ID A0A0V1DAK0_TRIBR Unreviewed; 1163 AA.
AC A0A0V1DAK0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:KRY58443.1};
GN ORFNames=T03_14978 {ECO:0000313|EMBL:KRY58443.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY58443.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY58443.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY58443.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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:KRY58443.1}.
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DR EMBL; JYDI01000021; KRY58443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1DAK0; -.
DR STRING; 45882.A0A0V1DAK0; -.
DR Proteomes; UP000054653; 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:UP000054653};
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..1163
FT /note="4a-hydroxytetrahydrobiopterin dehydratase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006876589"
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 1163 AA; 129726 MW; 302A0AB354A0D534 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 KMFWYHKTAD GTVKNATCEQ TASPTSGHTS ADEIVSACSI SLDTYFKSGF
YWCAACIAKS ANDWACNRNH GTNDGIQVDI VGPPLVYYEP VTEEKVDANE ARIIAQFCSD
PTPNSNDGFQ WTIDGQRLLP GERLGSFTAE MPHRNSTYPA CYNAGLMISP LTESDKKKFV
EYRIQNEHGE LKKAINLAAL IGNGNSSAYS EGDIGLAVGI AIAVLVLILI LLTLFLWWRR
IACFTNSKAK QAKVSKQQKK YPINIVPEVM RQAPKPERLP PVSAPHNDLY KPEVTYSWRN
AGGGGVGGRV SKEVAPQLLI PPKTSSPIVY PTQHPGSQTR EGLNYAELDL VKDAAARRPI
TTSNLPVEYS RLQPYKPPTS ISEISSACSM RLLKLGAKSL FCARALPFSS SSTVCRKMLP
SLLNDQEREQ HLNELIGQGW KLQEKRDAIQ KLFTFGDFNE AFGFMTQIAL KAEKMNHHPE
WFNVYNKVDI TLSTHDCNGL SMKDITLGKF IEGVAAYFSL SVTKVNLSRA EDSCCISELV
KVCILVTGCV CLARTIPMER AVERRLLKRI VNCFMMKVES VLSLEELCKN LTRYEEYTEL
KLTTVLKCLR QNPHHFRIEA KHGGNYSLMI TLNSLDAHKK GECENAYAVF KAKMSAGREA
SGDLILENFE LSFEAIMMFI CRERGGHFTM EEYEKYSTIL NIILHMDKIP IRLQDIYCEN
NLLKRSHILF ERGGIFHQQE DCVTRLLVNH GMNFKNFYEA ACNISFLSEE VKRKLHMESE
TSMMKFLCTH KWLFQMMKND VDGSDCIVCF RKLPSVDAVL LQAARMKAIA IGKLVTDLTD
QEATDSKELS VEECGEISAE SQE
//
