RIB7_CANGA
ID RIB7_CANGA Reviewed; 244 AA.
AC Q6FU96;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=CglRED;
GN Name=RIB7; OrderedLocusNames=CAGL0F05203g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, REACTION STEREOSPECIFICITY, AND SUBUNIT.
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).
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: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: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:18671734};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18671734}.
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; CR380952; CAG59122.1; -; Genomic_DNA.
DR RefSeq; XP_446198.1; XM_446198.1.
DR AlphaFoldDB; Q6FU96; -.
DR SMR; Q6FU96; -.
DR STRING; 5478.XP_446198.1; -.
DR EnsemblFungi; CAG59122; CAG59122; CAGL0F05203g.
DR GeneID; 2887749; -.
DR KEGG; cgr:CAGL0F05203g; -.
DR CGD; CAL0129209; RIB7.
DR VEuPathDB; FungiDB:CAGL0F05203g; -.
DR eggNOG; ENOG502RZWZ; Eukaryota.
DR HOGENOM; CLU_036590_5_0_1; -.
DR InParanoid; Q6FU96; -.
DR OMA; WYPFGED; -.
DR BRENDA; 1.1.1.302; 1113.
DR UniPathway; UPA00275; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:EnsemblFungi.
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; 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 NADP; Oxidoreductase; Reference proteome; Riboflavin biosynthesis.
FT CHAIN 1..244
FT /note="2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-
FT phosphate reductase"
FT /id="PRO_0000135937"
FT BINDING 74
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 183..187
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 244 AA; 27568 MW; 023343B53EF0460E CRC64;
MLRVRDDLPP FLKNYLPDGH RNGRPFVTLT YAQSIDAKIA KQRGVRTTIS HIETKEMTHY
LRYFHDGILI GSGTVLADDP GLNCKWIGPN NDPDESMEEK SPRPIILDPK LKWKYSGSKM
EELCNQGMGK PPIVITTKTP KVKEANVEYM IMEPDANDRI SWKSILDTLR RNYDMKSVMI
EGGSHVINQL LMCSDLIDSL IVTIGSIYLG SEGVTVSPPD EVKLKDISWW KGTSDVVMCS
RLQN
