ID A0A1I1NSW4_9FLAO Unreviewed; 151 AA.
AC A0A1I1NSW4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN04487987_102361 {ECO:0000313|EMBL:SFC97863.1};
OS Algibacter pectinivorans.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Algibacter.
OX NCBI_TaxID=870482 {ECO:0000313|EMBL:SFC97863.1, ECO:0000313|Proteomes:UP000199439};
RN [1] {ECO:0000313|Proteomes:UP000199439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25730 {ECO:0000313|Proteomes:UP000199439};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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|PIRSR:PIRSR006113-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006113-2};
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; FOMI01000002; SFC97863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1NSW4; -.
DR STRING; 870482.SAMN04487987_102361; -.
DR OrthoDB; 9804698at2; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000199439; 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; 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; 2.
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 ECO:0000256|PIRSR:PIRSR006113-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000199439};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR006113-2}.
FT ACT_SITE 26
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT ACT_SITE 76
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT BINDING 30
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"
SQ SEQUENCE 151 AA; 17283 MW; 60DCA2C6FFDD1839 CRC64;
MANNIRITKQ FSFETGHALY GYDGKCKNVH GHSYKLSVTV IGQPITDTNN VKYGMVIDFG
DLKKIVKEEI VNVFDHATVF NKNTPHVELA KELQDRGHNV LLVDYQPTSE MMVLDFAKKI
GKRLPGHIKL HSLKLQETDT SFAQWYQYDN I
//
