ID B1IL05_CLOBK Unreviewed; 276 AA.
AC B1IL05;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Xanthine dehydrogenase family protein, FAD-binding subunit {ECO:0000313|EMBL:ACA46017.1};
GN OrderedLocusNames=CLD_1719 {ECO:0000313|EMBL:ACA46017.1};
OS Clostridium botulinum (strain Okra / Type B1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498213 {ECO:0000313|EMBL:ACA46017.1, ECO:0000313|Proteomes:UP000008541};
RN [1] {ECO:0000313|EMBL:ACA46017.1, ECO:0000313|Proteomes:UP000008541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okra / Type B1 {ECO:0000313|Proteomes:UP000008541};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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DR EMBL; CP000939; ACA46017.1; -; Genomic_DNA.
DR RefSeq; WP_003405495.1; NC_010516.1.
DR AlphaFoldDB; B1IL05; -.
DR KEGG; cbb:CLD_1719; -.
DR HOGENOM; CLU_058050_5_0_9; -.
DR Proteomes; UP000008541; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR PANTHER; PTHR42659; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR PANTHER; PTHR42659:SF2; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 1..174
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 276 AA; 30705 MW; 1849BAFE6B6FFB32 CRC64;
MIPFDFEYYK PETIEEAVQL YAKLNARGKK PLYFGGGTEI ISMARAHNVY TEAVIDVKGV
SECNVQELRN NKLIIGSAVT LTQIAEANLF PLLGLTVQRI ADHTIQDKIT LGGNIAGTII
YREAVLPLLI SNAEILIAGS SGQKQVLLKD IFDKRIRLNY GEFIVNVSVD SHFLSLPSLH
VKRTKNDKID YPLITLAALK DNNRINISFS GVCDYPFRFS LIEDYLNDAS LANNIRINNS
INSIPDVILN DLAGSAGFRK FMLQKMLAEV LEKLEG
//
