ID A0A2N2QZR2_9PROT Unreviewed; 362 AA. AC A0A2N2QZR2; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 03-MAY-2023, entry version 17. 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; Pseudomonadota; Betaproteobacteria. OX NCBI_TaxID=2013718 {ECO:0000313|EMBL:PKO36208.1, ECO:0000313|Proteomes:UP000233284}; RN [1] {ECO:0000313|EMBL:PKO36208.1, ECO:0000313|Proteomes:UP000233284} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., Anantharaman K., RA Probst A., Burstein D., Thomas B.C., Banfield J.F.; RT "Potential for microbial H2 and metal transformations associated with novel RT bacteria and archaea in deep terrestrial subsurface sediments."; RL ISME J. 11:1915-1929(2017). CC -!- FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'- CC phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'- CC phosphate. {ECO:0000256|ARBA:ARBA00002151, CC ECO:0000256|PIRNR:PIRNR006769}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + CC H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+); CC Xref=Rhea:RHEA:21868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28938, 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-6-(D- CC ribitylamino)uracil from GTP: step 2/4. {ECO:0000256|ARBA:ARBA00004882, CC ECO:0000256|PIRNR:PIRNR006769}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D- CC ribitylamino)uracil from GTP: step 3/4. {ECO:0000256|ARBA:ARBA00004910, CC ECO:0000256|PIRNR:PIRNR006769}. CC -!- SIMILARITY: In the C-terminal section; belongs to the HTP reductase CC family. {ECO:0000256|ARBA:ARBA00007417, ECO:0000256|PIRNR:PIRNR006769}. CC -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and CC deoxycytidylate deaminase family. {ECO:0000256|ARBA:ARBA00005259, CC ECO:0000256|PIRNR:PIRNR006769}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 AlphaFoldDB; A0A2N2QZR2; -. DR UniPathway; UPA00275; UER00401. DR Proteomes; UP000233284; Unassembled WGS sequence. 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 CDD; cd01284; Riboflavin_deaminase-reductase; 1. DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1. DR Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 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 PANTHER; PTHR38011:SF7; 2,5-DIAMINO-6-RIBOSYLAMINO-4(3H)-PYRIMIDINONE 5'-PHOSPHATE REDUCTASE; 1. DR PANTHER; PTHR38011; DIHYDROFOLATE REDUCTASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_8G06820); 1. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR Pfam; PF01872; RibD_C; 1. DR PIRSF; PIRSF006769; RibD; 1. DR SUPFAM; SSF53927; Cytidine deaminase-like; 1. DR SUPFAM; SSF53597; Dihydrofolate reductase-like; 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|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR006769}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW NADP {ECO:0000256|PIRNR:PIRNR006769, ECO:0000256|PIRSR:PIRSR006769-2}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006769}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, KW ECO:0000256|PIRNR:PIRNR006769}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006769}. FT DOMAIN 5..126 FT /note="CMP/dCMP-type deaminase" FT /evidence="ECO:0000259|PROSITE:PS51747" FT ACT_SITE 56 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-1" FT BINDING 54 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3" FT BINDING 79 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3" FT BINDING 88 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3" FT BINDING 158 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 172 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 174 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 188 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 200 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 204 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 208 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 211 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 226 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 294 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 296..302 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000256|PIRSR: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 //