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Database: UniProt
Entry: O87941
LinkDB: O87941
Original site: O87941 
ID   BSSD_THAAR              Reviewed;         331 AA.
AC   O87941;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 2.
DT   05-DEC-2018, entry version 92.
DE   RecName: Full=Benzylsuccinate synthase activating enzyme;
DE            EC=1.97.1.-;
GN   Name=bssD;
OS   Thauera aromatica.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Zoogloeaceae; Thauera.
OX   NCBI_TaxID=59405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND INDUCTION.
RC   STRAIN=DSM 6984 / 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
RT   from Thauera aromatica: a new glycyl radical enzyme catalysing the
RT   first step in anaerobic toluene metabolism.";
RL   Mol. Microbiol. 28:615-628(1998).
RN   [2]
RP   INDUCTION.
RC   STRAIN=DSM 6984 / 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 / 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
RT   synthase in Thauera aromatica strain K172.";
RL   Arch. Microbiol. 177:132-138(2002).
CC   -!- FUNCTION: Activation of benzylsuccinate synthase under anaerobic
CC       conditions by generation of an organic free radical, using S-
CC       adenosylmethionine and reduced flavodoxin as cosubstrates to
CC       produce 5'-deoxy-adenosine. {ECO:0000305|PubMed:9632263}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000305};
CC       Note=Binds 3 [4Fe-4S] clusters. One cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000305};
CC   -!- PATHWAY: Xenobiotic degradation; toluene degradation [regulation].
CC       {ECO:0000269|PubMed:9632263}.
CC   -!- INDUCTION: Induced by toluene, probably via the TdiR/TdiS two-
CC       component regulatory system. {ECO:0000269|PubMed:11807562,
CC       ECO:0000269|PubMed:9632263, ECO:0000269|PubMed:9741082}.
CC   -!- SIMILARITY: Belongs to the organic radical-activating enzymes
CC       family. {ECO:0000305}.
DR   EMBL; AJ001848; CAA05050.2; -; Genomic_DNA.
DR   ProteinModelPortal; O87941; -.
DR   PRIDE; O87941; -.
DR   UniPathway; UPA00273; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0018805; F:benzylsuccinate synthase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR034462; Benzylsuc_synthase_activase.
DR   InterPro; IPR023880; Benzylsucc_Synthase_activating.
DR   InterPro; IPR034457; Organic_radical-activating.
DR   InterPro; IPR012839; Organic_radical_activase.
DR   InterPro; IPR001989; Radical_activat_CS.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30352; PTHR30352; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF000371; PFL_act_enz; 1.
DR   SFLD; SFLDF00297; benzylsuccinate_synthase_activ; 1.
DR   TIGRFAMs; TIGR04003; rSAM_BssD; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS01087; RADICAL_ACTIVATING; 1.
PE   2: Evidence at transcript level;
KW   4Fe-4S; Aromatic hydrocarbons catabolism; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Repeat; S-adenosyl-L-methionine.
FT   CHAIN         1    331       Benzylsuccinate synthase activating
FT                                enzyme.
FT                                /FTId=PRO_0000418876.
FT   DOMAIN       46     75       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       80    109       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   REGION       35     37       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:P0A9N4}.
FT   REGION      189    191       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250|UniProtKB:P0A9N4}.
FT   METAL        29     29       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000250|UniProtKB:P0A9N4}.
FT   METAL        33     33       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000250|UniProtKB:P0A9N4}.
FT   METAL        36     36       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000250|UniProtKB:P0A9N4}.
FT   METAL        55     55       Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
FT   METAL        58     58       Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
FT   METAL        61     61       Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
FT   METAL        65     65       Iron-sulfur 3 (4Fe-4S). {ECO:0000255}.
FT   METAL        89     89       Iron-sulfur 3 (4Fe-4S). {ECO:0000255}.
FT   METAL        92     92       Iron-sulfur 3 (4Fe-4S). {ECO:0000255}.
FT   METAL        95     95       Iron-sulfur 3 (4Fe-4S). {ECO:0000255}.
FT   METAL        99     99       Iron-sulfur 2 (4Fe-4S). {ECO:0000255}.
FT   BINDING     139    139       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000250|UniProtKB:P0A9N4}.
FT   BINDING     263    263       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P0A9N4}.
SQ   SEQUENCE   331 AA;  36052 MW;  4550F347D71992DB CRC64;
     MKIPLITEIQ RFSLQDGPGI RTTIFLKGCP LRCPWCHNPE TQDARQEFYF YPDRCVGCGR
     CVAVCPAETS RLVRNSDGRT IVQIDRTNCQ RCMRCVAACL TEARAIVGQH MSVDEILREA
     LSDSAFYRNS GGGVTISGGD PLYFPDFTRQ LASELHARGV HVAIETSCFP KQGKVVESMI
     GIVDLFIVDL KTLDAHKHLD VIGWPLAPIL ANLETLFAAG AKVRIHIPVI PGFNDSHADI
     DAYAEYLGKH AAAISGIDLL NFHCYGEGKY TFLGRAGSYQ YSGVDETPAE KIVPLAQALK
     ARGLAVTIGG IVGIANGKNE LTGDIALEVH H
//
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