ID PTPS_DICDI Reviewed; 135 AA. AC Q1ZXI0; DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=6-pyruvoyl tetrahydrobiopterin synthase; DE Short=PTP synthase; DE Short=PTPS; DE EC=4.2.3.12; GN Name=ptsA; ORFNames=DDB_G0279095; OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., RA Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., RA Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). CC -!- FUNCTION: Involved in the biosynthesis of tetrahydrobiopterin, an CC essential cofactor of aromatic amino acid hydroxylases. Catalyzes CC the transformation of 7,8-dihydroneopterin triphosphate into 6- CC pyruvoyl tetrahydropterin (By similarity). CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin 3'-triphosphate = 6- CC pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis; CC tetrahydrobiopterin from 2-amino-4-hydroxy-6-(erythro-1,2,3- CC trihydroxypropyl)-dihydropteridine triphosphate: step 1/3. CC -!- SUBUNIT: Homohexamer formed of two homotrimers in a head to head CC fashion (By similarity). CC -!- MISCELLANEOUS: The active site is at the interface between 2 CC subunits. The proton acceptor Cys is on one subunit, and the CC charge relay system is on the other subunit. CC -!- SIMILARITY: Belongs to the PTPS family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AAFI02000027; EAS66886.1; -; Genomic_DNA. DR RefSeq; XP_001134570.1; -. DR GeneID; 4238116; -. DR KEGG; ddi:DDB_0232952; -. DR dictyBase; DDB_G0279095; ptsA. DR BRENDA; 4.2.3.12; 424. DR GO; GO:0003874; F:6-pyruvoyltetrahydropterin synthase activity; IEA:EC. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR007115; 6-PTP_synth-rel. DR PANTHER; PTHR12589; 6_PTP_synth; 1. DR Pfam; PF01242; PTPS; 1. DR ProDom; PD004049; PTPS_hypoth; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Metal-binding; KW Tetrahydrobiopterin biosynthesis; Zinc. FT CHAIN 1 135 6-pyruvoyl tetrahydrobiopterin synthase. FT /FTId=PRO_0000327514. FT ACT_SITE 36 36 Proton acceptor (By similarity). FT ACT_SITE 81 81 Charge relay system (By similarity). FT ACT_SITE 124 124 Charge relay system (By similarity). FT METAL 17 17 Zinc (By similarity). FT METAL 40 40 Zinc (By similarity). FT METAL 42 42 Zinc (By similarity). SQ SEQUENCE 135 AA; 15771 MW; 75B75E9AE96F525D CRC64; MSRTVILTRR EVFSSSHRLY SDKLSLEENK KIYGKCINSH GHNYVLEVSI KGAVKEDIGM FMNITELKEI LKEKVMDKLD HKNLENDVPE LKGIVTTTEN LSIFIWDQLF PSLKDFLYEV KILETENNFV VYRGE //