RIB7_SCHPO
ID RIB7_SCHPO Reviewed; 268 AA.
AC Q9P7L3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 ORFNames=SPBC21C3.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; CU329671; CAB76046.1; -; Genomic_DNA.
DR PIR; T50354; T50354.
DR RefSeq; NP_596590.1; NM_001022510.2.
DR AlphaFoldDB; Q9P7L3; -.
DR SMR; Q9P7L3; -.
DR BioGRID; 277151; 1.
DR STRING; 4896.SPBC21C3.10c.1; -.
DR MaxQB; Q9P7L3; -.
DR PaxDb; Q9P7L3; -.
DR EnsemblFungi; SPBC21C3.10c.1; SPBC21C3.10c.1:pep; SPBC21C3.10c.
DR PomBase; SPBC21C3.10c; -.
DR VEuPathDB; FungiDB:SPBC21C3.10c; -.
DR eggNOG; ENOG502RZWZ; Eukaryota.
DR HOGENOM; CLU_036590_6_0_1; -.
DR InParanoid; Q9P7L3; -.
DR OMA; ERWNCIE; -.
DR PhylomeDB; Q9P7L3; -.
DR UniPathway; UPA00275; -.
DR PRO; PR:Q9P7L3; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; ISS:PomBase.
DR GO; GO:0009231; P:riboflavin biosynthetic process; ISO:PomBase.
DR Gene3D; 3.40.430.10; -; 1.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR002734; RibDG_C.
DR Pfam; PF01872; RibD_C; 1.
DR SUPFAM; SSF53597; SSF53597; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome; Riboflavin biosynthesis.
FT CHAIN 1..268
FT /note="2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-
FT phosphate reductase"
FT /id="PRO_0000135941"
FT BINDING 68
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 103..106
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 191..195
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 268 AA; 29752 MW; 40D1260B418805C3 CRC64;
MESSQAYFPP SANKKHVLLT WAQSINGRIG YVVESPSLGQ LRLSSKESFV MTHLLRTKFD
GIMVGSRTAE NDNPSLTAKL PDPANPDCLL PLNKQPIPII VDSNLRLDYA SLKVIRLARE
RLGKPPLIIV APSIWQQVQH DSKLKEAVKL IQSVGGRCII RNEDSPDSWS DYVALDKLLQ
NGVNRIMVEG GAELLAKAFG STDIDAYVVT IVPKIFSCSN TTEIKNLNNL NLTTNSHWYP
CGPDVIFTNY SDEFYESYKS LLTNSDAI
