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
//