ID A0A2A9M851_9APIC Unreviewed; 496 AA.
AC A0A2A9M851;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=6-pyruvoyltetrahydropterin synthase {ECO:0000256|ARBA:ARBA00013100};
DE EC=4.2.3.12 {ECO:0000256|ARBA:ARBA00013100};
GN ORFNames=BESB_017890 {ECO:0000313|EMBL:PFH32471.1};
OS Besnoitia besnoiti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH32471.1, ECO:0000313|Proteomes:UP000224006};
RN [1] {ECO:0000313|EMBL:PFH32471.1, ECO:0000313|Proteomes:UP000224006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH32471.1,
RC ECO:0000313|Proteomes:UP000224006};
RA Schares G., Venepally P., Lorenzi H.A.;
RT "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL Submitted (SEP-2017) 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:PFH32471.1}.
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DR EMBL; NWUJ01000011; PFH32471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9M851; -.
DR VEuPathDB; ToxoDB:BESB_017890; -.
DR OrthoDB; 48098at2759; -.
DR UniPathway; UPA00849; UER00819.
DR Proteomes; UP000224006; Chromosome x.
DR GO; GO:0003874; F:6-pyruvoyltetrahydropterin synthase activity; IEA:UniProtKB-EC.
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 PANTHER; PTHR12589:SF7; 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR PANTHER; PTHR12589; PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR Pfam; PF01242; PTPS; 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:UP000224006};
KW Tetrahydrobiopterin biosynthesis {ECO:0000256|ARBA:ARBA00023007};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 50759 MW; F59C90222F715E57 CRC64;
MPQRVAKINS SPSSPRRSSP DRRAPVARDA GVSLLDSHGA TSLRGEAPPG GSAPPLGGPP
PSSSNSNSAP REGAVFVPLS APSAPSPNHA VQGSSLSLGA SVATRAVGST ASDDSRSLAS
RPELSSSSFA GGSLGSVSPG GSTASCGSAS RRELSPQTAL AGYVVSMGTQ PHHQLLPQHP
LPQQLAQAPS AQSHPHGASS SVAATEGSPP SSPRSTFSSV HSFGQHEPVA LPPPSGLHTL
GGESAAGPAR IAGCLGGGAT PSLGSCCLGA AAGADASRAF CDAHGVLTSS PGVCGRGVGS
GRSPAAGDIA ALNGEGSAAD YVSLLSSGAF EVAVQSPDMS FNCSHFVAYR GYRERLHGHN
YAVAVRLGGA VGPDGYVLDF GEIKRNVREI CKSLNEYLIV PMRSDVLDIT QEGQSMIIRC
EDGAEFKIPC SDCQCLPLVH SSTEEICCYL WQLVIDKVTL AVLKKRGVKW LEVTVSETPL
QKASFRREIQ PMWSMS
//
