ID A0A0N4WUN1_HAEPC Unreviewed; 284 AA.
AC A0A0N4WUN1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=hypoxia-inducible factor-proline dioxygenase {ECO:0000256|ARBA:ARBA00039004};
DE EC=1.14.11.29 {ECO:0000256|ARBA:ARBA00039004};
GN ORFNames=HPLM_LOCUS15356 {ECO:0000313|EMBL:VDO56315.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001536401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001536401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO56315.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO56315.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-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; UZAF01018949; VDO56315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4WUN1; -.
DR STRING; 6290.A0A0N4WUN1; -.
DR WBParaSite; HPLM_0001536401-mRNA-1; HPLM_0001536401-mRNA-1; HPLM_0001536401.
DR OMA; GCEAINI; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; 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:UP000268014}.
FT DOMAIN 190..284
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 284 AA; 32877 MW; EB044BC92A7D222A CRC64;
MVQLDKIIEA GPPSRISAGV LLGRCRKRPT PSNSIIFKDH LKNLVYNTTL QDHQNMMKKR
GLTLNAHQTI VVRLRYIAEY VIRSLNEFGW AVVDNFLGDE HCRFTYKEIK CLYERGLFSA
GQLMDGKHKD EYHVKDIRSD QIYWFDGIDP RANDAATVRL LVSMIDSVIQ HFKGRLPPYD
ISGRSRGEKT SNTALYFQAM LAIYPGNGTR YVKHVDNPVK DGRCITTIYY CNEDWDINKH
GGTLRLYPET SLIPMDIDPK ADRLVLFWSD RRNPHEVMPV FRPR
//
