DHPR_DICDI
ID DHPR_DICDI Reviewed; 231 AA.
AC Q86A17; Q559B3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Dihydropteridine reductase;
DE EC=1.5.1.34;
DE AltName: Full=Quinoid dihydropteridine reductase;
GN Name=qdpr; ORFNames=DDB_G0272684;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP SUBUNIT, AND CRYSTALLIZATION.
RX PubMed=18997329; DOI=10.1107/s1744309108028479;
RA Chen C., Seo K.H., Kim H.L., Zhuang N., Park Y.S., Lee K.H.;
RT "Crystallization and preliminary characterization of dihydropteridine
RT reductase from Dictyostelium discoideum.";
RL Acta Crystallogr. F 64:1013-1015(2008).
CC -!- FUNCTION: The product of this enzyme, tetrahydrobiopterin (BH-4), is an
CC essential cofactor for phenylalanine, tyrosine, and tryptophan
CC hydroxylases. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydropteridine + NAD(+) = 6,7-dihydropteridine +
CC H(+) + NADH; Xref=Rhea:RHEA:17869, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28889, ChEBI:CHEBI:30156, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.5.1.34;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydropteridine + NADP(+) = 6,7-dihydropteridine +
CC H(+) + NADPH; Xref=Rhea:RHEA:17865, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28889, ChEBI:CHEBI:30156, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.5.1.34;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18997329}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AAFI02000008; EAL70979.1; -; Genomic_DNA.
DR RefSeq; XP_644903.1; XM_639811.1.
DR PDB; 3ORF; X-ray; 2.16 A; A/B/C/D=1-231.
DR PDBsum; 3ORF; -.
DR AlphaFoldDB; Q86A17; -.
DR SMR; Q86A17; -.
DR MINT; Q86A17; -.
DR STRING; 44689.DDB0237752; -.
DR PaxDb; Q86A17; -.
DR EnsemblProtists; EAL70979; EAL70979; DDB_G0272684.
DR GeneID; 8618582; -.
DR KEGG; ddi:DDB_G0272684; -.
DR dictyBase; DDB_G0272684; qdpr.
DR eggNOG; KOG4022; Eukaryota.
DR HOGENOM; CLU_010194_22_0_1; -.
DR InParanoid; Q86A17; -.
DR OMA; DWWVASI; -.
DR PhylomeDB; Q86A17; -.
DR BRENDA; 1.5.1.34; 1939.
DR Reactome; R-DDI-8964208; Phenylalanine metabolism.
DR PRO; PR:Q86A17; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0004155; F:6,7-dihydropteridine reductase activity; IDA:dictyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR GO; GO:0051287; F:NAD binding; IDA:dictyBase.
DR GO; GO:0070404; F:NADH binding; IBA:GO_Central.
DR GO; GO:0070402; F:NADPH binding; IBA:GO_Central.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IMP:dictyBase.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IMP:dictyBase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome;
KW Tetrahydrobiopterin biosynthesis.
FT CHAIN 1..231
FT /note="Dihydropteridine reductase"
FT /id="PRO_0000327797"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 6..30
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3ORF"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:3ORF"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:3ORF"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:3ORF"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3ORF"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:3ORF"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:3ORF"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3ORF"
FT HELIX 88..113
FT /evidence="ECO:0007829|PDB:3ORF"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:3ORF"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3ORF"
FT HELIX 136..152
FT /evidence="ECO:0007829|PDB:3ORF"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3ORF"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:3ORF"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:3ORF"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3ORF"
FT HELIX 193..205
FT /evidence="ECO:0007829|PDB:3ORF"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3ORF"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:3ORF"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:3ORF"
SQ SEQUENCE 231 AA; 24651 MW; 0D5E03DFF4F6AA14 CRC64;
MSKNILVLGG SGALGAEVVK FFKSKSWNTI SIDFRENPNA DHSFTIKDSG EEEIKSVIEK
INSKSIKVDT FVCAAGGWSG GNASSDEFLK SVKGMIDMNL YSAFASAHIG AKLLNQGGLF
VLTGASAALN RTSGMIAYGA TKAATHHIIK DLASENGGLP AGSTSLGILP VTLDTPTNRK
YMSDANFDDW TPLSEVAEKL FEWSTNSDSR PTNGSLVKFE TKSKVTTWTN L
