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Database: UniProt
Entry: A0A0Q6TM97_9CAUL
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Original site: A0A0Q6TM97_9CAUL 
ID   A0A0Q6TM97_9CAUL        Unreviewed;       121 AA.
AC   A0A0Q6TM97;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ORFNames=ASC62_22560 {ECO:0000313|EMBL:KQV54869.1};
OS   Caulobacter sp. Root342.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=1736519 {ECO:0000313|EMBL:KQV54869.1, ECO:0000313|Proteomes:UP000051656};
RN   [1] {ECO:0000313|EMBL:KQV54869.1, ECO:0000313|Proteomes:UP000051656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root342 {ECO:0000313|EMBL:KQV54869.1,
RC   ECO:0000313|Proteomes:UP000051656};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQV54869.1, ECO:0000313|Proteomes:UP000051656}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root342 {ECO:0000313|EMBL:KQV54869.1,
RC   ECO:0000313|Proteomes:UP000051656};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00002285}.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQV54869.1}.
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DR   EMBL; LMDD01000012; KQV54869.1; -; Genomic_DNA.
DR   RefSeq; WP_056048690.1; NZ_LMDD01000012.1.
DR   AlphaFoldDB; A0A0Q6TM97; -.
DR   STRING; 1736519.ASC62_22560; -.
DR   OrthoDB; 9804698at2; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000051656; 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   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   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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006113}.
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT   BINDING         32
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT   BINDING         34
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
SQ   SEQUENCE   121 AA;  13380 MW;  3A8DC7689F422129 CRC64;
     MKPVFEITKA AHFDAAHYIE QGPADHRYRK LHGHSFKVEA SVKGQMQDAG WVADLDGLDA
     ALKAVAIELD HGLLNDRPGL ETPTLERLCL YFAERLKVQF PGLSRVVLSR PTIGESCALT
     L
//
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