BSSD_THAAR
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 03-AUG-2022, entry version 101.
DE RecName: Full=Benzylsuccinate synthase activating enzyme;
DE EC=1.97.1.- {ECO:0000305|PubMed:9632263};
GN Name=bssD;
OS Thauera aromatica.
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=59405;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, 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: 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 produce
CC 5'-deoxy-adenosine. {ECO:0000305|PubMed:9632263}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-
CC methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+)
CC + L-methionine + semiquinone [flavodoxin]; Xref=Rhea:RHEA:61976,
CC Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:14480, Rhea:RHEA-COMP:15993,
CC Rhea:RHEA-COMP:15994, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:29947, ChEBI:CHEBI:32722, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:140311;
CC Evidence={ECO:0000305|PubMed:9632263};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; 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. {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-component
CC regulatory system. {ECO:0000269|PubMed:11807562,
CC ECO:0000269|PubMed:9632263, ECO:0000269|PubMed:9741082}.
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000305}.
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DR EMBL; AJ001848; CAA05050.2; -; Genomic_DNA.
DR AlphaFoldDB; O87941; -.
DR SMR; O87941; -.
DR UniPathway; UPA00273; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Aromatic hydrocarbons catabolism; Iron; Iron-sulfur; Metal-binding;
KW Oxidoreductase; Repeat; S-adenosyl-L-methionine.
FT CHAIN 1..331
FT /note="Benzylsuccinate synthase activating enzyme"
FT /id="PRO_0000418876"
FT DOMAIN 15..315
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 46..75
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 80..109
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 33
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 35..37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 36
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 65
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 189..191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="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
