ID   QUED_PYRAB              Reviewed;         157 AA.
AC   Q9UXZ4; G8ZK78;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=PYRAB17130; ORFNames=PAB1123;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248288; CAB50618.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE71185.1; -; Genomic_DNA.
DR   PIR; D75022; D75022.
DR   RefSeq; WP_010868831.1; NC_000868.1.
DR   AlphaFoldDB; Q9UXZ4; -.
DR   SMR; Q9UXZ4; -.
DR   STRING; 272844.PAB1123; -.
DR   EnsemblBacteria; CAB50618; CAB50618; PAB1123.
DR   GeneID; 1496014; -.
DR   KEGG; pab:PAB1123; -.
DR   PATRIC; fig|272844.11.peg.1830; -.
DR   eggNOG; arCOG02172; Archaea.
DR   HOGENOM; CLU_111016_3_0_2; -.
DR   OMA; WEDPRSY; -.
DR   OrthoDB; 104644at2157; -.
DR   PhylomeDB; Q9UXZ4; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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.
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_0000057933"
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;  18742 MW;  6EA2D11C6969531D CRC64;
     MKRVVSIKRR IYWTKEFDSS HFLELEYESK CRRLHGHTYR VEVEIEGEPN EHGMIFDFNH
     LSELIKTLDH KVIVSEKWVR YEEGYVLIEK NDKLLKLPRS EVVVIDKPNV TAEYIAEWIS
     ERILENAGEN VREIRVRVWE DPRSYAEITL TLKPQGS