ID RIB7_METJA Reviewed; 224 AA. AC Q58085; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 07-NOV-2018, entry version 114. DE RecName: Full=2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase; DE Short=DAROPP reductase; DE Short=DARP reductase; DE EC=1.1.1.302; DE AltName: Full=2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one reductase; DE AltName: Full=2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase; DE Short=DARIPP synthase; DE AltName: Full=MjaRED; GN Name=arfC; OrderedLocusNames=MJ0671; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; OC Methanococcales; Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY. RX PubMed=11889103; DOI=10.1128/JB.184.7.1952-1957.2002; RA Graupner M., Xu H., White R.H.; RT "The pyrimidine nucleotide reductase step in riboflavin and F(420) RT biosynthesis in archaea proceeds by the eukaryotic route to RT riboflavin."; RL J. Bacteriol. 184:1952-1957(2002). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION STEREOSPECIFICITY. RX PubMed=18671734; DOI=10.1111/j.1742-4658.2008.06586.x; RA Romisch-Margl W., Eisenreich W., Haase I., Bacher A., Fischer M.; RT "2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthases RT of fungi and archaea."; RL FEBS J. 275:4403-4414(2008). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 6-224 IN COMPLEX WITH NADP, RP PROTEIN SEQUENCE OF 2-11, CATALYTIC ACTIVITY, MASS SPECTROMETRY, RP SUBUNIT, AND REACTION MECHANISM. RX PubMed=16730025; DOI=10.1016/j.jmb.2006.04.045; RA Chatwell L., Krojer T., Fidler A., Romisch W., Eisenreich W., RA Bacher A., Huber R., Fischer M.; RT "Biosynthesis of riboflavin: structure and properties of 2,5-diamino- RT 6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase of RT Methanocaldococcus jannaschii."; RL J. Mol. Biol. 359:1334-1351(2006). CC -!- FUNCTION: Catalyzes an early step in riboflavin biosynthesis, the CC NAD(P)H-dependent reduction of the ribose side chain of 2,5- CC diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding CC 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate. The CC beta anomer is the authentic substrate, and the alpha anomer can CC serve as substrate subsequent to spontaneous anomerization. NADPH CC and NADH function equally well as the reductants. Does not CC catalyze the reduction of 5-amino-6-(5-phospho-D- CC ribosylamino)uracil to 5-amino-6-(5-phospho-D-ribitylamino)uracil. CC {ECO:0000269|PubMed:11889103, ECO:0000269|PubMed:18671734}. CC -!- CATALYTIC ACTIVITY: 2,5-diamino-6-(5-phospho-D- CC ribitylamino)pyrimidin-4(3H)-one + NAD(P)(+) = 2,5-diamino-6-(5- CC phospho-D-ribosylamino)pyrimidin-4(3H)-one + NAD(P)H. CC {ECO:0000269|PubMed:11889103, ECO:0000269|PubMed:16730025, CC ECO:0000269|PubMed:18671734}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16730025}. CC -!- MASS SPECTROMETRY: Mass=24906; Method=Electrospray; Range=2-224; CC Evidence={ECO:0000269|PubMed:16730025}; CC -!- MISCELLANEOUS: The protein sequence in PubMed:16730025 comes from CC protein expressed and processed in E.coli. CC -!- MISCELLANEOUS: Using chirally deuterated NADPH, the enzyme was CC shown to be A-type reductase catalyzing the transfer of deuterium CC from the 4(R) position of NADPH to the 1' (S) position of the CC substrate. CC -!- SIMILARITY: Belongs to the HTP reductase family. {ECO:0000305}. 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; L77117; AAB98665.1; -; Genomic_DNA. DR PIR; G64383; G64383. DR PDB; 2AZN; X-ray; 2.70 A; A/B/C/D/E/F=6-224. DR PDBsum; 2AZN; -. DR ProteinModelPortal; Q58085; -. DR SMR; Q58085; -. DR STRING; 243232.MJ_0671; -. DR EnsemblBacteria; AAB98665; AAB98665; MJ_0671. DR KEGG; mja:MJ_0671; -. DR eggNOG; arCOG01484; Archaea. DR eggNOG; COG1985; LUCA. DR InParanoid; Q58085; -. DR KO; K14654; -. DR OMA; CECGQEV; -. DR OrthoDB; POG093Z04B6; -. DR PhylomeDB; Q58085; -. DR BioCyc; MetaCyc:MONOMER-14596; -. DR BRENDA; 1.1.1.302; 3260. DR UniPathway; UPA00275; -. DR EvolutionaryTrace; Q58085; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB. DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB. DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB. DR GO; GO:0009231; P:riboflavin biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.40.430.10; -; 1. DR InterPro; IPR024072; DHFR-like_dom_sf. DR InterPro; IPR006401; Rib_reduct_arc. DR InterPro; IPR011549; RibD_C. DR InterPro; IPR002734; RibDG_C. DR Pfam; PF01872; RibD_C; 1. DR SUPFAM; SSF53597; SSF53597; 1. DR TIGRFAMs; TIGR01508; rib_reduct_arch; 1. DR TIGRFAMs; TIGR00227; ribD_Cterm; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; NAD; NADP; KW Oxidoreductase; Reference proteome; Riboflavin biosynthesis. FT INIT_MET 1 1 Removed. {ECO:0000305|PubMed:16730025}. FT CHAIN 2 224 2,5-diamino-6-ribosylamino-4(3H)- FT pyrimidinone 5'-phosphate reductase. FT /FTId=PRO_0000135944. FT NP_BIND 83 86 NADP. {ECO:0000269|PubMed:16730025}. FT NP_BIND 156 159 NADP. {ECO:0000269|PubMed:16730025}. FT BINDING 16 16 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000269|PubMed:16730025}. FT BINDING 57 57 NADP. {ECO:0000269|PubMed:16730025}. FT BINDING 61 61 NADP. {ECO:0000269|PubMed:16730025}. FT BINDING 134 134 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000269|PubMed:16730025}. FT STRAND 10 18 {ECO:0000244|PDB:2AZN}. FT STRAND 22 24 {ECO:0000244|PDB:2AZN}. FT HELIX 35 46 {ECO:0000244|PDB:2AZN}. FT STRAND 48 54 {ECO:0000244|PDB:2AZN}. FT HELIX 55 61 {ECO:0000244|PDB:2AZN}. FT STRAND 77 81 {ECO:0000244|PDB:2AZN}. FT HELIX 92 94 {ECO:0000244|PDB:2AZN}. FT STRAND 100 104 {ECO:0000244|PDB:2AZN}. FT HELIX 110 121 {ECO:0000244|PDB:2AZN}. FT STRAND 125 128 {ECO:0000244|PDB:2AZN}. FT STRAND 131 133 {ECO:0000244|PDB:2AZN}. FT HELIX 136 145 {ECO:0000244|PDB:2AZN}. FT STRAND 150 155 {ECO:0000244|PDB:2AZN}. FT HELIX 157 165 {ECO:0000244|PDB:2AZN}. FT STRAND 171 178 {ECO:0000244|PDB:2AZN}. FT STRAND 188 190 {ECO:0000244|PDB:2AZN}. FT HELIX 198 200 {ECO:0000244|PDB:2AZN}. FT STRAND 204 212 {ECO:0000244|PDB:2AZN}. FT STRAND 215 222 {ECO:0000244|PDB:2AZN}. SQ SEQUENCE 224 AA; 25037 MW; 4D8C15CE291E89D8 CRC64; MVMVMEKKPY IISNVGMTLD GKLATINNDS RISCEEDLIR VHKIRANVDG IMVGIGTVLK DDPRLTVHKI KSDRNPVRIV VDSKLRVPLN ARVLNKDAKT IIATTEDTNE EKEKKIKILE DMGVEVVKCG RGKVDLKKLM DILYDKGIKS ILLEGGGTLN WGMFKEGLVD EVSVYIAPKI FGGKEAPTYV DGEGFKTVDE CVKLELKNFY RLGEGIVLEF KVKK //