ID A0A0J6BM85_9SYNE Unreviewed; 315 AA.
AC A0A0J6BM85;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 08-NOV-2023, entry version 27.
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=SYNGFB01_01020 {ECO:0000313|EMBL:KMM17922.1};
OS Synechococcus sp. GFB01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1662190 {ECO:0000313|EMBL:KMM17922.1, ECO:0000313|Proteomes:UP000035901};
RN [1] {ECO:0000313|EMBL:KMM17922.1, ECO:0000313|Proteomes:UP000035901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GFB01 {ECO:0000313|EMBL:KMM17922.1,
RC ECO:0000313|Proteomes:UP000035901};
RA Guimaraes P.I., Leao T.F., de Melo A.G., Ramos R.T., Silva A., Fiore M.F.,
RA Schneider M.P.;
RT "Draft genome of the picocyanobacterium Synechococcus sp. strain GFB01
RT isolated from a freshwater lagoon of the Brazilian Amazon.";
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 -!- 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}.
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:KMM17922.1}.
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DR EMBL; LFEK01000006; KMM17922.1; -; Genomic_DNA.
DR RefSeq; WP_048016546.1; NZ_LFEK01000006.1.
DR AlphaFoldDB; A0A0J6BM85; -.
DR STRING; 1662190.SYNGFB01_01020; -.
DR PATRIC; fig|1662190.3.peg.2376; -.
DR OrthoDB; 9804698at2; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000035901; 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 PANTHER; PTHR12589:SF7; 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR PANTHER; PTHR12589; PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR Pfam; PF01242; PTPS; 2.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 2.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000035901};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 315 AA; 34369 MW; A9AA1C31F1749805 CRC64;
MSASAAAPHG KGRPCLITRR ATFSASHRYW LPEFSADDNR ARFGPCTLAP GHGHNYELLV
AMGGPLDGDG MVLNLSEVKH AIRAEVTDQL NFRHLNDVWP EFDLSRDEGC LPTTEALARA
IWVRLDPHLP LVGLRLHEQP DLWVDLLPPI PDSSARPAAP MEAFLSIRTH FAAAHRLARP
ELSQAENEAI YGKCARPHGH GHNYLLDVTV RGRIDPRTGM VCDLAALQQL VDDLVVEPFD
HTFLNKDVAH FATTVPTAEN IALHIADLLS GPIAATGARL HKVRLQESPN NAAEVFAETP
QLEMVPAALE ALAAG
//
