PTPS_SALSA
ID PTPS_SALSA Reviewed; 103 AA.
AC P80081;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=6-pyruvoyl tetrahydrobiopterin synthase;
DE Short=PTP synthase;
DE Short=PTPS;
DE EC=4.2.3.12;
DE Flags: Fragments;
GN Name=pts;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RC TISSUE=Liver;
RX PubMed=1734893; DOI=10.1016/0006-291x(92)91824-a;
RA Hauer C.R., Leimbacher W., Hunziker P., Neuheiser F., Blau N.,
RA Heizmann C.W.;
RT "6-pyruvoyl tetrahydropterin synthase from salmon liver: amino acid
RT sequence analysis by tandem mass spectrometry.";
RL Biochem. Biophys. Res. Commun. 182:953-959(1992).
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.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-
CC tetrahydropterin + H(+) + triphosphate; Xref=Rhea:RHEA:22048,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:58462,
CC ChEBI:CHEBI:136564; EC=4.2.3.12;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis;
CC tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
CC -!- SUBUNIT: Homohexamer formed of two homotrimers in a head to head
CC fashion. {ECO:0000250}.
CC -!- MISCELLANEOUS: Two isoforms of this protein have been found.
CC -!- MISCELLANEOUS: The active site is at the interface between 2 subunits.
CC The proton acceptor Cys is on one subunit, and the charge relay system
CC is on the other subunit.
CC -!- SIMILARITY: Belongs to the PTPS family. {ECO:0000305}.
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DR iPTMnet; P80081; -.
DR UniPathway; UPA00849; UER00819.
DR Proteomes; UP000087266; Genome assembly.
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 Gene3D; 3.30.479.10; -; 1.
DR InterPro; IPR007115; 6-PTP_synth/QueD.
DR InterPro; IPR038418; 6-PTP_synth/QueD_sf.
DR InterPro; IPR022469; PTPS_His_AS.
DR PANTHER; PTHR12589; PTHR12589; 1.
DR Pfam; PF01242; PTPS; 1.
DR PROSITE; PS00988; PTPS_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Lyase; Metal-binding;
KW Reference proteome; Tetrahydrobiopterin biosynthesis; Zinc.
FT CHAIN 1..103
FT /note="6-pyruvoyl tetrahydrobiopterin synthase"
FT /id="PRO_0000057917"
FT ACT_SITE 53
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10124"
FT ACT_SITE 92
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10124"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10123"
FT MOD_RES 1
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:1734893"
FT VARIANT 5..6
FT /note="AT -> DV"
FT UNSURE 38
FT /note="I or V"
FT UNSURE 41
FT /note="I or V"
FT UNSURE 45
FT /note="I or V"
FT NON_CONS 34..35
FT /evidence="ECO:0000305"
FT NON_CONS 49..50
FT /evidence="ECO:0000305"
FT NON_CONS 66..67
FT /evidence="ECO:0000305"
SQ SEQUENCE 103 AA; 11729 MW; 7E2D1094A5447D98 CRC64;
AQADATANEV AERIGYITRV QSFCASHRLH SPTLVMNITN IKEHIEEVIP LDHKNLDKDV
PYFANVNVAV YIXDNMVKQL PANLLYEVKI HETDKNIVVY RGE
