RIB7_YEAST
ID RIB7_YEAST Reviewed; 244 AA.
AC P33312; D6VQE8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 167.
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=YBR153W; ORFNames=YBR1203;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Buitrago M.J., Garcia-Ramirez J.J., Revuelta J.L.;
RT "Cloning and sequencing of the RIB7 gene from Saccharomyces cerevisiae.";
RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8488729; DOI=10.1002/yea.320090308;
RA Baur A., Schaaff-Gerstenschlaeger I., Boles E., Miosga T., Rose M.,
RA Zimmermann F.K.;
RT "Sequence of a 4.8 kb fragment of Saccharomyces cerevisiae chromosome II
RT including three essential open reading frames.";
RL Yeast 9:289-293(1993).
RN [3]
RP ERRATUM OF PUBMED:8488729.
RX PubMed=8203148; DOI=10.1002/yea.320100113;
RA Baur A., Schaaff-Gerstenschlaeger I., Boles E., Miosga T., Rose M.,
RA Zimmermann F.K.;
RL Yeast 10:131-131(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=4555411; DOI=10.1128/jb.110.3.818-822.1972;
RA Oltmanns O., Bacher A.;
RT "Biosynthesis of riboflavine in Saccharomyces cerevisiae: the role of genes
RT rib 1 and rib 7.";
RL J. Bacteriol. 110:818-822(1972).
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.
CC {ECO:0000305|PubMed:4555411}.
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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate a 6-hydroxy-
CC 2,4,5-triaminopyrimidine derivative. {ECO:0000269|PubMed:4555411}.
CC -!- SIMILARITY: Belongs to the HTP reductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC60554.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z21622; CAA79746.1; -; Genomic_DNA.
DR EMBL; X71329; CAA50471.1; -; Genomic_DNA.
DR EMBL; S59774; AAC60554.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z36022; CAA85112.1; -; Genomic_DNA.
DR EMBL; AY557713; AAS56039.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07268.1; -; Genomic_DNA.
DR PIR; S40698; S40698.
DR RefSeq; NP_009711.3; NM_001178501.3.
DR PDB; 4HA7; X-ray; 2.10 A; A/B=1-244.
DR PDB; 4HA9; X-ray; 2.35 A; A/B=1-244.
DR PDBsum; 4HA7; -.
DR PDBsum; 4HA9; -.
DR AlphaFoldDB; P33312; -.
DR SMR; P33312; -.
DR BioGRID; 32852; 63.
DR IntAct; P33312; 2.
DR STRING; 4932.YBR153W; -.
DR MaxQB; P33312; -.
DR PaxDb; P33312; -.
DR PRIDE; P33312; -.
DR EnsemblFungi; YBR153W_mRNA; YBR153W; YBR153W.
DR GeneID; 852450; -.
DR KEGG; sce:YBR153W; -.
DR SGD; S000000357; RIB7.
DR VEuPathDB; FungiDB:YBR153W; -.
DR eggNOG; ENOG502RZWZ; Eukaryota.
DR HOGENOM; CLU_036590_5_0_1; -.
DR OMA; WYPFGED; -.
DR BioCyc; MetaCyc:MON3O-27; -.
DR BioCyc; YEAST:MON3O-27; -.
DR UniPathway; UPA00275; -.
DR PRO; PR:P33312; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P33312; protein.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IDA:SGD.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome;
KW Riboflavin biosynthesis.
FT CHAIN 1..244
FT /note="2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-
FT phosphate reductase"
FT /id="PRO_0000135942"
FT BINDING 79
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 182..186
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT HELIX 10..15
FT /evidence="ECO:0007829|PDB:4HA7"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:4HA7"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:4HA7"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4HA7"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:4HA7"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:4HA7"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:4HA7"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4HA7"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:4HA7"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:4HA7"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:4HA7"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:4HA7"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:4HA7"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:4HA7"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:4HA7"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:4HA7"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:4HA7"
FT STRAND 197..207
FT /evidence="ECO:0007829|PDB:4HA7"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:4HA7"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:4HA7"
SQ SEQUENCE 244 AA; 27116 MW; BB19A9D2A1A8D7DB CRC64;
MSLTPLCEDL PQFLQNYLPN AGQTENTIVP FVTLTYAQSL DARVSRGPGV RTTISHPETK
TMTHYLRHHH DGILVGSGTV LADNPGLNCK WGPDPAANSP RPIIIDTKQK WRFDGSKMQE
LFIKRQGKPP IVVVTSEPII KEQHVDYAIC PINDTTKLVD WKKLFEILKE EFNIRSVMVE
GGANVINQLL LRSDIVNSLI ITIGSTFLGS SGTEVSPPQT VNLKDMSWWK GITDVVLCAR
LADD
