ID G1X2Z1_ARTOA Unreviewed; 539 AA.
AC G1X2Z1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 22-FEB-2023, entry version 34.
DE RecName: Full=4a-hydroxytetrahydrobiopterin dehydratase {ECO:0000256|ARBA:ARBA00013252};
DE EC=4.2.1.96 {ECO:0000256|ARBA:ARBA00013252};
GN ORFNames=AOL_s00043g64 {ECO:0000313|EMBL:EGX52275.1};
OS Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX52275.1, ECO:0000313|Proteomes:UP000008784};
RN [1] {ECO:0000313|EMBL:EGX52275.1, ECO:0000313|Proteomes:UP000008784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC {ECO:0000313|Proteomes:UP000008784};
RX PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT provide insights into nematode-trap formation.";
RL PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX52275.1}.
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DR EMBL; ADOT01000057; EGX52275.1; -; Genomic_DNA.
DR RefSeq; XP_011118853.1; XM_011120551.1.
DR AlphaFoldDB; G1X2Z1; -.
DR GeneID; 22890374; -.
DR HOGENOM; CLU_505220_0_0_1; -.
DR InParanoid; G1X2Z1; -.
DR Proteomes; UP000008784; 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 Gene3D; 3.30.1360.20; Transcriptional coactivator/pterin dehydratase; 1.
DR InterPro; IPR036428; PCD_sf.
DR InterPro; IPR001533; Pterin_deHydtase.
DR Pfam; PF01329; Pterin_4a; 1.
DR SUPFAM; SSF55248; PCD-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000008784}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 539 AA; 59638 MW; 8F7068468C8B9DE8 CRC64;
MHALRCAGRH ASTIPKPSSG IRRVPPSINL ITANQSAQTA CRRPYSSKTN DASSERGTPI
RELGTVGKIE EYYQLQRVKG MTPNEAARDE AINEINREKV NPEGGIPSLR FTDIKTGTKY
HAGRSLVTGE EAKELYNEFK AHTAIVKPGP TDLPGKPTQV HILYREPTSP PERILESIRR
LCFNPSYIVT KEFGPHAIKS TDLINVELGY CSHYLPHEMK PMVLVHKNWT ISKGGRSLEK
IFRFDNRTSA RDFANGLQRL IKIKVTKTML VEHHPAFGIY GRRVFVRWGT EQPHEAISSW
DIACAKQTDR WAGACNVKDL LPEILDWTFD TKFVDKSNPE QTHQTQTQQS DPETNASDNL
MDIIEGLMAT TKSLMQAAEE PSTVQSTLSM ASEALSKTIE KISKEKEENK ESAAAKEAEV
LRWLNSEEGT PKQESPKETV GVPQEVIGDL APAAEVEGSE IVNAEATKAE TVDVVVDVQT
EYLPSETTEP QTAEATTVKL ETEAVPAEVT EAVQAEATKT EAEDAPTDGQ PPNNEKTSQ
//
