ID   QUED_HALS3              Reviewed;         150 AA.
AC   B0R9W7;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Probable 6-carboxy-5,6,7,8-tetrahydropterin synthase;
DE            Short=CPH4 synthase;
DE            EC=4.1.2.50;
DE   AltName: Full=Archaeosine biosynthesis protein QueD;
GN   Name=queD; OrderedLocusNames=OE_5198R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OG   Plasmid PHS3.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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}.
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DR   EMBL; AM774418; CAP15548.1; -; Genomic_DNA.
DR   RefSeq; WP_010904153.1; NC_010368.1.
DR   AlphaFoldDB; B0R9W7; -.
DR   SMR; B0R9W7; -.
DR   EnsemblBacteria; CAP15548; CAP15548; OE_5198R.
DR   GeneID; 5954770; -.
DR   GeneID; 62888208; -.
DR   KEGG; hsl:OE_5198R; -.
DR   HOGENOM; CLU_111016_1_1_2; -.
DR   OMA; EWDHRFL; -.
DR   PhylomeDB; B0R9W7; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000001321; Plasmid PHS3.
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   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; Plasmid; Zinc.
FT   CHAIN           1..150
FT                   /note="Probable 6-carboxy-5,6,7,8-tetrahydropterin
FT                   synthase"
FT                   /id="PRO_0000408953"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        42
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        81
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        141
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         33
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         48
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   150 AA;  16234 MW;  8296E831E8081214 CRC64;
     MRSAQSKRSQ STATGERTLH IGRDRPIRIS AGHRLQHHDG KCSRPHGHNY EISVEITGQL
     TDEGWVVDKG TVTAVVSDWD HRFLLEDGDP LVDAFREAGD GDAVVVLEQP PTAEVMGVVL
     ERKLHDALPE TVSAVSVTVA ETPALTAGPN