ID A0A0C1U6F2_9CLOT Unreviewed; 282 AA.
AC A0A0C1U6F2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=FAD binding domain in molybdopterin dehydrogenase family protein {ECO:0000313|EMBL:KIE48304.1};
GN ORFNames=U732_4159 {ECO:0000313|EMBL:KIE48304.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE48304.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE48304.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE48304.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIE48304.1}.
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DR EMBL; AYSO01000010; KIE48304.1; -; Genomic_DNA.
DR RefSeq; WP_039629977.1; NZ_AYSO01000010.1.
DR AlphaFoldDB; A0A0C1U6F2; -.
DR STRING; 29341.RSJ17_10840; -.
DR OrthoDB; 9789842at2; -.
DR Proteomes; UP000031366; Unassembled WGS sequence.
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; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR005107; CO_DH_flav_C.
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; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR SMART; SM01092; CO_deh_flav_C; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031366}.
FT DOMAIN 1..172
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 282 AA; 32040 MW; 4D8EE3762C140ED4 CRC64;
MVNCYRPNTL KEALDILNKE ECIILAGGTD LMVRRKQWSG LIPNFEEQVL FINHLPELKE
VRVEDNDLII GSCCKLGELE MNSIIPQYLK DVIKEMASIG TRNIATIGGN ICNGSPAGDI
LSPLYALGSK VVIANSNGER KIPIKELIVG SGKTILKNNE ILKEIIIENY NFTDYYYHKV
GTRKSIALAK VSFIGFYKIE DDIVKDIRIA LGAVSPTIVN DRDLECSFIS LSRLETKEKL
EEIIERYKEI IMPIDDARST VRYRKKVSIN LINYFFNERI FK
//
