(data stored in SCRATCH zone)

SWISSPROT: Q8XE88_ECO57

ID   Q8XE88_ECO57            Unreviewed;       367 AA.
AC   Q8XE88; Q7AH13;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 117.
DE   RecName: Full=Riboflavin biosynthesis protein RibD {ECO:0000256|PIRNR:PIRNR006769};
GN   Name=ribD {ECO:0000313|EMBL:AAG54763.1};
GN   OrderedLocusNames=ECs0467 {ECO:0000313|EMBL:BAB33890.1}, Z0515
GN   {ECO:0000313|EMBL:AAG54763.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|Proteomes:UP000002519};
RN   [1] {ECO:0000313|EMBL:BAB33890.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558}, and Sakai
RC   {ECO:0000313|EMBL:BAB33890.1};
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., 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).
RN   [2] {ECO:0000313|EMBL:AAG54763.1, ECO:0000313|Proteomes:UP000002519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EDL933 {ECO:0000313|EMBL:AAG54763.1}, and O157:H7 / EDL933 /
RC   ATCC 700927 / EHEC {ECO:0000313|Proteomes:UP000002519};
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., 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).
CC   -!- FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone
CC       5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-
CC       pyrimidinedione 5'-phosphate. {ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006769,
CC         ECO:0000256|PIRSR:PIRSR006769-3};
CC       Note=Binds 1 zinc ion. {ECO:0000256|PIRNR:PIRNR006769,
CC       ECO:0000256|PIRSR:PIRSR006769-3};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC       6-(D-ribitylamino)uracil from GTP: step 2/4.
CC       {ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC       6-(D-ribitylamino)uracil from GTP: step 3/4.
CC       {ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the HTP
CC       reductase family. {ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and
CC       deoxycytidylate deaminase family. {ECO:0000256|PIRNR:PIRNR006769}.
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DR   EMBL; AE005174; AAG54763.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33890.1; -; Genomic_DNA.
DR   PIR; C90687; C90687.
DR   PIR; G85537; G85537.
DR   RefSeq; NP_308494.1; NC_002695.1.
DR   RefSeq; WP_001150441.1; NZ_MWVM01000009.1.
DR   STRING; 155864.Z0515; -.
DR   EnsemblBacteria; AAG54763; AAG54763; Z0515.
DR   EnsemblBacteria; BAB33890; BAB33890; BAB33890.
DR   GeneID; 914569; -.
DR   KEGG; ece:Z0515; -.
DR   KEGG; ecs:ECs0467; -.
DR   PATRIC; fig|386585.9.peg.567; -.
DR   eggNOG; ENOG4105D1W; Bacteria.
DR   eggNOG; COG0117; LUCA.
DR   eggNOG; COG1985; LUCA.
DR   HOGENOM; HOG000257442; -.
DR   KO; K11752; -.
DR   UniPathway; UPA00275; UER00401.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:InterPro.
DR   GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.430.10; -; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR024072; DHFR-like_dom.
DR   InterPro; IPR004794; Eubact_RibD.
DR   InterPro; IPR011549; RibD_C.
DR   InterPro; IPR002734; RibDG_C.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   Pfam; PF01872; RibD_C; 1.
DR   PIRSF; PIRSF006769; RibD; 1.
DR   SUPFAM; SSF53597; SSF53597; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR00326; eubact_ribD; 1.
DR   TIGRFAMs; TIGR00227; ribD_Cterm; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8XE88.
DR   SWISS-2DPAGE; Q8XE88.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558,
KW   ECO:0000313|Proteomes:UP000002519};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006769};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR006769,
KW   ECO:0000256|PIRSR:PIRSR006769-3};
KW   NADP {ECO:0000256|PIRNR:PIRNR006769, ECO:0000256|PIRSR:PIRSR006769-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006769};
KW   Riboflavin biosynthesis {ECO:0000256|PIRNR:PIRNR006769};
KW   Zinc {ECO:0000256|PIRNR:PIRNR006769, ECO:0000256|PIRSR:PIRSR006769-3}.
FT   DOMAIN        1    123       CMP/dCMP-type deaminase.
FT                                {ECO:0000259|PROSITE:PS51747}.
FT   NP_BIND     301    307       NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   ACT_SITE     52     52       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006769-1}.
FT   METAL        50     50       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR006769-3}.
FT   METAL        75     75       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR006769-3}.
FT   METAL        84     84       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR006769-3}.
FT   BINDING     154    154       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR006769-
FT                                2}.
FT   BINDING     168    168       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006769-2}.
FT   BINDING     170    170       NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     184    184       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006769-2}.
FT   BINDING     196    196       NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     200    200       NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     204    204       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     207    207       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006769-2}.
FT   BINDING     234    234       NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     299    299       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006769-2}.
SQ   SEQUENCE   367 AA;  40364 MW;  6B23906980774954 CRC64;
     MQDEYYMARA LKLAQRGRFT THPNPNVGCV IVKDGEIVGE GYHQRAGEPH AEVHALRMAG
     EKAKGATAYV TLEPCSHHGR TPPCCDALIA AGVARVVAAM QDPNPQVAGR GLYRLQQAGI
     DVSHGLMMSE AEQLNKGFLK RMRTGFPYIQ LKLGASLDGR TAMASGESQW ITSPQARRDV
     QRLRAQSHAI LTSSATVLAD DPALTVRWSE LDVQTQALYP QHHLRQPVRI VIDSQNRVTP
     EHHIVQQPGE TWFARTQEDS REWPETVRTL LIPEHKGHLD LVVLMMQLGK QQINSIWVEA
     GPTLAGALLQ AGLVDELIVY IAPKLLGSDA RGLCTLPGLE KLADAPQFKF KEIRHVGPDV
     CLHLVGA
//

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