ID   A5I413_CLOBH            Unreviewed;       482 AA.
AC   A5I413; A7G5E8;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   SubName: Full=Anaerobic glycerol-3-phosphate dehydrogenase protein {ECO:0000313|EMBL:CAL83783.1};
GN   OrderedLocusNames=CBO2244 {ECO:0000313|EMBL:CAL83783.1};
OS   Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium; Clostridium botulinum group.
OX   NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL83783.1, ECO:0000313|Proteomes:UP000001986};
RN   [1] {ECO:0000313|EMBL:CAL83783.1, 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; CAL83783.1; -; Genomic_DNA.
DR   RefSeq; WP_011986715.1; NC_009698.1.
DR   AlphaFoldDB; A5I413; -.
DR   GeneID; 5187509; -.
DR   KEGG; cbh:CLC_2167; -.
DR   KEGG; cbo:CBO2244; -.
DR   PATRIC; fig|413999.7.peg.2213; -.
DR   HOGENOM; CLU_024775_3_1_9; -.
DR   Proteomes; UP000001986; Chromosome.
DR   CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR052745; G3P_Oxidase/Oxidoreductase.
DR   PANTHER; PTHR42720:SF1; GLYCEROL 3-PHOSPHATE OXIDASE; 1.
DR   PANTHER; PTHR42720; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT   DOMAIN          3..349
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          394..447
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   482 AA;  53113 MW;  52488A6FBB58C043 CRC64;
     MYDVSIIGAG VVGSAIAREL SKYNLKVCLI EKEEDVGTGA SKANSGIVHG GYVAKYGTLK
     GELCIRGNSM YSQLEKELNF GYRNPGALVI GFDEDDENRI KKLYENGVKV GCDDLEIIYG
     DKIKELEPHI NKDVKVALYA KSVGVASPYE MTIALAENAI ENGVDLKLET KVLTIDKEHE
     TFIINTNKGE IKSKYIVNAA GLYSDKIANM LEMDDFKILP RRGQYVLSTK DQGYLVNKVI
     FQVPTEKGKG ILVTTTYHGN FMIGPDAQEV VDKEDIGTDI ESIEYIIKTA RKSIPDFDVR
     KSLTTFAGIR AISSTGDFVI EETKVKGFIN AAGIDSPGIT SSPAIAEKIV GILKEAGLQL
     IKNEKFNPYR KPIIIKKDKS FDGKIDDEDP TKNIICRCEK VTESEIIDAM KRGIPVKSTD
     AIKRRTRAGM GFCQGNFCRP RVKAIIAREM GIPVEKVTVR GKEGGEPPKR VNINVIRKIQ
     GV
//