ID   QUED_ARCFU              Reviewed;         115 AA.
AC   O29809;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=AF_0440;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB90801.1; -; Genomic_DNA.
DR   PIR; H69304; H69304.
DR   RefSeq; WP_010877947.1; NC_000917.1.
DR   AlphaFoldDB; O29809; -.
DR   SMR; O29809; -.
DR   STRING; 224325.AF_0440; -.
DR   EnsemblBacteria; AAB90801; AAB90801; AF_0440.
DR   GeneID; 24793977; -.
DR   KEGG; afu:AF_0440; -.
DR   eggNOG; arCOG02172; Archaea.
DR   HOGENOM; CLU_111016_6_1_2; -.
DR   OMA; KCEKLHG; -.
DR   OrthoDB; 104644at2157; -.
DR   PhylomeDB; O29809; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000002199; 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.
DR   TIGRFAMs; TIGR03367; queuosine_QueD; 1.
PE   3: Inferred from homology;
KW   Lyase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..115
FT                   /note="Putative 6-carboxy-5,6,7,8-tetrahydropterin
FT                   synthase"
FT                   /id="PRO_0000057930"
FT   ACT_SITE        25
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        68
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        105
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   115 AA;  13150 MW;  22A7D623D7DAFEFC CRC64;
     MEEEMIIGIS TSFSAAHSIP GHKKCGKVHG HNFKVEVEIS GKVKENGMVM DFFDLKRIVN
     EVVAKFDHTL LNEQIEIPTS ENICLRIFSE LAEKGLNVRR VRVAENEDKW AEIRR