(data stored in ACNUC7421 zone)

SWISSPROT: YAGS_ECO57

ID   YAGS_ECO57              Reviewed;         318 AA.
AC   Q8X6J0;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   07-JUN-2017, entry version 90.
DE   RecName: Full=Putative xanthine dehydrogenase YagS FAD-binding subunit;
DE            EC=1.17.1.4;
GN   Name=yagS; OrderedLocusNames=Z0351, ECs0315;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- CATALYTIC ACTIVITY: Xanthine + NAD(+) + H(2)O = urate + NADH.
CC   -!- CATALYTIC ACTIVITY: Hypoxanthine + NAD(+) + H(2)O = xanthine +
CC       NADH.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Heterotrimer of YagR, YagS and YagT. {ECO:0000305}.
DR   EMBL; AE005174; AAG54610.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33738.1; -; Genomic_DNA.
DR   PIR; C90668; C90668.
DR   PIR; F85518; F85518.
DR   RefSeq; NP_308342.1; NC_002695.1.
DR   RefSeq; WP_000643341.1; NZ_LPWC02000002.1.
DR   ProteinModelPortal; Q8X6J0; -.
DR   SMR; Q8X6J0; -.
DR   STRING; 155864.Z0351; -.
DR   PRIDE; Q8X6J0; -.
DR   EnsemblBacteria; AAG54610; AAG54610; Z0351.
DR   EnsemblBacteria; BAB33738; BAB33738; BAB33738.
DR   GeneID; 914414; -.
DR   KEGG; ece:Z0351; -.
DR   KEGG; ecs:ECs0315; -.
DR   PATRIC; fig|386585.9.peg.409; -.
DR   eggNOG; ENOG4105DIP; Bacteria.
DR   eggNOG; COG1319; LUCA.
DR   HOGENOM; HOG000244727; -.
DR   KO; K11178; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
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; SSF55447; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
DR   PRODOM; Q8X6J0.
DR   SWISS-2DPAGE; Q8X6J0.
KW   Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Purine metabolism; Purine salvage.
FT   CHAIN         1    318       Putative xanthine dehydrogenase YagS FAD-
FT                                binding subunit.
FT                                /FTId=PRO_0000166095.
FT   DOMAIN        1    223       FAD-binding PCMH-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00718}.
FT   NP_BIND      26     33       FAD. {ECO:0000255}.
FT   NP_BIND     107    111       FAD. {ECO:0000255}.
FT   BINDING     212    212       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255}.
FT   BINDING     227    227       FAD. {ECO:0000255}.
SQ   SEQUENCE   318 AA;  33886 MW;  32C48CE9D0F16F90 CRC64;
     MKAFTYERVN TPAEAALSAQ RVPGAKFIAG GTNLLDLMKL EIETPTHLID VNGLGLDKIE
     VTDAGGLRIG ALVRNTDLVA HERVRRDYAV LSRALLAGAS GQLRNQATTA GNLLQRTRCP
     YFYDTNQPCN KRLPGSGCAA LEGFSRQHAV VGVSEACIAT HPSDMAVAMR LLDAVVETIT
     PEGKTRSITL ADFYHPPGKT PHIETALLPG ELIVAVTLPP PLGGKHIYRK VRDRASYTFA
     LVSVAAIIQP DGSGRVALGG VAHKPWRIEA ADAQLSQGAQ AVYDALFASA HPTAENTFKL
     LLAKRTLASV LAEARAQA
//

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