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Q9R1Z7

- PTPS_MOUSE

UniProt

Q9R1Z7 - PTPS_MOUSE

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Protein

6-pyruvoyl tetrahydrobiopterin synthase

Gene

Pts

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Pathwayi

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

  1. 6-pyruvoyltetrahydropterin synthase activity Source: MGI
  2. identical protein binding Source: MGI
  3. metal ion binding Source: UniProtKB-KW
  4. protein homodimerization activity Source: MGI

GO - Biological processi

  1. 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_199047. 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: Chromosome 9

Organism-specific databases

MGIiMGI:1338783. Pts.

Subcellular locationi

GO - Cellular componenti

  1. 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

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.
GenevestigatoriQ9R1Z7.

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 .
CCDSi CCDS23164.1.
RefSeqi NP_035350.1. NM_011220.2.
UniGenei Mm.35856.

3D structure databases

ProteinModelPortali Q9R1Z7.
SMRi Q9R1Z7. Positions 17-144.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9R1Z7. 5 interactions.
MINTi MINT-217930.
STRINGi 10090.ENSMUSP00000034570.

PTM databases

PhosphoSitei Q9R1Z7.

Proteomic databases

MaxQBi Q9R1Z7.
PaxDbi Q9R1Z7.
PRIDEi Q9R1Z7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034570 ; ENSMUSP00000034570 ; ENSMUSG00000032067 .
GeneIDi 19286.
KEGGi mmu:19286.
UCSCi uc009pjp.1. mouse.

Organism-specific databases

CTDi 5805.
MGIi MGI:1338783. Pts.

Phylogenomic databases

eggNOGi COG0720.
GeneTreei ENSGT00390000002752.
HOGENOMi HOG000225069.
HOVERGENi HBG004358.
InParanoidi Q9R1Z7.
KOi K01737.
OMAi CHRLHSK.
OrthoDBi EOG7NSB3V.
PhylomeDBi Q9R1Z7.
TreeFami TF105796.

Enzyme and pathway databases

UniPathwayi UPA00849 ; UER00819 .
Reactomei REACT_199047. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.

Miscellaneous databases

ChiTaRSi Pts. mouse.
NextBioi 296210.
PROi Q9R1Z7.
SOURCEi Search...

Gene expression databases

Bgeei Q9R1Z7.
CleanExi MM_PTS.
Genevestigatori Q9R1Z7.

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. "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: November 26, 2014
This is version 116 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