ID RIBD1_BUCAP Reviewed; 147 AA. AC Q8K9A4; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 16-JUN-2009, entry version 46. DE RecName: Full=Diaminohydroxyphosphoribosylamino-pyrimidine deaminase; DE Short=DRAP deaminase; DE EC=3.5.4.26; DE AltName: Full=Riboflavin-specific deaminase; GN Name=ribD1; OrderedLocusNames=BUsg_445; OS Buchnera aphidicola subsp. Schizaphis graminum. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Buchnera. OX NCBI_TaxID=98794; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). CC -!- CATALYTIC ACTIVITY: 2,5-diamino-6-hydroxy-4-(5- CC phosphoribosylamino)pyrimidine + H(2)O = 5-amino-6-(5- CC phosphoribosylamino)uracil + NH(3). CC -!- COFACTOR: Binds 1 zinc ion (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 6,7- CC dimethyl-8-(1-D-ribityl)lumazine from GTP: step 2/4. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE013218; AAM67988.1; -; Genomic_DNA. DR RefSeq; NP_660777.1; -. DR HSSP; Q12178; 1UAQ. DR GeneID; 1005719; -. DR GenomeReviews; AE013218_GR; BUsg_445. DR KEGG; bas:BUsg445; -. DR HOGENOM; Q8K9A4; -. DR OMA; Q8K9A4; PPVGCVL. DR BioCyc; BAPH198804:BUSG445-MON; -. DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil red...; IEA:InterPro. DR GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine...; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR002125; CMP_dCMP_Zn_bd. DR InterPro; IPR004794; Eubact_ribD. DR PANTHER; PTHR11079:SF10; Eubact_ribD; 1. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR TIGRFAMs; TIGR00326; eubact_ribD; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Riboflavin biosynthesis; KW Zinc. FT CHAIN 1 147 Diaminohydroxyphosphoribosylamino- FT pyrimidine deaminase. FT /FTId=PRO_0000171726. FT ACT_SITE 52 52 Proton donor (By similarity). FT METAL 50 50 Zinc; catalytic (By similarity). FT METAL 75 75 Zinc; catalytic (By similarity). FT METAL 84 84 Zinc; catalytic (By similarity). SQ SEQUENCE 147 AA; 16233 MW; EBCCF068610EECF0 CRC64; MKDRFYMTRA IKLSKLGEFT TSPNPNVGCV IVQNKKIVGE GWHKKYGENH AEINALNMAG EKAKGSTAYI TLEPCNHFGK TPPCCDAIIQ SGIKNVIISS LDPNPKVSGK GVLYLRKKGI SVKIGLMSKE SQKYNKGFFK RMRTGLP //