ID   QUED_PYRHO              Reviewed;         157 AA.
AC   O59602;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Putative 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=PH1939;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(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}.
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DR   EMBL; BA000001; BAA31066.1; -; Genomic_DNA.
DR   PIR; C71209; C71209.
DR   RefSeq; WP_010886005.1; NC_000961.1.
DR   AlphaFoldDB; O59602; -.
DR   SMR; O59602; -.
DR   STRING; 70601.3258383; -.
DR   EnsemblBacteria; BAA31066; BAA31066; BAA31066.
DR   GeneID; 1442787; -.
DR   KEGG; pho:PH1939; -.
DR   eggNOG; arCOG02172; Archaea.
DR   OMA; WEDPRSY; -.
DR   OrthoDB; 104644at2157; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000000752; 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   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.
DR   PIRSF; PIRSF006113; PTP_synth; 1.
PE   3: Inferred from homology;
KW   Lyase; Metal-binding; Zinc.
FT   CHAIN           1..157
FT                   /note="Putative 6-carboxy-5,6,7,8-tetrahydropterin
FT                   synthase"
FT                   /id="PRO_0000057934"
FT   ACT_SITE        31
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        70
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        140
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   157 AA;  18629 MW;  2BB47C4551E130C1 CRC64;
     MTMRYIIKRK IYWTKEFDSS HFLELEYESK CKRIHGHTYK VEVEIEGELN EEGMIFDFTH
     LSEIVKELDH RLIVSKEWVK EVGDLVIIEK NRKILKVPRD EVVIIDKPNV TAEYLAEWFG
     ERIAENAGSN IKKIKVRIWE DPRSYAEVTF TLEPQGS