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P27213

- PTPS_RAT

UniProt

P27213 - PTPS_RAT

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Protein
6-pyruvoyl tetrahydrobiopterin synthase
Gene
Pts
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

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
Complete GO annotation...

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_199128. 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: 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 – 44
PRO_0000029868
Chaini5 – 1441406-pyruvoyl tetrahydrobiopterin synthase
PRO_0000029869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Phosphoserine By 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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP27213.

Family & Domainsi

Sequence similaritiesi

Belongs to the PTPS family.

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

MNAAVGLRRR ARLSRLVSFS ASHRLHSPSL SAEENLKVFG KCNNPNGHGH    50
NYKVVVTIHG EIDPVTGMVM NLTDLKEYME EAIMKPLDHK NLDLDVPYFA 100
DVVSTTENVA VYIWENLQRL LPVGALYKVK VYETDNNIVV YKGE 144
Length:144
Mass (Da):16,241
Last modified:August 1, 1992 - v1
Checksum:i0657C78F87C6FC3B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
M77850 mRNA. Translation: AAA40625.1 .
BC059140 mRNA. Translation: AAH59140.1 .
PIRi A39499.
RefSeqi NP_058916.1. NM_017220.1.
UniGenei Rn.87164.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B66 X-ray 1.90 A/B 5-144 [» ]
1B6Z X-ray 2.00 A/B 5-144 [» ]
1GTQ X-ray 2.30 A/B 5-144 [» ]
ProteinModelPortali P27213.
SMRi P27213. Positions 8-144.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000012434.

PTM databases

PhosphoSitei P27213.

Proteomic databases

PaxDbi P27213.
PRIDEi P27213.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000012434 ; ENSRNOP00000012434 ; ENSRNOG00000009250 .
GeneIDi 29498.
KEGGi rno:29498.
UCSCi RGD:68367. rat.

Organism-specific databases

CTDi 5805.
RGDi 68367. Pts.

Phylogenomic databases

eggNOGi COG0720.
GeneTreei ENSGT00390000002752.
HOGENOMi HOG000225069.
HOVERGENi HBG004358.
InParanoidi P27213.
KOi K01737.
OMAi CHRLHSK.
OrthoDBi EOG7NSB3V.
PhylomeDBi P27213.
TreeFami TF105796.

Enzyme and pathway databases

UniPathwayi UPA00849 ; UER00819 .
BRENDAi 4.2.3.12. 5301.
Reactomei REACT_199128. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.

Miscellaneous databases

EvolutionaryTracei P27213.
NextBioi 609392.
PROi P27213.

Gene expression databases

Genevestigatori P27213.

Family and domain databases

InterProi IPR007115. 6-PTP_synth/QueD.
IPR022470. PTPS_Cys_AS.
IPR022469. PTPS_His_AS.
[Graphical view ]
PANTHERi PTHR12589. PTHR12589. 1 hit.
Pfami PF01242. PTPS. 1 hit.
[Graphical view ]
PIRSFi PIRSF006113. PTP_synth. 1 hit.
TIGRFAMsi TIGR00039. 6PTHBS. 1 hit.
PROSITEi PS00987. PTPS_1. 1 hit.
PS00988. PTPS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 125 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

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