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2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase (DAROPP reductase) (DARP reductase) (EC 1.1.1.302) (2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one reductase) (2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase) (DARIPP synthase) (AaeRED)

 RIB7_AQUAE              Reviewed;         224 AA.
O66747;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
28-FEB-2018, entry version 83.
RecName: Full=2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase;
Short=DAROPP reductase;
Short=DARP reductase;
EC=1.1.1.302;
AltName: Full=2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one reductase;
AltName: Full=2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase;
Short=DARIPP synthase;
AltName: Full=AaeRED;
Name=ribD2; OrderedLocusNames=aq_436;
Aquifex aeolicus (strain VF5).
Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
NCBI_TaxID=224324;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VF5;
PubMed=9537320; DOI=10.1038/32831;
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
"The complete genome of the hyperthermophilic bacterium Aquifex
aeolicus.";
Nature 392:353-358(1998).
[2]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
STRAIN=VF5;
PubMed=18671734; DOI=10.1111/j.1742-4658.2008.06586.x;
Romisch-Margl W., Eisenreich W., Haase I., Bacher A., Fischer M.;
"2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthases
of fungi and archaea.";
FEBS J. 275:4403-4414(2008).
-!- FUNCTION: Catalyzes an early step in riboflavin biosynthesis, the
NADPH-dependent reduction of the ribose side chain of 2,5-diamino-
6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-
diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate.
{ECO:0000269|PubMed:18671734}.
-!- CATALYTIC ACTIVITY: 2,5-diamino-6-(5-phospho-D-
ribitylamino)pyrimidin-4(3H)-one + NAD(P)(+) = 2,5-diamino-6-(5-
phospho-D-ribosylamino)pyrimidin-4(3H)-one + NAD(P)H.
{ECO:0000269|PubMed:18671734}.
-!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18671734}.
-!- SIMILARITY: Belongs to the HTP reductase family. {ECO:0000305}.
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EMBL; AE000657; AAC06708.1; -; Genomic_DNA.
PIR; G70339; G70339.
RefSeq; NP_213307.1; NC_000918.1.
RefSeq; WP_010880245.1; NC_000918.1.
ProteinModelPortal; O66747; -.
SMR; O66747; -.
STRING; 224324.aq_436; -.
EnsemblBacteria; AAC06708; AAC06708; aq_436.
GeneID; 1193073; -.
KEGG; aae:aq_436; -.
PATRIC; fig|224324.8.peg.360; -.
eggNOG; ENOG4105WCJ; Bacteria.
eggNOG; COG1985; LUCA.
HOGENOM; HOG000225965; -.
InParanoid; O66747; -.
KO; K00082; -.
OMA; CECGQEV; -.
OrthoDB; POG091H01D3; -.
BioCyc; AAEO224324:G1G15-324-MONOMER; -.
BRENDA; 1.1.1.302; 396.
UniPathway; UPA00275; -.
Proteomes; UP000000798; Chromosome.
GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
GO; GO:0009231; P:riboflavin biosynthetic process; IDA:UniProtKB.
GO; GO:0009451; P:RNA modification; IBA:GO_Central.
Gene3D; 3.40.430.10; -; 1.
InterPro; IPR024072; DHFR-like_dom_sf.
InterPro; IPR006401; Rib_reduct_arc.
InterPro; IPR011549; RibD_C.
InterPro; IPR002734; RibDG_C.
Pfam; PF01872; RibD_C; 1.
SUPFAM; SSF53597; SSF53597; 1.
TIGRFAMs; TIGR01508; rib_reduct_arch; 1.
TIGRFAMs; TIGR00227; ribD_Cterm; 1.
1: Evidence at protein level;
Complete proteome; NADP; Oxidoreductase; Reference proteome;
Riboflavin biosynthesis.
CHAIN 1 224 2,5-diamino-6-ribosylamino-4(3H)-
pyrimidinone 5'-phosphate reductase.
/FTId=PRO_0000418811.
NP_BIND 82 85 NADP. {ECO:0000250}.
NP_BIND 153 156 NADP. {ECO:0000250}.
BINDING 57 57 NADP. {ECO:0000250}.
BINDING 61 61 NADP. {ECO:0000250}.
BINDING 131 131 NADP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
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


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