ID A0A0J7IPB2_9FLAO Unreviewed; 148 AA.
AC A0A0J7IPB2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=ACM39_10690 {ECO:0000313|EMBL:KMQ67807.1};
OS Chryseobacterium sp. FH2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1674291 {ECO:0000313|EMBL:KMQ67807.1, ECO:0000313|Proteomes:UP000036315};
RN [1] {ECO:0000313|EMBL:KMQ67807.1, ECO:0000313|Proteomes:UP000036315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH2 {ECO:0000313|EMBL:KMQ67807.1,
RC ECO:0000313|Proteomes:UP000036315};
RA Stropko S.J., Miller J.R., Newman J.D.;
RL Submitted (JUN-2015) 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 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:KMQ67807.1}.
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DR EMBL; LFNE01000006; KMQ67807.1; -; Genomic_DNA.
DR RefSeq; WP_048511040.1; NZ_LFNE01000006.1.
DR AlphaFoldDB; A0A0J7IPB2; -.
DR STRING; 1674291.ACM39_10690; -.
DR PATRIC; fig|1674291.3.peg.2221; -.
DR OrthoDB; 9804698at2; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000036315; 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 ACT_SITE 23
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT ACT_SITE 73
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT ACT_SITE 134
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 148 AA; 16833 MW; A5AC07AED38621F5 CRC64;
MIRITKIFTF ETAHVLYNYD GKCKNMHGHS YKLFVTVKGK PVNDLENPKN GMVVDFGDIK
SIVKSEIVDV WDHAVLINGL SPHKELGEGL ENQGHKVIYC NFQPTCENML YAIAAKIKSK
LPSEISLAYL KLHETENSYG EWFAEDNQ
//