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 02-DEC-2020, entry version 96. 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., Sicheritz-Ponten T., RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., RA 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 triphosphate CC (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy- CC 5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate; CC Xref=Rhea:RHEA:27966, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:58462, CC ChEBI:CHEBI:61032; EC=4.1.2.50; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC -!- MISCELLANEOUS: The active site is at the interface between 2 subunits. CC The proton acceptor Cys is on one subunit, and the charge relay system CC is on the other subunit (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PTPS family. QueD subfamily. {ECO:0000305}. 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 RefSeq; WP_004595914.1; NC_000963.1. DR STRING; 272947.RP178; -. DR EnsemblBacteria; CAA14645; CAA14645; CAA14645. DR GeneID; 45168438; -. DR KEGG; rpr:RP178; -. DR PATRIC; fig|272947.5.peg.183; -. DR eggNOG; COG0720; Bacteria. DR HOGENOM; CLU_111016_1_1_5; -. DR OMA; VHGHSYK; -. DR BioCyc; RPRO272947:G1GT0-181-MONOMER; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000002480; Chromosome. DR GO; GO:0070497; F:6-carboxy-5,6,7,8-tetrahydropterin synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.30.479.10; -; 1. DR InterPro; IPR007115; 6-PTP_synth/QueD. DR InterPro; IPR038418; 6-PTP_synth/QueD_sf. DR PANTHER; PTHR12589; PTHR12589; 1. DR Pfam; PF01242; PTPS; 1. PE 3: Inferred from homology; KW Lyase; Metal-binding; Queuosine biosynthesis; Reference proteome; Zinc. FT CHAIN 1..138 FT /note="6-carboxy-5,6,7,8-tetrahydropterin synthase" FT /id="PRO_0000057928" FT ACT_SITE 23 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 68 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 130 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT METAL 14 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 27 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 29 FT /note="Zinc" FT /evidence="ECO:0000250" SQ SEQUENCE 138 AA; 16227 MW; 014B19A34593B968 CRC64; MIKCTRRINF DAGHRIIGHK NKCQFLHGHH YVLEITIAAN KTDTLGMVID FGLIKNLAKK WIDANFDHNL ILHQDDKEMG QQIENYTRQK IYYMRNNPTA ENIATHLKNE IFPKLFVSQN FFVTSLKLYE TQNCFVEV //