ID PTPS_RICFE Reviewed; 138 AA. AC Q4UKI6; DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 16-JUN-2009, entry version 26. DE RecName: Full=Putative 6-pyruvoyl tetrahydrobiopterin synthase; DE Short=PTP synthase; DE Short=PTPS; DE EC=4.2.3.12; GN OrderedLocusNames=RF_1094; OS Rickettsia felis (Rickettsia azadi). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=42862; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1525 / URRWXCal2; RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248; RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., RA Parinello H., Claverie J.-M., Raoult D.; RT "The genome sequence of Rickettsia felis identifies the first putative RT conjugative plasmid in an obligate intracellular parasite."; RL PLoS Biol. 3:1-12(2005). 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; CP000053; AAY61945.1; -; Genomic_DNA. DR RefSeq; YP_247110.1; -. DR GeneID; 3400204; -. DR GenomeReviews; CP000053_GR; RF_1094. DR KEGG; rfe:RF_1094; -. DR NMPDR; fig|315456.3.peg.1093; -. DR HOGENOM; Q4UKI6; -. DR OMA; Q4UKI6; GHKTVVL. DR BioCyc; RFEL315456:RF_1094-MON; -. DR BRENDA; 4.2.3.12; 297363. 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 1 138 Putative 6-pyruvoyl tetrahydrobiopterin FT synthase. FT /FTId=PRO_0000272631. FT ACT_SITE 23 23 Proton acceptor (By similarity). FT ACT_SITE 68 68 Charge relay system (By similarity). FT ACT_SITE 130 130 Charge relay system (By similarity). FT METAL 14 14 Zinc (By similarity). FT METAL 27 27 Zinc (By similarity). FT METAL 29 29 Zinc (By similarity). SQ SEQUENCE 138 AA; 16040 MW; BEBBC34B5943EE46 CRC64; MIKCTRRIEF DAGHRIIGHQ NKCQFLHGHR YVLEIAIAAN KTDKLGMVID FGLIKDVAKK WIDENFDHSL ILHQDDKEMG QQIENCTGQK IYYMQNNPTA ENIATHLKNE IFPKLFVGQN FFVSNLKLYE TPNCFVEV //