMGNPPWA EDERFATIEM RRRHAAELDE
     RIEGWTATQY GDWLMEALLK AGVAAGEVRD AREAIEDEHL RRRGFWAYLD HPEVGVTLYN
     RAPIVFSRTP VEMKSAAPSI GQHTREVLGG MLGYSHGEIE DLAAQQVLV