ID A0A2T5XY18_9FLAO Unreviewed; 350 AA. AC A0A2T5XY18; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 07-NOV-2018, entry version 4. 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 ORFNames=C8P65_10182 {ECO:0000313|EMBL:PTX08418.1}; OS Capnocytophaga leadbetteri. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=327575 {ECO:0000313|EMBL:PTX08418.1, ECO:0000313|Proteomes:UP000243985}; RN [1] {ECO:0000313|EMBL:PTX08418.1, ECO:0000313|Proteomes:UP000243985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22902 {ECO:0000313|EMBL:PTX08418.1, RC ECO:0000313|Proteomes:UP000243985}; RA Goeker M.; RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II RT (KMG-II): from individual species to whole genera."; RL Submitted (APR-2018) 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: 2,5-diamino-6-hydroxy-4-(5- CC phosphoribosylamino)pyrimidine + H(2)O = 5-amino-6-(5- CC phosphoribosylamino)uracil + NH(3). CC {ECO:0000256|PIRNR:PIRNR006769}. CC -!- CATALYTIC ACTIVITY: 5-amino-6-(5-phospho-D-ribitylamino)uracil + CC NADP(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NADPH. CC {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:PTX08418.1}. 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; QBKG01000001; PTX08418.1; -; Genomic_DNA. DR UniPathway; UPA00275; UER00401. DR Proteomes; UP000243985; 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: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; 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 PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1. DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000243985}; 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 1 125 CMP/dCMP-type deaminase. FT {ECO:0000259|PROSITE:PS51747}. 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 77 77 Zinc; catalytic. {ECO:0000256|PIRSR: FT PIRSR006769-3}. FT METAL 86 86 Zinc; catalytic. {ECO:0000256|PIRSR: FT PIRSR006769-3}. FT BINDING 156 156 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000256|PIRSR:PIRSR006769- FT 2}. FT BINDING 175 175 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 189 189 Substrate. {ECO:0000256|PIRSR: FT PIRSR006769-2}. FT BINDING 201 201 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 205 205 NADP. {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 209 209 Substrate; via amide nitrogen. FT {ECO:0000256|PIRSR:PIRSR006769-2}. FT BINDING 212 212 Substrate. {ECO:0000256|PIRSR: FT PIRSR006769-2}. FT BINDING 291 291 Substrate. {ECO:0000256|PIRSR: FT PIRSR006769-2}. SQ SEQUENCE 350 AA; 39328 MW; 4D22C58BDB4C1C54 CRC64; MTDQQYIHRC IQLAQNGLGT TYPNPVVGSV IVYKDRVIGE GWHVRAGEAH AEVRAIASVK DKQLLSQSTL YVSLEPCSHY GKTPPCADLI IAHRIPRVVI GCTDPFAKVA GRGIQKLREA GCEVVVGVCQ EECEALNKRF FTFHQKKRPY IFLKWAETRD GLIAPLHKQE RAPQWITGAY ARQYVHLLRS TEAAILVGAG TVWADNPSLS TRSWYGKSPL RVIIDPRLST RKDFNVWNDE VPTLFIADRD YKGVRHFGQR TEVACIDFGG EVLPQLCKVL YEREVQSLIV EGGAHTLQQF IKADLWDEAL VFRGDTVFTN GLKAPQLSHA CLHSVESFPP DFLMTMVNNK //