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Protein

6-pyruvoyl tetrahydrobiopterin synthase

Gene

Pts

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathway:itetrahydrobiopterin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. 6-pyruvoyl tetrahydrobiopterin synthase (Pts)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
This subpathway is part of the pathway tetrahydrobiopterin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate, the pathway tetrahydrobiopterin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231ZincPROSITE-ProRule annotation
Active sitei42 – 421Proton acceptorPROSITE-ProRule annotation
Metal bindingi48 – 481ZincPROSITE-ProRule annotation
Metal bindingi50 – 501ZincPROSITE-ProRule annotation
Active sitei89 – 891Charge relay systemPROSITE-ProRule annotation
Active sitei133 – 1331Charge relay systemPROSITE-ProRule annotation

GO - Molecular functioni

  • 6-pyruvoyltetrahydropterin synthase activity Source: MGI
  • identical protein binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: MGI

GO - Biological processi

  • tetrahydrobiopterin biosynthetic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tetrahydrobiopterin biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_273079. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1338783. Pts.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 1441446-pyruvoyl tetrahydrobiopterin synthasePRO_0000057915Add
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

MaxQBiQ9R1Z7.
PaxDbiQ9R1Z7.
PRIDEiQ9R1Z7.

PTM databases

PhosphoSiteiQ9R1Z7.

Expressioni

Gene expression databases

BgeeiQ9R1Z7.
CleanExiMM_PTS.
GenevisibleiQ9R1Z7. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ9R1Z7. 5 interactions.
MINTiMINT-217930.
STRINGi10090.ENSMUSP00000034570.

Structurei

3D structure databases

ProteinModelPortaliQ9R1Z7.
SMRiQ9R1Z7. Positions 17-144.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PTPS family.Curated

Phylogenomic databases

eggNOGiCOG0720.
GeneTreeiENSGT00390000002752.
HOGENOMiHOG000225069.
HOVERGENiHBG004358.
InParanoidiQ9R1Z7.
KOiK01737.
OMAiCHRLHSK.
OrthoDBiEOG7NSB3V.
PhylomeDBiQ9R1Z7.
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.

Q9R1Z7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAAGDLRRR ARLSRLVSFS ASHRLHSPSL SDEENLRVFG KCNNPNGHGH
60 70 80 90 100
NYKVVVTVHG EIDPVTGMVM NLTDLKEYME EAIMKPLDHK NLDLDVPYFA
110 120 130 140
DAVSTTENVA VYIWESLQKL LPVGALYKVK VFETDNNIVV YKGE
Length:144
Mass (Da):16,188
Last modified:November 1, 2002 - v2
Checksum:iAAB034E27ED7A9E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61D → G in AAD15827 (PubMed:9894812).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061880, AF061878, AF061879 Genomic DNA. Translation: AAD15827.1.
AF043225 mRNA. Translation: AAD02249.1.
AK002614 mRNA. Translation: BAB22231.1.
AK146987 mRNA. Translation: BAE27590.1.
BC029013 mRNA. Translation: AAH29013.1.
CCDSiCCDS23164.1.
RefSeqiNP_035350.1. NM_011220.2.
UniGeneiMm.35856.

Genome annotation databases

EnsembliENSMUST00000034570; ENSMUSP00000034570; ENSMUSG00000032067.
GeneIDi19286.
KEGGimmu:19286.
UCSCiuc009pjp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061880, AF061878, AF061879 Genomic DNA. Translation: AAD15827.1.
AF043225 mRNA. Translation: AAD02249.1.
AK002614 mRNA. Translation: BAB22231.1.
AK146987 mRNA. Translation: BAE27590.1.
BC029013 mRNA. Translation: AAH29013.1.
CCDSiCCDS23164.1.
RefSeqiNP_035350.1. NM_011220.2.
UniGeneiMm.35856.

3D structure databases

ProteinModelPortaliQ9R1Z7.
SMRiQ9R1Z7. Positions 17-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9R1Z7. 5 interactions.
MINTiMINT-217930.
STRINGi10090.ENSMUSP00000034570.

PTM databases

PhosphoSiteiQ9R1Z7.

Proteomic databases

MaxQBiQ9R1Z7.
PaxDbiQ9R1Z7.
PRIDEiQ9R1Z7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034570; ENSMUSP00000034570; ENSMUSG00000032067.
GeneIDi19286.
KEGGimmu:19286.
UCSCiuc009pjp.1. mouse.

Organism-specific databases

CTDi5805.
MGIiMGI:1338783. Pts.

Phylogenomic databases

eggNOGiCOG0720.
GeneTreeiENSGT00390000002752.
HOGENOMiHOG000225069.
HOVERGENiHBG004358.
InParanoidiQ9R1Z7.
KOiK01737.
OMAiCHRLHSK.
OrthoDBiEOG7NSB3V.
PhylomeDBiQ9R1Z7.
TreeFamiTF105796.

Enzyme and pathway databases

UniPathwayiUPA00849; UER00819.
ReactomeiREACT_273079. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.

Miscellaneous databases

ChiTaRSiPts. mouse.
NextBioi296210.
PROiQ9R1Z7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R1Z7.
CleanExiMM_PTS.
GenevisibleiQ9R1Z7. MM.

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. "Structure, genomic localization and recombinant expression of the mouse 6-pyruvoyl-tetrahydropterin synthase gene."
    Turri M.O., Ilg E.C., Thony B., Blau N.
    Biol. Chem. 379:1441-1447(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Ola.
  2. Thony B., Turri M., Blau N.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6J.
    Tissue: Placenta.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney and Stomach.
  4. "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: Retina.

Entry informationi

Entry nameiPTPS_MOUSE
AccessioniPrimary (citable) accession number: Q9R1Z7
Secondary accession number(s): Q3UIB6, Q9Z2N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 2002
Last modified: June 24, 2015
This is version 121 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.