ID A0A3B4D631_PYGNA Unreviewed; 322 AA.
AC A0A3B4D631;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=6-pyruvoyl tetrahydrobiopterin synthase {ECO:0000256|ARBA:ARBA00015587};
DE EC=4.2.3.12 {ECO:0000256|ARBA:ARBA00013100};
GN Name=PTS {ECO:0000313|Ensembl:ENSPNAP00000019822.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000019822.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000019822.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Involved in the biosynthesis of tetrahydrobiopterin, an
CC essential cofactor of aromatic amino acid hydroxylases. Catalyzes the
CC transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl
CC tetrahydropterin. {ECO:0000256|ARBA:ARBA00025266}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis;
CC tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00005126}.
CC -!- SIMILARITY: Belongs to the PTPS family.
CC {ECO:0000256|ARBA:ARBA00009164}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B4D631; -.
DR STRING; 42514.ENSPNAP00000019822; -.
DR Ensembl; ENSPNAT00000029913.1; ENSPNAP00000019822.1; ENSPNAG00000026559.1.
DR GeneTree; ENSGT00390000002752; -.
DR UniPathway; UPA00849; UER00819.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR GO; GO:0003874; F:6-pyruvoyltetrahydropterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00470; PTPS; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.479.10; 6-pyruvoyl tetrahydropterin synthase/QueD; 1.
DR InterPro; IPR007115; 6-PTP_synth/QueD.
DR InterPro; IPR038418; 6-PTP_synth/QueD_sf.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR022470; PTPS_Cys_AS.
DR InterPro; IPR022469; PTPS_His_AS.
DR PANTHER; PTHR12589:SF7; 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR PANTHER; PTHR12589; PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR Pfam; PF01242; PTPS; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 2.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
DR PROSITE; PS00987; PTPS_1; 1.
DR PROSITE; PS00988; PTPS_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Tetrahydrobiopterin biosynthesis {ECO:0000256|ARBA:ARBA00023007};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 134..316
FT /note="Myosin tail"
FT /evidence="ECO:0000259|Pfam:PF01576"
FT REGION 282..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 322 AA; 37522 MW; 4937F6ED0F3434C8 CRC64;
MEKNNTQRSA ERVGYITRVE SLSACHRLHS KSLSDEENKR IFGKCNNPNG HGHNYKVEVT
VRGKIDQDTG MVMNLTDLKQ YIEEAIMKPL DHKNLDLDVP YFANVVSTTE NLAVYIWDSM
VKLLPPNMLY EIKEQESLQQ AEQRCVQLAQ ARRELEVQVA GLEERLEEEE GASAQLVSQR
QRLEAECCDL RRDLEELEST LTSVERDKQS SDCTVRKLSE ELSQKDVLVQ KFQKEKDHLF
ELSQQAIEDL QCEEEKVNLL TKEKAKLQVH VEELEYQLEQ ERKQRSELER NRRRLEGDSK
NTMENLTELG KMRASLEELI KK
//
