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Database: UniProt
Entry: A5I0R2_CLOBH
LinkDB: A5I0R2_CLOBH
Original site: A5I0R2_CLOBH 
ID   A5I0R2_CLOBH            Unreviewed;       418 AA.
AC   A5I0R2; A7G2H3;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:CAL82623.1};
GN   OrderedLocusNames=CBO1069 {ECO:0000313|EMBL:CAL82623.1};
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL82623.1, ECO:0000313|Proteomes:UP000001986};
RN   [1] {ECO:0000313|EMBL:CAL82623.1, ECO:0000313|Proteomes:UP000001986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC   {ECO:0000313|Proteomes:UP000001986};
RX   PubMed=17519437; DOI=10.1101/gr.6282807;
RA   Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA   Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA   Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA   Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA   Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA   Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA   White B., Whithead S., Parkhill J.;
RT   "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT   Hall A and comparative analysis of the clostridial genomes.";
RL   Genome Res. 17:1082-1092(2007).
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DR   EMBL; AM412317; CAL82623.1; -; Genomic_DNA.
DR   RefSeq; WP_011948740.1; NC_009698.1.
DR   RefSeq; YP_001253600.1; NC_009495.1.
DR   RefSeq; YP_001386988.1; NC_009698.1.
DR   AlphaFoldDB; A5I0R2; -.
DR   GeneID; 5185324; -.
DR   KEGG; cbh:CLC_1121; -.
DR   KEGG; cbo:CBO1069; -.
DR   PATRIC; fig|413999.7.peg.1064; -.
DR   HOGENOM; CLU_030705_0_0_9; -.
DR   Proteomes; UP000001986; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   PANTHER; PTHR42949; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR   PANTHER; PTHR42949:SF3; OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT   DOMAIN          4..299
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   418 AA;  46052 MW;  0626988065DF1AD2 CRC64;
     MQQYDVVIIG GGPAGLAAAI KAKEEGVDSI LILERDKRLG GILNQCIHNG FGLHTFKEEL
     TGPEYAQRFV DKVEEMKIPY KLNTMVIDMN KDKIITAVNE EDGLIEVQAK SIVLAMGCRE
     RSRGAINIPG TRCSGIYSAG TAQKFVNIEG EMPGKEVVIL GSGDIGLIMA RRMTLEGSKV
     KAVVELMPYS GGLKRNIVQC LDDFGIPLKL AHTITKIEGK ERLEAVTIAK VDEKLKPIKG
     TEEYIKCDTL LLSVGLLPEN DLSRKADVKL GVTGGPEVDE TMQTNIDGVF ACGNVLHVHD
     LVDFVTEESY NAGKNAADYV KGKKVEGEKI ELVAENGVGY TVPKSIHKSN IENTVDVRFR
     VRNVFKDSFI SVYFDNERVI HRKKKVIAPG EMETVKLTKD MFEKHLDCKK ITVKVEGE
//
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