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Database: UniProt
Entry: K0NM05_DESTT
LinkDB: K0NM05_DESTT
Original site: K0NM05_DESTT 
ID   K0NM05_DESTT            Unreviewed;       809 AA.
AC   K0NM05;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=BssA3: benzylsuccinate synthase, alpha subunit {ECO:0000313|EMBL:CCK79722.1};
DE            EC=4.1.99.11 {ECO:0000313|EMBL:CCK79722.1};
GN   Name=bssA3 {ECO:0000313|EMBL:CCK79722.1};
GN   OrderedLocusNames=TOL2_C15590 {ECO:0000313|EMBL:CCK79722.1};
OS   Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfobacula.
OX   NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK79722.1, ECO:0000313|Proteomes:UP000007347};
RN   [1] {ECO:0000313|EMBL:CCK79722.1, ECO:0000313|Proteomes:UP000007347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX   PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA   Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA   Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT   "Complete genome, catabolic sub-proteomes and key-metabolites of
RT   Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT   sulfate-reducing bacterium.";
RL   Environ. Microbiol. 15:1334-55(2013).
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DR   EMBL; FO203503; CCK79722.1; -; Genomic_DNA.
DR   RefSeq; WP_014957066.1; NC_018645.1.
DR   AlphaFoldDB; K0NM05; -.
DR   STRING; 651182.TOL2_C15590; -.
DR   KEGG; dto:TOL2_C15590; -.
DR   PATRIC; fig|651182.5.peg.1871; -.
DR   HOGENOM; CLU_009096_0_1_7; -.
DR   OrthoDB; 9803969at2; -.
DR   Proteomes; UP000007347; Chromosome.
DR   GO; GO:0018805; F:benzylsuccinate synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.20.70.20; -; 1.
DR   InterPro; IPR001150; Gly_radical.
DR   InterPro; IPR004184; PFL_dom.
DR   PANTHER; PTHR43641:SF2; DEHYDRATASE YBIW-RELATED; 1.
DR   PANTHER; PTHR43641; FORMATE ACETYLTRANSFERASE 3-RELATED; 1.
DR   Pfam; PF01228; Gly_radical; 1.
DR   Pfam; PF02901; PFL-like; 1.
DR   PIRSF; PIRSF000379; For_Ac_trans_1; 1.
DR   SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR   PROSITE; PS51149; GLY_RADICAL_2; 1.
DR   PROSITE; PS51554; PFL; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CCK79722.1};
KW   Organic radical {ECO:0000256|ARBA:ARBA00022818,
KW   ECO:0000256|PIRSR:PIRSR000379-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007347}.
FT   DOMAIN          5..679
FT                   /note="PFL"
FT                   /evidence="ECO:0000259|PROSITE:PS51554"
FT   DOMAIN          687..807
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000259|PROSITE:PS51149"
FT   MOD_RES         782
FT                   /note="Glycine radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000379-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00493"
SQ   SEQUENCE   809 AA;  91244 MW;  D2AD5934749E0B38 CRC64;
     MPTTERTTRL KDRCRFKHVA GGEYVDAGVK AGVERARLIT QSHKKNVGEP NCIMRARGLE
     NILKNITIHI QDDELIVGAN TEHPDYFPMY PELSYFATVD MVESPYCEYK EEMREIAEYW
     KPYTIQTKGE KYFTPEEINI MYSATTVQPP LFVTAFSSLV PNYESVLEDG LIKRIEEVEK
     KIADANDKMR QSPWNAQDNL HFMDKLDQWE AMVIAMKAVV GWAQRYARLA RIMAENFLTD
     AKRKQELLEI SDICRHVPAN PARGLKDAMQ SKWFTFLLCH SMERYSSGYG HKADKLLWPY
     FQKSVINKTD QPMTREEAVE LFECERLKVS EHGSTKGRQL REFFAGSNDL FIFTLGGINP
     DGSDASNDCT NAILEAAESI VTTEPSIGFR WNKTGNVETK KRVFNCIKKG FGFPSIKNDE
     LNTEQLIKYF NVPENIARDW ALVLCMSPGI TGRRGTQKTR NEGGGDVYPA KAMEIALTNG
     FDEFFTNIQL GPQTGDAANF TSFDEVWNAY KLQLRYAIEL TLRSKDVGRI IESTHLCCPF
     ISSIDDGCVE KGMDANALAE VANPWHNICS GSVVVIDSLA AIKKLVFEDK KYTMAELMDA
     LKNNWEGKEE MRLDFWNAPK FGNDDDYADA MATKYYNLIA DEWKRNTTYS GTYPLPLAQS
     VAGYIVNGPK TAATANGRHA GEALDDGGCS PYMGCDTNGP TAVLKSVSRI DASRHKGVLL
     NQRLSNILMH SDAGFDLWHA YMKTWHSLGI DHVQFNVIST EDMKAAQIEP EKYANTLVRI
     AGYSAKFIDL ARYSQDTIIA RTEQDMAAG
//
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