ID A0A2N2QZR2_9PROT Unreviewed; 362 AA. AC A0A2N2QZR2; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 10-APR-2019, entry version 7. 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:PKO36208.1}; GN ORFNames=CVU33_19595 {ECO:0000313|EMBL:PKO36208.1}; OS Betaproteobacteria bacterium HGW-Betaproteobacteria-6. OC Bacteria; Proteobacteria; Betaproteobacteria. OX NCBI_TaxID=2013718 {ECO:0000313|EMBL:PKO36208.1}; RN [1] {ECO:0000313|EMBL:PKO36208.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGW-Betaproteobacteria-6 {ECO:0000313|EMBL:PKO36208.1}; RX PubMed=28350393; DOI=10.1038/ismej.2017.39; RA Hernsdorf A.W., Amano Y., Miyakawa K., Ise K., Suzuki Y., RA Anantharaman K., Probst A., Burstein D., Thomas B.C., Banfield J.F.; RT "Potential for microbial H2 and metal transformations associated with RT novel bacteria and archaea in deep terrestrial subsurface sediments."; RL ISME J. 11:1915-1929(2017). RN [2] {ECO:0000313|EMBL:PKO36208.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HGW-Betaproteobacteria-6 {ECO:0000313|EMBL:PKO36208.1}; RA Han C.G.; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. 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}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PKO36208.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; PHCF01000167; PKO36208.1; -; Genomic_DNA. DR UniPathway; UPA00275; UER00401. 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; 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 5 126 CMP/dCMP-type deaminase. FT {ECO:0000259|PROSITE:PS51747}. FT NP_BIND 296 302 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT ACT_SITE 56 56 Proton donor. {ECO:0000256|PIRSR: FT PIRSR006769-1}. FT METAL 54 54 Zinc; catalytic. {ECO:0000256|PIRSR: FT PIRSR006769-3}. FT METAL 79 79 Zinc; catalytic. {ECO:0000256|PIRSR: FT PIRSR006769-3}. FT METAL 88 88 Zinc; catalytic. {ECO:0000256|PIRSR: FT PIRSR006769-3}. FT BINDING 158 158 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR006769- FT 2}. FT BINDING 172 172 Substrate. {ECO:0000256|PIRSR: FT PIRSR006769-2}. FT BINDING 174 174 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 188 188 Substrate. {ECO:0000256|PIRSR: FT PIRSR006769-2}. FT BINDING 200 200 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 204 204 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 208 208 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 211 211 Substrate. {ECO:0000256|PIRSR: FT PIRSR006769-2}. FT BINDING 226 226 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 294 294 Substrate. {ECO:0000256|PIRSR: FT PIRSR006769-2}. SQ SEQUENCE 362 AA; 38834 MW; 583FA7754E7D5400 CRC64; MSFSADDFRL MARALQLAER GLWTTSPNPR VGCVLVRDGD IVGEGWHEKA GEPHAEVHAL RVAGDRARGA TAYVTLEPCS HHGRTPPCAE ALIAAGVSRV VAAMTDPNPL VSGKGLALLQ AAGITTASGL LENEARELNI GFVSRMTRGR PWLRLKAAAS LDGKTALNNG VSQWITGPAA RRDGHAWRAR ACAILTGIGT VRDDDPSLTV RDVATTRQPL RVVVDSRLEI APTARILQGE PVLIVGAVEN AEKMALLRST GNFVEILNNG SGKVDLKALL ELLAQRGINE VHAEAGFKLN GSLLREGLVD ELLLYLAPCL IGHEASGLFN LPELTTLDGK RQLKIRDLRQ LGEDIRLIAR LP //