ID   A0A084QV36_STAC4        Unreviewed;       195 AA.
AC   A0A084QV36;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=S40285_06956 {ECO:0000313|EMBL:KFA67821.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA67821.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA67821.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA67821.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
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}.
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DR   EMBL; KL660101; KFA67821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084QV36; -.
DR   STRING; 1283841.A0A084QV36; -.
DR   HOGENOM; CLU_081974_1_0_1; -.
DR   InParanoid; A0A084QV36; -.
DR   OMA; VHWTTHR; -.
DR   OrthoDB; 117067at2759; -.
DR   Proteomes; UP000028524; 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   Gene3D; 3.30.1360.20; Transcriptional coactivator/pterin dehydratase; 1.
DR   InterPro; IPR036428; PCD_sf.
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   SUPFAM; SSF55248; PCD-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028524}.
SQ   SEQUENCE   195 AA;  21265 MW;  8A599361779AD261 CRC64;
     MVASRITKPA AQFKPAVKLL THTVTPRLAS SVAAAMQQPR FSAGTDDAHV KPQLDTLLES
     AGGRWALTAG GEGLERSFKF KTFAKTWVCV PLGDYQRDQD GLKRELVQDF MTAVSLQCKV
     KNHHPEWSNV YNTTFIRWTT HSPKGLSEKD VTLAAMCDAI ARDFGELDPE PSSCELKGLA
     DGVAASARDC CAPKK
//