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Protein

6-pyruvoyl tetrahydrobiopterin synthase

Gene

Pts

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.

Catalytic activityi

7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231Zinc
Active sitei42 – 421Proton acceptor
Metal bindingi48 – 481Zinc
Metal bindingi50 – 501Zinc
Active sitei89 – 891Charge relay system
Active sitei133 – 1331Charge relay system

GO - Molecular functioni

  1. 6-pyruvoyltetrahydropterin synthase activity Source: RGD
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. tetrahydrobiopterin biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tetrahydrobiopterin biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.3.12. 5301.
ReactomeiREACT_310165. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
UniPathwayiUPA00849; UER00819.

Names & Taxonomyi

Protein namesi
Recommended name:
6-pyruvoyl tetrahydrobiopterin synthase (EC:4.2.3.12)
Short name:
PTP synthase
Short name:
PTPS
Gene namesi
Name:Pts
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi68367. Pts.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Deficiency leads to phenylketonuria.

Keywords - Diseasei

Phenylketonuria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 44PRO_0000029868
Chaini5 – 1441406-pyruvoyl tetrahydrobiopterin synthasePRO_0000029869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181PhosphoserineBy similarity
Modified residuei127 – 1271PhosphotyrosineBy similarity

Post-translational modificationi

Phosphorylation of Ser-18 is required for maximal enzyme activity.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP27213.
PRIDEiP27213.

PTM databases

PhosphoSiteiP27213.

Expressioni

Gene expression databases

GenevestigatoriP27213.

Interactioni

Subunit structurei

Homohexamer formed of two homotrimers in a head to head fashion.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012434.

Structurei

Secondary structure

1
144
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 2314Combined sources
Helixi32 – 398Combined sources
Helixi40 – 434Combined sources
Beta strandi48 – 6114Combined sources
Turni64 – 663Combined sources
Helixi72 – 8211Combined sources
Helixi84 – 874Combined sources
Helixi92 – 954Combined sources
Helixi97 – 993Combined sources
Beta strandi100 – 1023Combined sources
Helixi106 – 12015Combined sources
Turni123 – 1253Combined sources
Beta strandi126 – 1349Combined sources
Beta strandi137 – 1415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B66X-ray1.90A/B5-144[»]
1B6ZX-ray2.00A/B5-144[»]
1GTQX-ray2.30A/B5-144[»]
ProteinModelPortaliP27213.
SMRiP27213. Positions 8-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27213.

Family & Domainsi

Sequence similaritiesi

Belongs to the PTPS family.Curated

Phylogenomic databases

eggNOGiCOG0720.
GeneTreeiENSGT00390000002752.
HOGENOMiHOG000225069.
HOVERGENiHBG004358.
InParanoidiP27213.
KOiK01737.
OMAiCHRLHSK.
OrthoDBiEOG7NSB3V.
PhylomeDBiP27213.
TreeFamiTF105796.

Family and domain databases

InterProiIPR007115. 6-PTP_synth/QueD.
IPR022470. PTPS_Cys_AS.
IPR022469. PTPS_His_AS.
[Graphical view]
PANTHERiPTHR12589. PTHR12589. 1 hit.
PfamiPF01242. PTPS. 1 hit.
[Graphical view]
PIRSFiPIRSF006113. PTP_synth. 1 hit.
TIGRFAMsiTIGR00039. 6PTHBS. 1 hit.
PROSITEiPS00987. PTPS_1. 1 hit.
PS00988. PTPS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27213-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAAVGLRRR ARLSRLVSFS ASHRLHSPSL SAEENLKVFG KCNNPNGHGH
60 70 80 90 100
NYKVVVTIHG EIDPVTGMVM NLTDLKEYME EAIMKPLDHK NLDLDVPYFA
110 120 130 140
DVVSTTENVA VYIWENLQRL LPVGALYKVK VYETDNNIVV YKGE
Length:144
Mass (Da):16,241
Last modified:August 1, 1992 - v1
Checksum:i0657C78F87C6FC3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77850 mRNA. Translation: AAA40625.1.
BC059140 mRNA. Translation: AAH59140.1.
PIRiA39499.
RefSeqiNP_058916.1. NM_017220.1.
UniGeneiRn.87164.

Genome annotation databases

EnsembliENSRNOT00000012434; ENSRNOP00000012434; ENSRNOG00000009250.
GeneIDi29498.
KEGGirno:29498.
UCSCiRGD:68367. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77850 mRNA. Translation: AAA40625.1.
BC059140 mRNA. Translation: AAH59140.1.
PIRiA39499.
RefSeqiNP_058916.1. NM_017220.1.
UniGeneiRn.87164.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B66X-ray1.90A/B5-144[»]
1B6ZX-ray2.00A/B5-144[»]
1GTQX-ray2.30A/B5-144[»]
ProteinModelPortaliP27213.
SMRiP27213. Positions 8-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000012434.

PTM databases

PhosphoSiteiP27213.

Proteomic databases

PaxDbiP27213.
PRIDEiP27213.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000012434; ENSRNOP00000012434; ENSRNOG00000009250.
GeneIDi29498.
KEGGirno:29498.
UCSCiRGD:68367. rat.

Organism-specific databases

CTDi5805.
RGDi68367. Pts.

Phylogenomic databases

eggNOGiCOG0720.
GeneTreeiENSGT00390000002752.
HOGENOMiHOG000225069.
HOVERGENiHBG004358.
InParanoidiP27213.
KOiK01737.
OMAiCHRLHSK.
OrthoDBiEOG7NSB3V.
PhylomeDBiP27213.
TreeFamiTF105796.

Enzyme and pathway databases

UniPathwayiUPA00849; UER00819.
BRENDAi4.2.3.12. 5301.
ReactomeiREACT_310165. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.

Miscellaneous databases

EvolutionaryTraceiP27213.
NextBioi609392.
PROiP27213.

Gene expression databases

GenevestigatoriP27213.

Family and domain databases

InterProiIPR007115. 6-PTP_synth/QueD.
IPR022470. PTPS_Cys_AS.
IPR022469. PTPS_His_AS.
[Graphical view]
PANTHERiPTHR12589. PTHR12589. 1 hit.
PfamiPF01242. PTPS. 1 hit.
[Graphical view]
PIRSFiPIRSF006113. PTP_synth. 1 hit.
TIGRFAMsiTIGR00039. 6PTHBS. 1 hit.
PROSITEiPS00987. PTPS_1. 1 hit.
PS00988. PTPS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification and cDNA cloning of rat 6-pyruvoyl-tetrahydropterin synthase."
    Inoue Y., Kawasaki Y., Harada T., Hatakeyama K., Kagamiyama H.
    J. Biol. Chem. 266:20791-20796(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Wistar.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  3. "Three-dimensional structure of 6-pyruvoyl tetrahydropterin synthase, an enzyme involved in tetrahydrobiopterin biosynthesis."
    Nar H., Huber R., Heizmann C.W., Thoeny B., Buergisser D.
    EMBO J. 13:1255-1262(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  4. "Crystallographic and kinetic investigations on the mechanism of 6-pyruvoyl tetrahydropterin synthase."
    Ploom T., Thoeny B., Yim J., Lee S., Nar H., Leimbacher W., Richardson J., Huber R., Auerbach G.
    J. Mol. Biol. 286:851-860(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiPTPS_RAT
AccessioniPrimary (citable) accession number: P27213
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 1, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is at the interface between 2 subunits. The proton acceptor Cys is on one subunit, and the charge relay system is on the other subunit.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.