RIB7_AQUAE
ID RIB7_AQUAE Reviewed; 224 AA.
AC O66747;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, 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;
DE AltName: Full=AaeRED;
GN Name=ribD2; OrderedLocusNames=aq_436;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=VF5;
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 -!- SIMILARITY: Belongs to the HTP reductase family. {ECO:0000305}.
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DR EMBL; AE000657; AAC06708.1; -; Genomic_DNA.
DR PIR; G70339; G70339.
DR RefSeq; NP_213307.1; NC_000918.1.
DR RefSeq; WP_010880245.1; NC_000918.1.
DR AlphaFoldDB; O66747; -.
DR SMR; O66747; -.
DR STRING; 224324.aq_436; -.
DR PRIDE; O66747; -.
DR EnsemblBacteria; AAC06708; AAC06708; aq_436.
DR KEGG; aae:aq_436; -.
DR PATRIC; fig|224324.8.peg.360; -.
DR eggNOG; COG1985; Bacteria.
DR HOGENOM; CLU_036590_4_1_0; -.
DR InParanoid; O66747; -.
DR OMA; CECGQEV; -.
DR OrthoDB; 900513at2; -.
DR BRENDA; 1.1.1.302; 396.
DR UniPathway; UPA00275; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:InterPro.
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; 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 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome; Riboflavin biosynthesis.
FT CHAIN 1..224
FT /note="2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-
FT phosphate reductase"
FT /id="PRO_0000418811"
FT BINDING 57
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 82..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 224 AA; 25257 MW; E4A21E2EA4540024 CRC64;
MERPYVIIVS EVSVDGKLTL YRGASSKELM SLMDEEAYKY LHEIRAKVDG IMVGCETVRT
DNPSLTVRYA KGKNPVRIIP CSTANVPLDA NVLNTKEAPT IIATTERAPK ERLEKIKELG
AEVIVVGDEL VDFDKLLPEL YRRGIKSLMV EGGASINWEF VRRRVVDEIR LIHLPVIVGG
ENVPTLVGGE GFKKLKNLLH LRLRSHFVRG KQLITEWEVV NKIR
