ID A0A1V6SQU9_9EURO Unreviewed; 324 AA.
AC A0A1V6SQU9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=4a-hydroxytetrahydrobiopterin dehydratase {ECO:0000256|ARBA:ARBA00013252};
DE EC=4.2.1.96 {ECO:0000256|ARBA:ARBA00013252};
DE AltName: Full=4-alpha-hydroxy-tetrahydropterin dehydratase {ECO:0000256|ARBA:ARBA00030497};
GN ORFNames=PENFLA_c029G07841 {ECO:0000313|EMBL:OQE16074.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE16074.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin =
CC (6R)-L-erythro-6,7-dihydrobiopterin + H2O; Xref=Rhea:RHEA:11920,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15642, ChEBI:CHEBI:43120; EC=4.2.1.96;
CC Evidence={ECO:0000256|ARBA:ARBA00001554};
CC -!- SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase
CC family. {ECO:0000256|ARBA:ARBA00006472}.
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:OQE16074.1}.
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DR EMBL; MLQL01000029; OQE16074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6SQU9; -.
DR STRING; 254877.A0A1V6SQU9; -.
DR OrthoDB; 117067at2759; -.
DR Proteomes; UP000191342; Unassembled WGS sequence.
DR GO; GO:0008124; F:4-alpha-hydroxytetrahydrobiopterin dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro.
DR CDD; cd00488; PCD_DCoH; 1.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.30.1360.20; Transcriptional coactivator/pterin dehydratase; 1.
DR InterPro; IPR036428; PCD_sf.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR001533; Pterin_deHydtase.
DR PANTHER; PTHR12599; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE; 1.
DR PANTHER; PTHR12599:SF0; PTERIN-4-ALPHA-CARBINOLAMINE DEHYDRATASE; 1.
DR Pfam; PF01329; Pterin_4a; 1.
DR Pfam; PF14681; UPRTase; 1.
DR SUPFAM; SSF55248; PCD-like; 1.
DR SUPFAM; SSF53271; PRTase-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000191342}.
SQ SEQUENCE 324 AA; 35690 MW; 38D80ECF5E0D268A CRC64;
MQKEEEKMAI PAPIIELPQT PTLTNLMTTF CSPSSTPKIM QDTIHTLTHE IISAAKSHDQ
TLQSPTTMIP ILRGALPMFV AAQPLLPATS CILARCSKTK GTQDVVVDWL GRRPFPPAFD
DGKIVILDTI IATGDTVVKL CEELWEMSGG LPSSVVVLCV YAAPEALERV ARCPVVEYVV
VGRRAERCDE RGYLVPYTNG DIGDKIYGGV RRKEGEMGEP VVAEGEEVQS VLSGVQSLLA
ENGGLWKLTE DGLAIEREIQ FSGFKEAWEI KTFMNHVADT ATKLRHHPEW SNVYNKVSIR
WTTHRPKGLT SLDVVAAQLC DSYV
//