ID   YGCU_ECOLI              Reviewed;         484 AA.
AC   Q46911; Q2MA57; Q46910; Q46912; Q6BF63;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 4.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Uncharacterized FAD-linked oxidoreductase YgcU;
DE            EC=1.-.-.-;
GN   Name=ygcU; Synonyms=ygcT, ygcV; OrderedLocusNames=b4463, JW5442;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=16397293; DOI=10.1093/nar/gkj405;
RA   Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA   Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA   Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA   Thomson N.R., Wishart D., Wanner B.L.;
RT   "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT   -- 2005.";
RL   Nucleic Acids Res. 34:1-9(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69282.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA69283.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA69284.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U29579; AAA69284.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U29579; AAA69283.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U29579; AAA69282.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00096; AAT48151.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76849.1; -; Genomic_DNA.
DR   RefSeq; WP_000059307.1; NZ_LN832404.1.
DR   RefSeq; YP_026183.1; NC_000913.3.
DR   AlphaFoldDB; Q46911; -.
DR   SMR; Q46911; -.
DR   BioGRID; 4260744; 32.
DR   DIP; DIP-12136N; -.
DR   STRING; 511145.b4463; -.
DR   PaxDb; Q46911; -.
DR   PRIDE; Q46911; -.
DR   EnsemblBacteria; AAT48151; AAT48151; b4463.
DR   EnsemblBacteria; BAE76849; BAE76849; BAE76849.
DR   GeneID; 2847709; -.
DR   KEGG; ecj:JW5442; -.
DR   KEGG; eco:b4463; -.
DR   PATRIC; fig|1411691.4.peg.3965; -.
DR   EchoBASE; EB2929; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_2_3_6; -.
DR   InParanoid; Q46911; -.
DR   OMA; PRCHDEV; -.
DR   PhylomeDB; Q46911; -.
DR   BioCyc; EcoCyc:G7439-MON; -.
DR   PRO; PR:Q46911; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
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; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..484
FT                   /note="Uncharacterized FAD-linked oxidoreductase YgcU"
FT                   /id="PRO_0000128183"
FT   DOMAIN          47..226
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   484 AA;  53737 MW;  6DC18635146103D1 CRC64;
     MSLSRAAIVD QLKEIVGADR VITDETVLKK NSIDRFRKFP DIHGIYTLPI PAAVVKLGST
     EQVSRVLNFM NAHKINGVPR TGASATEGGL ETVVENSVVL DGSAMNQIIN IDIENMQATA
     QCGVPLEVLE NALREKGYTT GHSPQSKPLA QMGGLVATRS IGQFSTLYGA IEDMVVGLEA
     VLADGTVTRI KNVPRRAAGP DIRHIIIGNE GALCYITEVT VKIFKFTPEN NLFYGYILED
     MKTGFNILRE IMVEGYRPSI ARLYDAEDGT QHFTHFADGK CVLIFMAEGN PRIAKVTGEG
     IAEIVARYPQ CQRVDSKLIE TWFNNLNWGP DKVAAERVQI LKTGNMGFTT EVSGCWSCIH
     EIYESVINRI RTEFPHADDI TMLGGHSSHS YQNGTNMYFV YDYNVVDCKP EEEIDKYHNP
     LNKIICEETI RLGGSMVHHH GIGKHRVHWS KLEHGSAWAL LEGLKKQFDP NGIMNTGTIY
     PIEK