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Database: UniProt
Entry: F4VI75_ECOLX
LinkDB: F4VI75_ECOLX
Original site: F4VI75_ECOLX 
ID   F4VI75_ECOLX            Unreviewed;       292 AA.
AC   F4VI75;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Xanthine dehydrogenase FAD-binding subunit {ECO:0000313|EMBL:EGI45003.1};
GN   ORFNames=ECPG_04149 {ECO:0000313|EMBL:EGI45003.1};
OS   Escherichia coli H591.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=656408 {ECO:0000313|EMBL:EGI45003.1, ECO:0000313|Proteomes:UP000004681};
RN   [1] {ECO:0000313|EMBL:EGI45003.1, ECO:0000313|Proteomes:UP000004681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H591 {ECO:0000313|EMBL:EGI45003.1,
RC   ECO:0000313|Proteomes:UP000004681};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Escherichia coli H591.";
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GL884456; EGI45003.1; -; Genomic_DNA.
DR   RefSeq; WP_000459177.1; NZ_GL884456.1.
DR   AlphaFoldDB; F4VI75; -.
DR   GeneID; 66673260; -.
DR   HOGENOM; CLU_058050_0_1_6; -.
DR   Proteomes; UP000004681; 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:SF9; XANTHINE DEHYDROGENASE FAD-BINDING SUBUNIT XDHB-RELATED; 1.
DR   PANTHER; PTHR42659; 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   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827}.
FT   DOMAIN          1..176
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   292 AA;  31547 MW;  2D7A3CA964AAF640 CRC64;
     MFDFASYHRA ATLADAINLL ADNPQAKLLA GGTDVLIQLH HHNDRYRHIV DIHNLAELRG
     ITLAEDGSLR IGSATTFTQL IEDPITQRHL PALCAAATSI AGPQIRNVAT YGGNICNGAT
     SADSATPTLI YDAKLEIHSP HGVRFVPING FHTGPGKVSL EHDEILVAFH FPPQPKEHAG
     SAHFKYAMRD AMDISTIGCA AHCRLDNGNF SELRLAFGVA APTPIRCQHA EHTAQNAPLN
     LQTLEAISES VLQDVAPRSS WRASKEFRLH LIQTMTKKVI SEAVAAAGGK LQ
//
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