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Entry: A0A1Y6FS18_9BACI
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ID   A0A1Y6FS18_9BACI        Unreviewed;       158 AA.
AC   A0A1Y6FS18;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=6-carboxy-5,6,7,8-tetrahydropterin synthase {ECO:0000256|ARBA:ARBA00018141};
DE            EC=4.1.2.50 {ECO:0000256|ARBA:ARBA00012982};
DE   AltName: Full=Queuosine biosynthesis protein QueD {ECO:0000256|ARBA:ARBA00031449};
GN   ORFNames=SAMN05444673_2914 {ECO:0000313|EMBL:SMQ77579.1};
OS   Bacillus sp. OV166.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1882763 {ECO:0000313|EMBL:SMQ77579.1, ECO:0000313|Proteomes:UP000194454};
RN   [1] {ECO:0000313|EMBL:SMQ77579.1, ECO:0000313|Proteomes:UP000194454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV166 {ECO:0000313|EMBL:SMQ77579.1};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005061}.
CC   -!- SIMILARITY: Belongs to the PTPS family. QueD subfamily.
CC       {ECO:0000256|ARBA:ARBA00008900}.
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DR   EMBL; FXWM01000001; SMQ77579.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6FS18; -.
DR   OrthoDB; 9804698at2; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000194454; Unassembled WGS sequence.
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; 6-pyruvoyl tetrahydropterin synthase/QueD; 2.
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   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   158 AA;  18887 MW;  AE20CF4CEA062A27 CRC64;
     MGFRIVDKLQ KINEDIQPHQ LKYHSKRVLV SKEFTFDASH HLHCYEGKCK NLHGHTYRVI
     FGLSGFVDER GLMIDFGDIK DIWKNEIEIY LDHQYLNETL PSMNTTAENM VVWIYEKMKD
     ALATEERRNQ YHGARVEFVR LFETPTSYAE ARREWMEE
//
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