ID A0A2T5XY18_9FLAO Unreviewed; 350 AA. AC A0A2T5XY18; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 12-SEP-2018, entry version 2. 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 Note=Binds 1 zinc ion. {ECO:0000256|PIRNR:PIRNR006769}; 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 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 NADP {ECO:0000256|PIRNR:PIRNR006769}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006769}; KW Riboflavin biosynthesis {ECO:0000256|PIRNR:PIRNR006769}; KW Zinc {ECO:0000256|PIRNR:PIRNR006769}. FT DOMAIN 1 125 CMP/dCMP-type deaminase. FT {ECO:0000259|PROSITE:PS51747}. 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 //