6-pyruvoyl tetrahydrobiopterin synthase precursor

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P27213 (PTPS_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
6-pyruvoyl tetrahydrobiopterin synthase
Short name=PTP synthase
Short name=PTPS
EC=4.2.3.12

Gene names

Name:

Pts

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	144 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Tetrahydrobiopterin biosynthesis
Disease	Phenylketonuria
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	tetrahydrobiopterin biosynthetic process Traceable author statement Ref.1. Source: RGD
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	6-pyruvoyltetrahydropterin synthase activity Inferred from direct assay Ref.1. Source: RGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 4

PRO_0000029868

Chain

5 – 144

140

6-pyruvoyl tetrahydrobiopterin synthase

PRO_0000029869

Sites

Active site

Proton acceptor

Active site

Charge relay system

Active site

133

Charge relay system

Metal binding

Zinc

Metal binding

Zinc

Metal binding

Zinc

Amino acid modifications

Modified residue

Phosphoserine By similarity

Secondary structure

144

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P27213 [UniParc].

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

FASTA

144

16,241

        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' referencesShow '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.

IPI

IPI00195017.

PIR

A39499.

RefSeq

NP_058916.1. NM_017220.1.

UniGene

Rn.87164.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P27213.

SMR

P27213. Positions 8-144.

ModBase

Search...

Protein-protein interaction databases

STRING

10116.ENSRNOP00000012434.

PTM databases

PhosphoSite

P27213.

Proteomic databases

PaxDb

P27213.

PRIDE

P27213.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000012434; ENSRNOP00000012434; ENSRNOG00000009250.

GeneID

29498.

KEGG

rno:29498.

UCSC

RGD:68367. rat.

Organism-specific databases

CTD

5805.

RGD

68367. Pts.

Phylogenomic databases

eggNOG

COG0720.

GeneTree

ENSGT00390000002752.

HOGENOM

HOG000225069.

HOVERGEN

HBG004358.

InParanoid

P27213.

K01737.

OMA

EVKIHET.

OrthoDB

EOG4V1722.

Enzyme and pathway databases

BRENDA

4.2.3.12. 5301.

UniPathway

UPA00849; UER00819.

Gene expression databases

Genevestigator

P27213.

GermOnline

ENSRNOG00000009250. Rattus norvegicus.

Family and domain databases

InterPro

IPR007115. 6-PTP_synth/QueD.
IPR022470. PTPS_Cys_AS.
IPR022469. PTPS_His_AS.
[Graphical view]

PANTHER

PTHR12589. PTHR12589. 1 hit.

Pfam

PF01242. PTPS. 1 hit.
[Graphical view]

PIRSF

PIRSF006113. PTP_synth. 1 hit.

TIGRFAMs

TIGR00039. 6PTHBS. 1 hit.

PROSITE

PS00987. PTPS_1. 1 hit.
PS00988. PTPS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P27213.

NextBio

609392.

Entry information

Entry name

PTPS_RAT

Accession

Primary (citable) accession number: P27213

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	April 3, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents