(data stored in ACNUC10821 zone)

SWISSPROT: C8U298_ECO10

ID   C8U298_ECO10            Unreviewed;       367 AA.
AC   C8U298;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Riboflavin biosynthesis protein RibD {ECO:0000256|PIRNR:PIRNR006769};
DE   Includes:
DE     RecName: Full=Diaminohydroxyphosphoribosylaminopyrimidine deaminase {ECO:0000256|PIRNR:PIRNR006769};
DE              Short=DRAP deaminase {ECO:0000256|PIRNR:PIRNR006769};
DE              EC=3.5.4.26 {ECO:0000256|PIRNR:PIRNR006769};
DE     AltName: Full=Riboflavin-specific deaminase {ECO:0000256|PIRNR:PIRNR006769};
DE   Includes:
DE     RecName: Full=5-amino-6-(5-phosphoribosylamino)uracil reductase {ECO:0000256|PIRNR:PIRNR006769};
DE              EC=1.1.1.193 {ECO:0000256|PIRNR:PIRNR006769};
DE     AltName: Full=HTP reductase {ECO:0000256|PIRNR:PIRNR006769};
GN   Name=ribD {ECO:0000313|EMBL:BAI29256.1};
GN   OrderedLocusNames=ECO103_0388 {ECO:0000313|EMBL:BAI29256.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29256.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29256.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-
CC         pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-
CC         ribosylamino)uracil + NH4(+); Xref=Rhea:RHEA:21868,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58453, ChEBI:CHEBI:58614; EC=3.5.4.26;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006769};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5-
CC         amino-6-(5-phospho-D-ribosylamino)uracil + H(+) + NADPH;
CC         Xref=Rhea:RHEA:17845, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:58421, ChEBI:CHEBI:58453;
CC         EC=1.1.1.193; Evidence={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; AP010958; BAI29256.1; -; Genomic_DNA.
DR   RefSeq; WP_001150451.1; NC_013353.1.
DR   EnsemblBacteria; BAI29256; BAI29256; ECO103_0388.
DR   KEGG; eoh:ECO103_0388; -.
DR   HOGENOM; HOG000257442; -.
DR   KO; K11752; -.
DR   OMA; DEMYMAR; -.
DR   BioCyc; ECOL585395:ECO103_RS02035-MONOMER; -.
DR   UniPathway; UPA00275; UER00401.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:UniProtKB-EC.
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_sf.
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; C8U298.
DR   SWISS-2DPAGE; C8U298.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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;  40427 MW;  9F679F507DE0CF9B CRC64;
     MQDEYYMARA LKLAQRGRFT THPNPNVGCV IVKDGEIVGE GYHQRAGEPH AEVHALRMAG
     EKAKGATAYV TLEPCSHHGR TPPCCDALIA AGVARVVAAM QDPNPQVAGR GLYRLQQAGI
     DVSHGLMMSE AEQLNKGFLK RMRTGFPYIQ LKLGASLDGR TAMASGESQW ITSTQARRDV
     QRLRAQSHAI LTSSATVLAD DPALTVRWSE LDEQTQVLYP QQNLRQPVRI VIDSQNRVTP
     EHRIVQQPGE TWFARTQEDS REWPETVRTL LIPEHKGHLD LVVLMMQLGK QQINSIWVEA
     GPTLAGALLQ VGLVDELIVY IAPKLLGSDA RGLCSLPGLE KLADAPQFKF KEIRHVGPDV
     CLHLVGA
//

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