(data stored in SCRATCH zone)

SWISSPROT: Q3Z4Z5_SHISS

ID   Q3Z4Z5_SHISS            Unreviewed;       367 AA.
AC   Q3Z4Z5;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 87.
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:AAZ87167.1};
GN   OrderedLocusNames=SSON_0391 {ECO:0000313|EMBL:AAZ87167.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87167.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87167.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87167.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87167.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87167; AAZ87167; SSON_0391.
DR   KEGG; ssn:SSON_0391; -.
DR   HOGENOM; HOG000257442; -.
DR   KO; K11752; -.
DR   OMA; DEMYMAR; -.
DR   BioCyc; SSON300269:G1GL2-453-MONOMER; -.
DR   UniPathway; UPA00275; UER00401.
DR   Proteomes; UP000002529; 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; Q3Z4Z5.
DR   SWISS-2DPAGE; Q3Z4Z5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
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;  40327 MW;  CDA61225453A3194 CRC64;
     MQDEYYMARA LKLAQRGRFT THPNPNVGCV IVKDGEIVGE GYHQRAGEPH AEVHALRMAG
     EKAKGATAYV TLEPCSHHGR TPPCCDALIA AGVARVVAAM QDPNPQVAGR GLYRLQQAGI
     DVSHGLMMSE AEQLNKGFLK RMRTGFPYIQ LKLGASLDGR TAMASGESQW ITSPQARRDV
     QRQRAQSHAI LTSSATVLAD DPALTVRWSE LDEQTQALYP QQNLRQPVRI VIDSQNRVTP
     EHRIVQQPGE TWFARTQEDS SEWPETVRTL LIPEHKGHLD LVVLMMQLGK QQINSIWVEA
     GPTLAGALLQ AGLVDELIVY IAPKLLGSDA RGLCTLPGLE KLADAPQFKF KEIRHVGPDV
     CLHLVGA
//

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