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RIB7_SACS2
ID   RIB7_SACS2              Reviewed;         213 AA.
AC   P95872;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 118.
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   OrderedLocusNames=SSO2097; ORFNames=C06025, C06_008;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA   Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA   Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA   Ragan M.A., Charlebois R.L.;
RT   "Organizational characteristics and information content of an archaeal
RT   genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL   Mol. Microbiol. 22:175-191(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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; Y08256; CAA69508.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK42277.1; -; Genomic_DNA.
DR   PIR; S74011; S74011.
DR   RefSeq; WP_010923770.1; NC_002754.1.
DR   AlphaFoldDB; P95872; -.
DR   SMR; P95872; -.
DR   STRING; 273057.SSO2097; -.
DR   EnsemblBacteria; AAK42277; AAK42277; SSO2097.
DR   GeneID; 44130802; -.
DR   KEGG; sso:SSO2097; -.
DR   PATRIC; fig|273057.12.peg.2179; -.
DR   eggNOG; arCOG01484; Archaea.
DR   HOGENOM; CLU_036590_4_1_2; -.
DR   InParanoid; P95872; -.
DR   OMA; CECGQEV; -.
DR   PhylomeDB; P95872; -.
DR   UniPathway; UPA00275; -.
DR   Proteomes; UP000001974; Chromosome.
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: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; IBA:GO_Central.
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   3: Inferred from homology;
KW   NADP; Oxidoreductase; Reference proteome; Riboflavin biosynthesis.
FT   CHAIN           1..213
FT                   /note="2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-
FT                   phosphate reductase"
FT                   /id="PRO_0000135946"
FT   BINDING         53
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         79..82
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         145..148
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  24561 MW;  A741F6CADEF7631C CRC64;
     MVMKPYVIIF STVSIDGRLA TKTGYSELSC PYDKQRQHEI RSEVDAVMVG ANTVRVDNPS
     LTVKYGKNRR NPIRVVVTRS FNLDPSYKIF TTPPSTVIYT SNYESEKVEE FIRKGVIVRK
     FLHLDDLLED LYDNFNVRRL MVEGGGHLIW WFIKDNLYDE IRITISPRIF GNGVSFTQGE
     GFIGEDSPRL ELIDAKICEC GNEVHLTYKK YMT
 
 
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