Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9R1Z7 (PTPS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length144 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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 By similarity.

Post-translational modification

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

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

Chain1 – 1441446-pyruvoyl tetrahydrobiopterin synthase
PRO_0000057915

Sites

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

Amino acid modifications

Modified residue181Phosphoserine By similarity

Experimental info

Sequence conflict61D → G in AAD15827. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9R1Z7 [UniParc].

Last modified November 1, 2002. Version 2.
Checksum: AAB034E27ED7A9E3

FASTA14416,188
        10         20         30         40         50         60 
MSAAGDLRRR ARLSRLVSFS ASHRLHSPSL SDEENLRVFG KCNNPNGHGH NYKVVVTVHG 

        70         80         90        100        110        120 
EIDPVTGMVM NLTDLKEYME EAIMKPLDHK NLDLDVPYFA DAVSTTENVA VYIWESLQKL 

       130        140 
LPVGALYKVK VFETDNNIVV YKGE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS23164.1.
RefSeqNP_035350.1. NM_011220.2.
UniGeneMm.35856.

3D structure databases

ProteinModelPortalQ9R1Z7.
SMRQ9R1Z7. Positions 17-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9R1Z7. 5 interactions.
MINTMINT-217930.
STRING10090.ENSMUSP00000034570.

PTM databases

PhosphoSiteQ9R1Z7.

Proteomic databases

MaxQBQ9R1Z7.
PaxDbQ9R1Z7.
PRIDEQ9R1Z7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034570; ENSMUSP00000034570; ENSMUSG00000032067.
GeneID19286.
KEGGmmu:19286.
UCSCuc009pjp.1. mouse.

Organism-specific databases

CTD5805.
MGIMGI:1338783. Pts.

Phylogenomic databases

eggNOGCOG0720.
GeneTreeENSGT00390000002752.
HOGENOMHOG000225069.
HOVERGENHBG004358.
InParanoidQ9R1Z7.
KOK01737.
OMACHRLHSK.
OrthoDBEOG7NSB3V.
PhylomeDBQ9R1Z7.
TreeFamTF105796.

Enzyme and pathway databases

UniPathwayUPA00849; UER00819.

Gene expression databases

BgeeQ9R1Z7.
CleanExMM_PTS.
GenevestigatorQ9R1Z7.

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

ChiTaRSPTS. mouse.
NextBio296210.
PROQ9R1Z7.
SOURCESearch...

Entry information

Entry namePTPS_MOUSE
AccessionPrimary (citable) accession number: Q9R1Z7
Secondary accession number(s): Q3UIB6, Q9Z2N2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: November 1, 2002
Last modified: July 9, 2014
This is version 112 of the entry and version 2 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot