ID A0A024G1L7_9STRA Unreviewed; 305 AA.
AC A0A024G1L7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 28-JUN-2023, entry version 26.
DE RecName: Full=6-pyruvoyltetrahydropterin synthase {ECO:0000256|ARBA:ARBA00013100};
DE EC=4.2.3.12 {ECO:0000256|ARBA:ARBA00013100};
GN ORFNames=BN9_013340 {ECO:0000313|EMBL:CCI40550.1};
OS Albugo candida.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI40550.1, ECO:0000313|Proteomes:UP000053237};
RN [1] {ECO:0000313|EMBL:CCI40550.1, ECO:0000313|Proteomes:UP000053237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI40550.1,
RC ECO:0000313|Proteomes:UP000053237};
RA Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA Jones J.D.G.;
RT "Recombination and specialization in a pathogen metapopulation.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis;
CC tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00005126}.
CC -!- SIMILARITY: Belongs to the PTPS family.
CC {ECO:0000256|ARBA:ARBA00009164}.
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:CCI40550.1}.
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DR EMBL; CAIX01000009; CCI40550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024G1L7; -.
DR InParanoid; A0A024G1L7; -.
DR OrthoDB; 48098at2759; -.
DR UniPathway; UPA00849; UER00819.
DR Proteomes; UP000053237; Unassembled WGS sequence.
DR GO; GO:0003874; F:6-pyruvoyltetrahydropterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-UniPathway.
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 InterPro; IPR003656; Znf_BED.
DR PANTHER; PTHR12589:SF7; 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR PANTHER; PTHR12589; PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR Pfam; PF01242; PTPS; 1.
DR Pfam; PF02892; zf-BED; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000053237};
KW Tetrahydrobiopterin biosynthesis {ECO:0000256|ARBA:ARBA00023007};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 65..98
FT /note="BED-type"
FT /evidence="ECO:0000259|Pfam:PF02892"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 305 AA; 33807 MW; F8C2D332E507A7BF CRC64;
MLRALSEDAN SVVENNEVSD AVTPTEIDDH HHNQSLSDDL PRKKRKFATM TKELSPDQKA
IVKLHVSREA TSEGFVKCNF CNKEITSKNV DRWASHLRGC GKTPEDVKVQ IQPFRTVVNA
HANIISAALS AANVPQASLQ HSTNTNHLGN LQNAITTSYN EVFKVHVAKD YMKFNAAHFI
AYKGYREKLH GHNYRVAVTL SGVVGPDGYV VDFGEIKKIS RVISKDLDES FLVPMNSDVL
KITFDGTNVH ILTEDNAKFS FPKSDCSLLP IVHSSAEELA IYFSNQLIDA FTLVALLASK
SIILN
//