ID A0A7L5UF69_9LACO Unreviewed; 351 AA. AC A0A7L5UF69; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 19-JAN-2022, 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 Name=ribD {ECO:0000313|EMBL:QLL69106.1}; GN ORFNames=GTO83_00200 {ECO:0000313|EMBL:QLL69106.1}; OS Lactobacillus sp. 3B(2020). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus; unclassified Lactobacillus. OX NCBI_TaxID=2695882 {ECO:0000313|EMBL:QLL69106.1, ECO:0000313|Proteomes:UP000510624}; RN [1] {ECO:0000313|EMBL:QLL69106.1, ECO:0000313|Proteomes:UP000510624} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=3B(2020) {ECO:0000313|Proteomes:UP000510624}; RA Hassan H.M.; RT "Complete and circular genome sequences of six lactobacillus isolates from RT horses."; RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases. 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|ARBA:ARBA00000334, CC 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|ARBA:ARBA00000659, 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-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 --------------------------------------------------------------------------- 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; CP047410; QLL69106.1; -; Genomic_DNA. DR UniPathway; UPA00275; UER00401. DR Proteomes; UP000510624; Chromosome. 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 Hydrolase {ECO:0000256|PIRNR:PIRNR006769, ECO:0000313|EMBL:QLL69106.1}; 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 ECO:0000313|EMBL:QLL69106.1}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, KW ECO:0000256|PIRNR:PIRNR006769}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006769}. FT DOMAIN 2..125 FT /note="CMP/dCMP-type deaminase" FT /evidence="ECO:0000259|PROSITE:PS51747" FT NP_BIND 290..296 FT /note="NADP" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT ACT_SITE 53 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-1" FT METAL 51 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3" FT METAL 77 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3" FT METAL 86 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-3" FT BINDING 156 FT /note="NADP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 185 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 197 FT /note="NADP" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 201 FT /note="NADP" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 205 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" FT BINDING 288 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR006769-2" SQ SEQUENCE 351 AA; 38579 MW; C70C3C32C8DFEA65 CRC64; MNHDQAMMQL AINAAKEGRF LTWQNPMVGA AVVKDGHVLA LGHHVKYGAV HAERNAIEKL TPEQLFNATL YVTLEPCNHQ GKQPPCSELI IHSKIKRVVI GQTDPHALVT GKGIARLKTA GIEVITGVLA DQATALNPFY TYFFQHHQPW ITLKQAISLD HKLSLPGQRI TLSSSAALKQ VHFERANYQG ILIGSETAII DDPSLLTTVK SPFPPIRMII DRRGRLLNHP NLKLLTDGAA PTWIFTQNNQ LGNHQWPAHV KVISLADGQL SSVIDYLTDQ GIQSLYVEGG RRLHQAFCDA GLGNELITYL APVTLGKNGV PAYQPKAGQL IKPSYQFFGN TIRIQGGIQN V //