ID A0A0N4V8C9_ENTVE Unreviewed; 372 AA.
AC A0A0N4V8C9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=hypoxia-inducible factor-proline dioxygenase {ECO:0000256|ARBA:ARBA00039004};
DE EC=1.14.11.29 {ECO:0000256|ARBA:ARBA00039004};
GN ORFNames=EVEC_LOCUS6177 {ECO:0000313|EMBL:VDD91426.1};
OS Enterobius vermicularis (Human pinworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000660301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EVEC_0000660301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDD91426.1, ECO:0000313|Proteomes:UP000274131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[hypoxia-inducible factor alpha
CC subunit] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[hypoxia-
CC inducible factor alpha subunit]; Xref=Rhea:RHEA:48400, Rhea:RHEA-
CC COMP:12093, Rhea:RHEA-COMP:12094, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.29;
CC Evidence={ECO:0000256|ARBA:ARBA00035981};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; UXUI01008407; VDD91426.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4V8C9; -.
DR STRING; 51028.A0A0N4V8C9; -.
DR WBParaSite; EVEC_0000660301-mRNA-1; EVEC_0000660301-mRNA-1; EVEC_0000660301.
DR Proteomes; UP000038041; Unplaced.
DR Proteomes; UP000274131; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR12907; EGL NINE HOMOLOG-RELATED; 1.
DR PANTHER; PTHR12907:SF26; HIF PROLYL HYDROXYLASE, ISOFORM C; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000274131}.
FT DOMAIN 123..221
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 372 AA; 43120 MW; 0583A313817AA6F4 CRC64;
MGKHLTMLCS DPVKYPSITR YQAMALRVKE IADHVINKLK EYGWAVVDNF FGPDHCRQAL
GYYSLYFSLF ASELKFCIFS RIFWFDVKDK RVANAVSLRL LVSAIDSVTY HFQDRIYPYN
ICSRARPMIA VFPGGGTHYV KHVDNPAKDG RCITSIYYCN ENWDVEKDGG AFRLYPENSA
SPITITPKAD RLLFFFSDRR NPHEVLPTFR KRFAMTIWYH DRDEKNAAMG NRRLLQLRRK
HTGIGIAGEN CASEETGLRK DSVEITEPPT KWKVLGFLSA LWNGPRCYWL SSKLRLVSFT
SIMRLFSYFI FVDCFRLKGK IFLLHLITLA VCHTLMGRFL HCELARSTVQ ICVVQRRLRI
ASQISCCALK RR
//
