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 23-FEB-2022, entry version 125. 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 / JCM OS 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC 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., Sutton G.G., RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., RA 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 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 of RT 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, SUBUNIT, RP 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., Bacher A., RA Huber R., Fischer M.; RT "Biosynthesis of riboflavin: structure and properties of 2,5-diamino-6- RT 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-diamino-6- CC ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6- CC ribitylamino-4(3H)-pyrimidinone 5'-phosphate. The beta anomer is the CC authentic substrate, and the alpha anomer can serve as substrate CC subsequent to spontaneous anomerization. NADPH and NADH function CC equally well as the reductants. Does not catalyze the reduction of 5- CC amino-6-(5-phospho-D-ribosylamino)uracil to 5-amino-6-(5-phospho-D- CC ribitylamino)uracil. {ECO:0000269|PubMed:11889103, CC ECO:0000269|PubMed:18671734}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'- CC phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin- CC 4(3H)-one 5'-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:27278, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:58890, ChEBI:CHEBI:59545; EC=1.1.1.302; CC Evidence={ECO:0000269|PubMed:11889103, ECO:0000269|PubMed:16730025, CC ECO:0000269|PubMed:18671734}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'- CC phosphate + NAD(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)- CC one 5'-phosphate + H(+) + NADH; Xref=Rhea:RHEA:27274, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:58890, ChEBI:CHEBI:59545; EC=1.1.1.302; CC Evidence={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; 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 shown to CC be A-type reductase catalyzing the transfer of deuterium from the 4(R) CC position of NADPH to the 1' (S) position of the 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 SMR; Q58085; -. DR STRING; 243232.MJ_0671; -. DR EnsemblBacteria; AAB98665; AAB98665; MJ_0671. DR KEGG; mja:MJ_0671; -. DR eggNOG; arCOG01484; Archaea. DR HOGENOM; CLU_036590_4_1_2; -. DR InParanoid; Q58085; -. DR OMA; CECGQEV; -. DR PhylomeDB; Q58085; -. 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; Direct protein sequencing; NAD; NADP; Oxidoreductase; KW Reference proteome; Riboflavin biosynthesis. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000305|PubMed:16730025" FT CHAIN 2..224 FT /note="2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'- FT phosphate reductase" FT /id="PRO_0000135944" FT NP_BIND 83..86 FT /note="NADP" FT /evidence="ECO:0000269|PubMed:16730025" FT NP_BIND 156..159 FT /note="NADP" FT /evidence="ECO:0000269|PubMed:16730025" FT BINDING 16 FT /note="NADP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000269|PubMed:16730025" FT BINDING 57 FT /note="NADP" FT /evidence="ECO:0000269|PubMed:16730025" FT BINDING 61 FT /note="NADP" FT /evidence="ECO:0000269|PubMed:16730025" FT BINDING 134 FT /note="NADP; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000269|PubMed:16730025" FT STRAND 10..18 FT /evidence="ECO:0007829|PDB:2AZN" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:2AZN" FT HELIX 35..46 FT /evidence="ECO:0007829|PDB:2AZN" FT STRAND 48..54 FT /evidence="ECO:0007829|PDB:2AZN" FT HELIX 55..61 FT /evidence="ECO:0007829|PDB:2AZN" FT STRAND 77..81 FT /evidence="ECO:0007829|PDB:2AZN" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:2AZN" FT STRAND 100..104 FT /evidence="ECO:0007829|PDB:2AZN" FT HELIX 110..121 FT /evidence="ECO:0007829|PDB:2AZN" FT STRAND 125..128 FT /evidence="ECO:0007829|PDB:2AZN" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:2AZN" FT HELIX 136..145 FT /evidence="ECO:0007829|PDB:2AZN" FT STRAND 150..155 FT /evidence="ECO:0007829|PDB:2AZN" FT HELIX 157..165 FT /evidence="ECO:0007829|PDB:2AZN" FT STRAND 171..178 FT /evidence="ECO:0007829|PDB:2AZN" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:2AZN" FT HELIX 198..200 FT /evidence="ECO:0007829|PDB:2AZN" FT STRAND 204..212 FT /evidence="ECO:0007829|PDB:2AZN" FT STRAND 215..222 FT /evidence="ECO:0007829|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 //