ID SPRE_BOVIN Reviewed; 267 AA.
AC Q17QK8; A7YKV0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE RecName: Full=Sepiapterin reductase;
DE Short=SPR;
DE EC=1.1.1.153;
GN Name=SPR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Pung Y.F., Cai H.;
RT "Cloning and sequencing of cDNA encoding bovine sepiapterin reductase
RT isoform 2.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the final one or two reductions in tetra-
CC hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-erythro-7,8-dihydrobiopterin + NADP(+) = H(+) + NADPH +
CC sepiapterin; Xref=Rhea:RHEA:18953, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16095, ChEBI:CHEBI:43029, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.153;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = 6-
CC pyruvoyl-5,6,7,8-tetrahydropterin + 2 H(+) + 2 NADPH;
CC Xref=Rhea:RHEA:32627, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:59560, ChEBI:CHEBI:136564;
CC EC=1.1.1.153;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sepiapterin reductase family. {ECO:0000305}.
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DR EMBL; DQ978331; ABI79460.1; -; mRNA.
DR EMBL; BC118299; AAI18300.1; -; mRNA.
DR RefSeq; NP_001069471.1; NM_001076003.1.
DR AlphaFoldDB; Q17QK8; -.
DR SMR; Q17QK8; -.
DR STRING; 9913.ENSBTAP00000064495; -.
DR PaxDb; 9913-ENSBTAP00000029280; -.
DR GeneID; 533836; -.
DR KEGG; bta:533836; -.
DR CTD; 6697; -.
DR eggNOG; KOG1204; Eukaryota.
DR HOGENOM; CLU_010194_2_11_1; -.
DR InParanoid; Q17QK8; -.
DR OrthoDB; 64672at2759; -.
DR TreeFam; TF326358; -.
DR BRENDA; 1.1.1.153; 908.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004757; F:sepiapterin reductase activity; ISS:UniProtKB.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IBA:GO_Central.
DR CDD; cd05367; SPR-like_SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR006393; Sepiapterin_red.
DR NCBIfam; TIGR01500; sepiapter_red; 1.
DR PANTHER; PTHR44085; SEPIAPTERIN REDUCTASE; 1.
DR PANTHER; PTHR44085:SF2; SEPIAPTERIN REDUCTASE; 1.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..267
FT /note="Sepiapterin reductase"
FT /id="PRO_0000327641"
FT BINDING 20..26
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 48..49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 75..76
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 163..164
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 207..212
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P18297"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18297"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18297"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35270"
FT CONFLICT 236
FT /note="E -> Q (in Ref. 1; ABI79460)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 28939 MW; 4F2B7089A40F8C52 CRC64;
MEGSVGKVGG LGRTLCVLTG ASRGFGRTLA QVLAPLMSPR SVLVLSARND EALRQLETEL
GAEWPGLRIV RVPADLGAET GLQQLVGALC DLPRPEGLQR VLLINNAGTL GDVSKRWVDL
TDPTEVNNYW TLNLTSTLCL TSSILQAFPD SPGLSRTVVN ISSICALQPF KGWGLYCAGK
AARNMMFQVL AAEEPSVRVL SYGPGPLDTD MQQLARETSV DPDLRKSLQE LKRKGELVDC
KISAQKLLSL LQNDKFESGA HIDFYDE
//
