ID A0A0V1L6P4_9BILA Unreviewed; 1137 AA.
AC A0A0V1L6P4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 Name=pcbd-1 {ECO:0000313|EMBL:KRZ55153.1};
GN ORFNames=T02_10414 {ECO:0000313|EMBL:KRZ55153.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ55153.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ55153.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ55153.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ55153.1}.
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DR EMBL; JYDW01000121; KRZ55153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1L6P4; -.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd00914; PCD_DCoH_subfamily_b; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.1360.20; Transcriptional coactivator/pterin dehydratase; 1.
DR HAMAP; MF_00434; Pterin_4_alpha; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
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; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF55248; PCD-like; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1137
FT /note="4a-hydroxytetrahydrobiopterin dehydratase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006881563"
FT TRANSMEM 514..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 182..258
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 269..365
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
SQ SEQUENCE 1137 AA; 127411 MW; 9F3DD096BA884ADD CRC64;
MYPLISSSSL LLLLAFIGIF YTGAAQFQVW GQGTPNSALP LGTANQQPNH GDPSIRGFGS
TVAPKLAITL DLLPIGRAMH LQRISWRTPF STPLYCVSDQ SGVRPMFSCL DCNSTEFNNL
LQAKSLDKST VAEFAATWLD SVPINGSMHG KRLVCSVYYD GPSGPSNVSV MSVMDVQFLD
EPTIVDEKYH PALNGNKFFS NFPSTLHCKA IGNPPPTQFS WFIEGSRLFD GPMIALGIDH
RLKSIQCQAM NTLYEKMSKV VVVDKLSYPQ LSGHNFQSIK TSSVFEPGSN RARMGQQITL
LCKATGYPLP KMFWYHKMAD NTVRNATCEQ NASPTSGHTS ADEIVSACSI SLDTYFKSGF
YWCSACIAKS ANDWACNRNH GTNDGIQVDI VGPPLVYYEP VTEEKVDANE ARIIAQFCSD
PTPNSNDGFQ WTIDGQRLLP GERLGSFTAE MPHRNSTYPA CYNAGLMISP LTESDKKKFV
EYRIQNEHGE LKKAINLVAL IGNGNSSAYS EGDIGLAVGI AIAVLILILI LLTLFLWWRR
IACFTNSKAK QAKVSKQQKK YPINIVPEVM RQAPKPERLP PVSAPHNDLY KPEPQLLIPP
KTSSPIVYPT QHPGSQTREG LNYAELDLVK DAAARRPITT SNLPVEYSRL QPYKPPTSIS
EISMRLLKLG AKSLFCARAL PFSSSSTVCR KMLPSLLNDQ EREQHLNELI GQGWKLQEKR
DAIQKLFTFG DFNEAFGFMT QIALKAEKMN HHPEWFNVYN KVDITLSTHD CNGLSMKDIT
LGKFIEGVAA YFSLSVTKVN LSRAEDSYCI SELVKVCILV TGCVCLARTI PMERAVERRL
LKRIVNCFMM KVESVLSLEE LCKNLTRYEE YTELKLTTVL KCLRQNPHHF RIEAKHGGNY
SLMITLNSLD AHKKGECENA YAVFKGKMSA GREASGDLIL ENFELSFEAI IMFICRERGG
HFTMEEFEKY STILNIILHM DKIPIRLQDI YCENNLLKRS HILFERGGIF HQQEDCVTRL
LVNHGMNFKN FYEAACNISF LSEEVKRKLH MESETSMMKF LCTHKWLFQM MKNDVDGSDC
IVCFRKLPSV DAILLQAARI KAIAIGKLVT DLTDQEATDS KELSVEECGE ISVESQE
//
