RIB7_DEBHA
ID RIB7_DEBHA Reviewed; 247 AA.
AC Q6BII9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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;
GN Name=RIB7; OrderedLocusNames=DEHA2G10010g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalyzes an early step in riboflavin biosynthesis, the
CC NADPH-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. {ECO:0000250}.
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 -!- 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 -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HTP reductase family. {ECO:0000305}.
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DR EMBL; CR382139; CAG90452.1; -; Genomic_DNA.
DR RefSeq; XP_461982.1; XM_461982.1.
DR AlphaFoldDB; Q6BII9; -.
DR SMR; Q6BII9; -.
DR STRING; 4959.XP_461982.1; -.
DR EnsemblFungi; CAG90452; CAG90452; DEHA2G10010g.
DR GeneID; 2904875; -.
DR KEGG; dha:DEHA2G10010g; -.
DR eggNOG; ENOG502RZWZ; Eukaryota.
DR HOGENOM; CLU_036590_5_0_1; -.
DR InParanoid; Q6BII9; -.
DR OMA; WYPFGED; -.
DR OrthoDB; 1535581at2759; -.
DR UniPathway; UPA00275; -.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.430.10; -; 1.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR011549; RibD_C.
DR InterPro; IPR002734; RibDG_C.
DR Pfam; PF01872; RibD_C; 1.
DR SUPFAM; SSF53597; SSF53597; 1.
DR TIGRFAMs; TIGR00227; ribD_Cterm; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome; Riboflavin biosynthesis.
FT CHAIN 1..247
FT /note="2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-
FT phosphate reductase"
FT /id="PRO_0000135938"
FT BINDING 75
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 187..191
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 247 AA; 27372 MW; FD6DE11C29F94DAC CRC64;
MSLLPLTPSL RPFLEEYLPR PCSNRPFVTL TYAQSLDSRI AAKPGEQTKI SHLETKTMTH
YIRSKHDGIM VGIGTVLADD PKLNCRFEAE DGNISTPRPI ILDPTGKWAY HKSQLRSVCD
NNKGLAPFIL IDETVTPRNE DVEVLDKQDG AFVRLPLLRN ADKVGNWNII LKKLFQLGIK
SIMVEGGASI INDLLVYSKI IDSLIITIGP VFLGKDGVEV SPSGHAGLID VKWWQGIQDS
VLCARLT
