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P27213 (PTPS_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-pyruvoyl tetrahydrobiopterin synthase

Short name=PTP synthase
Short name=PTPS
EC=4.2.3.12
Gene names
Name:Pts
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length144 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

Binds 1 zinc ion per subunit.

Pathway

Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.

Subunit structure

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

Post-translational modification

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

Involvement in disease

Deficiency leads to phenylketonuria.

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.

Sequence similarities

Belongs to the PTPS family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 44
PRO_0000029868
Chain5 – 1441406-pyruvoyl tetrahydrobiopterin synthase
PRO_0000029869

Sites

Active site421Proton acceptor
Active site891Charge relay system
Active site1331Charge relay system
Metal binding231Zinc
Metal binding481Zinc
Metal binding501Zinc

Amino acid modifications

Modified residue181Phosphoserine By similarity

Secondary structure

.......................... 144
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P27213 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 0657C78F87C6FC3B

FASTA14416,241
        10         20         30         40         50         60 
MNAAVGLRRR ARLSRLVSFS ASHRLHSPSL SAEENLKVFG KCNNPNGHGH NYKVVVTIHG 

        70         80         90        100        110        120 
EIDPVTGMVM NLTDLKEYME EAIMKPLDHK NLDLDVPYFA DVVSTTENVA VYIWENLQRL 

       130        140 
LPVGALYKVK VYETDNNIVV YKGE 

« Hide

References

« Hide 'large scale' references
[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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M77850 mRNA. Translation: AAA40625.1.
BC059140 mRNA. Translation: AAH59140.1.
PIRA39499.
RefSeqNP_058916.1. NM_017220.1.
UniGeneRn.87164.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B66X-ray1.90A/B5-144[»]
1B6ZX-ray2.00A/B5-144[»]
1GTQX-ray2.30A/B5-144[»]
ProteinModelPortalP27213.
SMRP27213. Positions 8-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000012434.

PTM databases

PhosphoSiteP27213.

Proteomic databases

PaxDbP27213.
PRIDEP27213.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000012434; ENSRNOP00000012434; ENSRNOG00000009250.
GeneID29498.
KEGGrno:29498.
UCSCRGD:68367. rat.

Organism-specific databases

CTD5805.
RGD68367. Pts.

Phylogenomic databases

eggNOGCOG0720.
GeneTreeENSGT00390000002752.
HOGENOMHOG000225069.
HOVERGENHBG004358.
InParanoidP27213.
KOK01737.
OMACIEEVIM.
OrthoDBEOG7NSB3V.
PhylomeDBP27213.
TreeFamTF105796.

Enzyme and pathway databases

BRENDA4.2.3.12. 5301.
UniPathwayUPA00849; UER00819.

Gene expression databases

GenevestigatorP27213.

Family and domain databases

InterProIPR007115. 6-PTP_synth/QueD.
IPR022470. PTPS_Cys_AS.
IPR022469. PTPS_His_AS.
[Graphical view]
PANTHERPTHR12589. PTHR12589. 1 hit.
PfamPF01242. PTPS. 1 hit.
[Graphical view]
PIRSFPIRSF006113. PTP_synth. 1 hit.
TIGRFAMsTIGR00039. 6PTHBS. 1 hit.
PROSITEPS00987. PTPS_1. 1 hit.
PS00988. PTPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP27213.
NextBio609392.
PROP27213.

Entry information

Entry namePTPS_RAT
AccessionPrimary (citable) accession number: P27213
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways