ID   BBSG_THAAR              Reviewed;         406 AA.
AC   Q9KJE8;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=(R)-benzylsuccinyl-CoA dehydrogenase;
DE            EC=1.3.8.3;
GN   Name=bbsG;
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 1-10, 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   PROTEIN SEQUENCE OF 1-6, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RC   STRAIN=DSM 6984 / CIP 107765 / K172;
RX   PubMed=12420174; DOI=10.1007/s00203-002-0484-5;
RA   Leutwein C., Heider J.;
RT   "(R)-benzylsuccinyl-CoA dehydrogenase of Thauera aromatica, an enzyme of
RT   the anaerobic toluene catabolic pathway.";
RL   Arch. Microbiol. 178:517-524(2002).
CC   -!- FUNCTION: Catalyzes the oxidation of benzylsuccinyl-CoA to
CC       benzylidenesuccinyl-CoA. {ECO:0000269|PubMed:12420174}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-2-benzylsuccinyl-CoA + H(+) + oxidized [electron-transfer
CC         flavoprotein] = (E)-2-benzylidenesuccinyl-CoA + reduced [electron-
CC         transfer flavoprotein]; Xref=Rhea:RHEA:20876, Rhea:RHEA-COMP:10685,
CC         Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57253,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:58519; EC=1.3.8.3;
CC         Evidence={ECO:0000269|PubMed:12420174};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:12420174};
CC   -!- ACTIVITY REGULATION: Inhibited by (S)-benzylsuccinyl-CoA.
CC       {ECO:0000269|PubMed:12420174}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=110 uM for benzylsuccinyl-CoA {ECO:0000269|PubMed:12420174};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:12420174};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.
CC         {ECO:0000269|PubMed:12420174};
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC       {ECO:0000269|PubMed:10629170, ECO:0000269|PubMed:12420174}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12420174}.
CC   -!- INDUCTION: Induced by toluene. {ECO:0000269|PubMed:10629170}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AF173961; AAF89842.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KJE8; -.
DR   SMR; Q9KJE8; -.
DR   KEGG; ag:AAF89842; -.
DR   BioCyc; MetaCyc:MON-687; -.
DR   UniPathway; UPA00273; -.
DR   GO; GO:0033734; F:(R)-benzylsuccinyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; FAD;
KW   Flavoprotein; Oxidoreductase.
FT   CHAIN           1..406
FT                   /note="(R)-benzylsuccinyl-CoA dehydrogenase"
FT                   /id="PRO_0000201205"
SQ   SEQUENCE   406 AA;  45583 MW;  FC6B7DDC3BD48B11 CRC64;
     MDFSLSEEQT MLKEVARRFT ANELMPLEKV LLEREMRMWT DGYTLLPEAD HARLMKITQE
     MGFWGIEVDE KLGGQGLGMF AKTLVVEEMS KSLIGFSHHG FTLPPDAPNL YYLEECGSPA
     QRDKYVRRYC RGEIDSAMMA TEPGAGSDIS GLTTTAVREN GQWVINGSKI FISKCDKDEL
     FFICIAVTDK EAPTKRRFTA FILDKDTPGL RIGAEIPVIG AMPTWSVYLD NVRVGDEAVL
     GEVGDAFIPL QNRFGVRRIE LAAHCTGMAE RLIQMMIDQA NLRKTFGVAL ADRQTVQNWI
     ADSTIELEQV RLQLYFTAWK SDQGHKDLRL EAASLKIAAT EMLTRVADRA IQLHGGLGLS
     REMGIEYVAR MVRIWRVVEG ASEIHRMSIA KKLLTDGRTY SPFVAA