ID A0A1B7VVI5_APHFL Unreviewed; 404 AA.
AC A0A1B7VVI5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=AN481_12620 {ECO:0000313|EMBL:OBQ24972.1};
OS Aphanizomenon flos-aquae LD13.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Aphanizomenon.
OX NCBI_TaxID=1710894 {ECO:0000313|EMBL:OBQ24972.1, ECO:0000313|Proteomes:UP000092382};
RN [1] {ECO:0000313|EMBL:OBQ24972.1, ECO:0000313|Proteomes:UP000092382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDT13 {ECO:0000313|EMBL:OBQ24972.1};
RA Driscoll C.;
RT "Whole genome shotgun sequence assembly of Aphanizomenon flos-aquae
RT UKL13.";
RL Submitted (SEP-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:OBQ24972.1}.
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DR EMBL; LJOY01000040; OBQ24972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7VVI5; -.
DR STRING; 1803587.GCA_001593825_03299; -.
DR PATRIC; fig|1710894.3.peg.285; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000092382; 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; 3.
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; 3.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 3.
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 404 AA; 45873 MW; 9378002DA1CDB7E4 CRC64;
MQCIVNRRDQ FSAISRYWLP ELSEIENLQK FGAYSKFPGH GHNYVLFISM LGEIDEYGMV
LNLSDVKHVI KREITGQLDF SYLNDVWTEF QPTLPSTENI ARVIWKRLAP HLPLVRVQLF
ENPQLWADYR GEGKQADLTI RTHFSAAHRL APNLSAEKYG KCTNTHGHNY HLEVTVEGEI
DSRTGMIVNV AALNQVVEDY VVKIFDHSCL NDDIPYFADI VPTTENIARY ISNLLESPID
ELGVKLSNVK LFESHQLWAD YTGNDMQGYL NISTHFSSAH RLAHPDLSLP ENTEIYGKCA
RINGHGHNYQ LELTVKGEID TSTGMVIDLG ALNQVITDYI VEPFDHTFLN KDIPFFAKVV
PTAENIALYI SNTLRSPIQE LGAKLYKVKL VESPNNACEI YITD
//
