ID   BSSA_THAAR              Reviewed;         861 AA.
AC   O87943;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Benzylsuccinate synthase alpha subunit;
DE            EC=4.1.99.11;
GN   Name=bssA;
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 2-31, FUNCTION,
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   PATHWAY, SUBUNIT, AND INDUCTION.
RC   STRAIN=DSM 6984 / CIP 107765 / K172;
RX   PubMed=9632263; DOI=10.1046/j.1365-2958.1998.00826.x;
RA   Leuthner B., Leutwein C., Schulz H., Horth P., Haehnel W., Schiltz E.,
RA   Schagger H., Heider J.;
RT   "Biochemical and genetic characterization of benzylsuccinate synthase from
RT   Thauera aromatica: a new glycyl radical enzyme catalysing the first step in
RT   anaerobic toluene metabolism.";
RL   Mol. Microbiol. 28:615-628(1998).
RN   [2]
RP   INDUCTION.
RC   STRAIN=DSM 6984 / CIP 107765 / K172;
RX   PubMed=9741082; DOI=10.1111/j.1574-6968.1998.tb13180.x;
RA   Leuthner B., Heider J.;
RT   "A two-component system involved in regulation of anaerobic toluene
RT   metabolism in Thauera aromatica.";
RL   FEMS Microbiol. Lett. 166:35-41(1998).
RN   [3]
RP   INDUCTION.
RC   STRAIN=DSM 6984 / CIP 107765 / K172;
RX   PubMed=11807562; DOI=10.1007/s00203-001-0375-1;
RA   Hermuth K., Leuthner B., Heider J.;
RT   "Operon structure and expression of the genes for benzylsuccinate synthase
RT   in Thauera aromatica strain K172.";
RL   Arch. Microbiol. 177:132-138(2002).
CC   -!- FUNCTION: Catalyzes the addition of fumarate to the methyl group of
CC       toluene, leading to the formation of benzylsuccinate.
CC       {ECO:0000269|PubMed:9632263}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=fumarate + toluene = 2-benzylsuccinate; Xref=Rhea:RHEA:10416,
CC         ChEBI:CHEBI:17578, ChEBI:CHEBI:29806, ChEBI:CHEBI:57621;
CC         EC=4.1.99.11; Evidence={ECO:0000269|PubMed:9632263};
CC   -!- ACTIVITY REGULATION: Activated by the benzylsuccinate synthase
CC       activating enzyme BssD. Rapidly inactivated by oxygen.
CC       {ECO:0000269|PubMed:9632263}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:9632263};
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC       {ECO:0000269|PubMed:9632263}.
CC   -!- SUBUNIT: Heterohexamer composed of 2 alpha subunits, 2 beta subunits
CC       and 2 gamma subunits. {ECO:0000269|PubMed:9632263}.
CC   -!- INDUCTION: Induced by toluene, probably via the TdiR/TdiS two-component
CC       regulatory system. {ECO:0000269|PubMed:11807562,
CC       ECO:0000269|PubMed:9632263, ECO:0000269|PubMed:9741082}.
CC   -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family. BSS
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AJ001848; CAA05052.1; -; Genomic_DNA.
DR   AlphaFoldDB; O87943; -.
DR   SMR; O87943; -.
DR   KEGG; ag:CAA05052; -.
DR   BioCyc; MetaCyc:MON-670; -.
DR   BRENDA; 4.1.99.11; 6271.
DR   UniPathway; UPA00273; -.
DR   GO; GO:0018805; F:benzylsuccinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001150; Gly_radical.
DR   InterPro; IPR004184; PFL_dom.
DR   Pfam; PF01228; Gly_radical; 1.
DR   Pfam; PF02901; PFL-like; 1.
DR   PROSITE; PS51149; GLY_RADICAL_2; 1.
DR   PROSITE; PS51554; PFL; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; Lyase;
KW   Organic radical.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9632263"
FT   CHAIN           2..861
FT                   /note="Benzylsuccinate synthase alpha subunit"
FT                   /id="PRO_0000418872"
FT   DOMAIN          40..712
FT                   /note="PFL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT   DOMAIN          731..850
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT   REGION          718..744
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         825
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   861 AA;  97736 MW;  C62E8DA75A288EE5 CRC64;
     MSDVQTLEYK GKVVQFAPEN PREAEIPADE LHEHLQNPST ERTRRLKARC RWKHAAAGEF
     CEKGVTAGIE RMRLLTESHW ATRGEPEPIR RAHGLKNILD KSTLVLQTDE FIVGYHAEDP
     NMFPLYPELS YMAVQDYLKS KYSPQPAKEA QEIVDYWKPF SLQARCEPYF DPVDLHRGYQ
     VSTIEGPVFA TGYNSVIPPY ETVLEDGLQA RIALAEEKIE HARAEMEKFP WHAPSGLEWI
     DKIDNWKAMV IACKAVIAWA RRHARLCKIV AEHFETDPKR KAELLEIADI CQRMPAEPAR
     GLKDAMQSKW FTFLICHAIE RYASGFAQKE DSLLWPYYKA SVIDKTFQPM EHKDAVELIE
     MERLKVSEHG AGKSRAYREI FPGSNDLFIL TLGGTNGDGS DACNDMTDAI LEATKRIRTT
     EPSIVFRYSK KNRAKTLRWV FECIRDGLGY PSIKHNELGV QQMLEMAKYS RNGNGATPEE
     AHYWVNVLCM APGLAGRRKA QKTRSEGGSA IFPAKLLEIT LNNGYDWSYA DMQMGPETGY
     AKDFATFDQL WEAFRKQYQY AIALAIRCKD VSRTMECRFL QMPFVSALDD GCMELGMDAN
     ALSEQPNGWH NPITSIVAGN SLVAIKKLIY DEKKYTMAQL MDALQANWEG YEEMRRDFKN
     APKWGNDDDD ADVLISRFYE EILGGEMMKN INYSGGPVKP TGQAVGLYME VGSRTGPTPD
     GRFGGEAADD GGISPYSGTD KKGPTAVLRS VSKVQKNQKA NLLNQRLSVP IMRSKHGFDI
     WHAYMDTWHD LNIDHVQFNV VSTEEMKAAQ REPEKHQDLI VRVSGFSARF VDIPTYGQNT
     IIARNEQNFN AQDLEFLNVE L