ID A5I0R1_CLOBH Unreviewed; 472 AA.
AC A5I0R1; A7G2H2;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE SubName: Full=Anaerobic glycerol-3-phosphate dehydrogenase subunit a {ECO:0000313|EMBL:CAL82622.1};
DE EC=1.1.99.5 {ECO:0000313|EMBL:CAL82622.1};
GN Name=glpA {ECO:0000313|EMBL:CAL82622.1};
GN OrderedLocusNames=CBO1068 {ECO:0000313|EMBL:CAL82622.1};
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:CAL82622.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL82622.1, 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; CAL82622.1; -; Genomic_DNA.
DR RefSeq; WP_011948739.1; NC_009698.1.
DR RefSeq; YP_001253599.1; NC_009495.1.
DR RefSeq; YP_001386987.1; NC_009698.1.
DR AlphaFoldDB; A5I0R1; -.
DR GeneID; 5185323; -.
DR KEGG; cbh:CLC_1120; -.
DR KEGG; cbo:CBO1068; -.
DR PATRIC; fig|413999.7.peg.1063; -.
DR HOGENOM; CLU_024775_3_1_9; -.
DR OMA; WGVSKAN; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR42720:SF1; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE PROTEIN-RELATED; 1.
DR PANTHER; PTHR42720; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF04324; Fer2_BFD; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:CAL82622.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT DOMAIN 3..353
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 398..452
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
SQ SEQUENCE 472 AA; 52441 MW; 578EAA5624DF454F CRC64;
MFDVTIIGSG VTGAAVAREL SKYNLKTCVV EKAIDVANGT SKANSGIVHA GEDPIPGTLK
AKMNVRGNEM FDKLQEEIDF PFKRNESFVL CFDEKDIEKL EELRQRGLKN GLPDTMEILN
REEALKLEPN LSEYVVAALR LPTGGIVSPY EFNIALAESA AMNGVEFKLE TEIIDIEKKE
DGYILKTNKG DIETKVVVNA AGVFGDKINN MVSEKKYHIT ARKGEYLLFD KTVGDMVQRT
IFQLPTKMGK GVLVTPTADG NLLLGPTSVD VEEKDDFGTT REGLDTVAEK AKLSIKEIPM
RQVITSFAGL RAHEENSDFI IEEAEDAKNF INAIGIESPG LTSAPAIGEY IREMIVEKLK
PEENKEFNPI RKDIPKFREM TNEERKEMIK ENSAYGKIVC RCEVVTEGEI RDAIRRPLGA
KTVDGIKRRT RAGMGRCQSG FCSNRIVEIL AEELGIKRNE VTKFGGNSKI LY
//