ID   A5D2E2_PELTS            Unreviewed;       129 AA.
AC   A5D2E2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=6-carboxy-5,6,7,8-tetrahydropterin synthase {ECO:0000256|ARBA:ARBA00018141, ECO:0000256|PIRNR:PIRNR006113};
DE            EC=4.-.-.- {ECO:0000256|PIRNR:PIRNR006113};
GN   OrderedLocusNames=PTH_1403 {ECO:0000313|EMBL:BAF59584.1};
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF59584.1, ECO:0000313|Proteomes:UP000006556};
RN   [1] {ECO:0000313|Proteomes:UP000006556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT   evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7,8-dihydroneopterin 3'-triphosphate + H2O = 6-
CC         carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) +
CC         triphosphate; Xref=Rhea:RHEA:27966, ChEBI:CHEBI:15343,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18036,
CC         ChEBI:CHEBI:58462, ChEBI:CHEBI:61032; EC=4.1.2.50;
CC         Evidence={ECO:0000256|ARBA:ARBA00001293,
CC         ECO:0000256|PIRNR:PIRNR006113};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006113,
CC         ECO:0000256|PIRSR:PIRSR006113-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR006113,
CC       ECO:0000256|PIRSR:PIRSR006113-2};
CC   -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005061, ECO:0000256|PIRNR:PIRNR006113}.
CC   -!- SIMILARITY: Belongs to the PTPS family. QueD subfamily.
CC       {ECO:0000256|ARBA:ARBA00008900, ECO:0000256|PIRNR:PIRNR006113}.
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DR   EMBL; AP009389; BAF59584.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5D2E2; -.
DR   STRING; 370438.PTH_1403; -.
DR   KEGG; pth:PTH_1403; -.
DR   eggNOG; COG0720; Bacteria.
DR   HOGENOM; CLU_111016_6_3_9; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000006556; 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; 6-pyruvoyl tetrahydropterin synthase/QueD; 1.
DR   InterPro; IPR007115; 6-PTP_synth/QueD.
DR   InterPro; IPR038418; 6-PTP_synth/QueD_sf.
DR   NCBIfam; TIGR03367; queuosine_QueD; 1.
DR   PANTHER; PTHR12589:SF7; 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR   PANTHER; PTHR12589; PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR   Pfam; PF01242; PTPS; 1.
DR   PIRSF; PIRSF006113; PTP_synth; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR006113};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR006113};
KW   Queuosine biosynthesis {ECO:0000256|PIRNR:PIRNR006113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006556};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006113}.
FT   ACT_SITE        23
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT   ACT_SITE        67
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT   ACT_SITE        117
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
SQ   SEQUENCE   129 AA;  14400 MW;  165F53207F41DFAB CRC64;
     MYEIVVRTSF AAAHSIKGYD GPCSRMHGHT WLVEAVLRGG QLDQKGMLVD FKEVKNILRS
     AVGELDHQNL NEIKPFAGGS GDSPTAENIA RYLFCRIKPE IVKLERNIHL AMVRVWESDT
     AAASYLEVD
//