ID QUED_RICPR Reviewed; 138 AA. AC Q9ZDY5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 16-OCT-2013, entry version 76. DE RecName: Full=6-carboxy-5,6,7,8-tetrahydropterin synthase; DE Short=CPH4 synthase; DE EC=4.1.2.50; DE AltName: Full=Queuosine biosynthesis protein QueD; GN Name=queD; OrderedLocusNames=RP178; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., RA Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., RA Eriksson A.-S., Winkler H.H., Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin CC triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) CC and acetaldehyde (By similarity). CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin 3'-triphosphate + H(2)O = CC 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. 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 (By similarity). CC -!- SIMILARITY: Belongs to the PTPS family. QueD subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ235270; CAA14645.1; -; Genomic_DNA. DR PIR; F71728; F71728. DR RefSeq; NP_220568.1; NC_000963.1. DR ProteinModelPortal; Q9ZDY5; -. DR STRING; 272947.RP178; -. DR EnsemblBacteria; CAA14645; CAA14645; CAA14645. DR GeneID; 883870; -. DR KEGG; rpr:RP178; -. DR PATRIC; 17901106; VBIRicPro72556_0183. DR eggNOG; COG0720; -. DR HOGENOM; HOG000225068; -. DR KO; K01737; -. DR OMA; TPNCWAE; -. DR ProtClustDB; CLSK870781; -. DR UniPathway; UPA00391; -. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR007115; 6-PTP_synth/QueD. DR PANTHER; PTHR12589; PTHR12589; 1. DR Pfam; PF01242; PTPS; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Metal-binding; Queuosine biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 138 6-carboxy-5,6,7,8-tetrahydropterin FT synthase. FT /FTId=PRO_0000057928. 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; 16227 MW; 014B19A34593B968 CRC64; MIKCTRRINF DAGHRIIGHK NKCQFLHGHH YVLEITIAAN KTDTLGMVID FGLIKNLAKK WIDANFDHNL ILHQDDKEMG QQIENYTRQK IYYMRNNPTA ENIATHLKNE IFPKLFVSQN FFVTSLKLYE TQNCFVEV //