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Database: UniProt
Entry: C3SW15_ECOLX
LinkDB: C3SW15_ECOLX
Original site: C3SW15_ECOLX 
ID   C3SW15_ECOLX            Unreviewed;       259 AA.
AC   C3SW15;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=ECs3753 {ECO:0000313|EMBL:ACI78654.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:ACI78654.1};
RN   [1] {ECO:0000313|EMBL:ACI78654.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TB182A {ECO:0000313|EMBL:ACI78654.1};
RX   PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA   Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA   Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA   Sawyer S.A., Whittam T.S., Tarr P.I.;
RT   "A precise reconstruction of the emergence and constrained radiations of
RT   Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
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DR   EMBL; EU896098; ACI78654.1; -; Genomic_DNA.
DR   RefSeq; WP_000572431.1; NZ_SAGF01000001.1.
DR   AlphaFoldDB; C3SW15; -.
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   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; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR017698; Molybdo-cont_Rdtase_FAD-bd_su.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   NCBIfam; TIGR03312; Se_sel_red_FAD; 1.
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   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;
FT   DOMAIN          1..159
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   259 AA;  28631 MW;  3615EA104F54EAED CRC64;
     MIEQFFRPDS VEQALELKHR YQDEAVWFAG GSKLNATPTR TDKKIAISLQ DLELDWVDWD
     NGALRIGAMS RLQPLRDARF IPAALREALG FVYSRHVRNQ STIGGEIAAR QEESVLLPVL
     LALDAELVFG NGETLSIEDY LACPCDRLLT EIIIKDPYRT CATRKISRSQ AGLTVVTAAV
     AMTDHDGMRI ALDGVASKAL RLHDVEKQNL EGNALEQAVA NAIFPQEDLR GSVAYKRYIT
     GVLVADLYAD CQQAGEEAV
//
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