ID   BBSE_THAAR              Reviewed;         410 AA.
AC   Q9KJF0;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Succinyl-CoA:(R)-benzylsuccinate CoA-transferase subunit BbsE;
DE            EC=2.8.3.15;
GN   Name=bbsE;
OS   Thauera aromatica.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=59405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF173961; AAF89840.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KJF0; -.
DR   SMR; Q9KJF0; -.
DR   KEGG; ag:AAF89840; -.
DR   BioCyc; MetaCyc:MON-685; -.
DR   SABIO-RK; Q9KJF0; -.
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                   /evidence="ECO:0000269|PubMed:10629170"
FT   CHAIN           2..410
FT                   /note="Succinyl-CoA:(R)-benzylsuccinate CoA-transferase
FT                   subunit BbsE"
FT                   /id="PRO_0000418886"
SQ   SEQUENCE   410 AA;  45613 MW;  C97BCD62B6D2697F CRC64;
     MGQDFSRFRV VDMTGELGPY TAKMFAGLGA DVIHVESPAG DPLRRVGPWF RNQPGVQASL
     PYLYYNAGKR GFAVDLEHEA GREVFRTLCS GADLLVESCR PGYLDGLGLS YEELSRDNAR
     LVQTSVTPFG RTGPLAAYPG SDLTCSALSG FLWLAGIDGD KPVRAPDNQA YRMAEAYAAV
     GSAIALFSAQ RTGKGQLVDV ACIEAEAMAL ENAAQFWDLE GKIRRGRGRE AGSATLHPCA
     DGYIALVAIM GRNKDMWTPF VRWMEAEGVE EWPLFDDDKW IDYAYRTSEE GYTTFCRVFE
     RYTRSRSKAE LYEIGQRFNV AVTPVSDGRD LLANPQLAHR EFWQTQFNDT LGADITYPGA
     PYEFGELQWQ LGRNAPRIGE HTREILVECG YPAFEIDNLL RMGAVYAEQH