ID H2US29_TAKRU Unreviewed; 256 AA.
AC H2US29;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Sepiapterin reductase {ECO:0000256|ARBA:ARBA00019170};
DE EC=1.1.1.153 {ECO:0000256|ARBA:ARBA00013075};
GN Name=smyd1 {ECO:0000313|Ensembl:ENSTRUP00000039752.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000039752.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000039752.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000039752.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the sepiapterin reductase family.
CC {ECO:0000256|ARBA:ARBA00010483}.
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DR AlphaFoldDB; H2US29; -.
DR Ensembl; ENSTRUT00000039893.3; ENSTRUP00000039752.3; ENSTRUG00000015565.3.
DR eggNOG; KOG1204; Eukaryota.
DR GeneTree; ENSGT00940000156114; -.
DR HOGENOM; CLU_010194_2_11_1; -.
DR OMA; RWTVVNV; -.
DR TreeFam; TF326358; -.
DR Proteomes; UP000005226; Chromosome 21.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004757; F:sepiapterin reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro.
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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226}.
SQ SEQUENCE 256 AA; 27345 MW; E8ADB2F2BC1E19B5 CRC64;
MPDASSSHQT SLGRCLCVIT GASRGLGRAM AREVCGLMKP GSVLLLVARS ETLLQELKEE
LRGLTGTAQP AVRCVAVDLS AAGGVNEAVE VARQEAGTDP DHVLLINNAG SLGDISKFSS
FSDLNEVNSY LSLNVSSALA LTAGMLKVFP SRPGLRWSVV NISSLFAVQA LPNWALYCTA
KAARKMMFSV LADEEPNVKV LSYSPGPMDT EMQKDIQRLT GIKHHLIPCK EPAAKLMKLL
LVNEFASGSH LDFFTA
//
