ID A0A3B4W9A1_SERLL Unreviewed; 242 AA.
AC A0A3B4W9A1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=hypoxia-inducible factor-proline dioxygenase {ECO:0000256|ARBA:ARBA00039004};
DE EC=1.14.11.29 {ECO:0000256|ARBA:ARBA00039004};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000000316.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000000316.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 AlphaFoldDB; A0A3B4W9A1; -.
DR STRING; 1841481.ENSSLDP00000000316; -.
DR Ensembl; ENSSLDT00000000359.1; ENSSLDP00000000316.1; ENSSLDG00000000320.1.
DR GeneTree; ENSGT00940000158745; -.
DR Proteomes; UP000261360; Unplaced.
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:SF29; PROLYL HYDROXYLASE EGLN3; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 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}.
FT DOMAIN 117..218
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 242 AA; 27174 MW; FD4CE4C50136FBF7 CRC64;
MPFIEHVSDA DLERLALERV VPALLSHGFC HVDGLLGQLA GDAVLEQVKE MHRSGALQDG
RLAGSVRGIH RKSIRGDKIA WVSGSERGCE AISFLLNLID KLISVCASRL GSKAIRERSK
AMVACYPGNG AGYVKHVDNP NSDGRCITCI YYLNKNWNAT EHGGVLRIFP EGKSYVADIK
PLFDRLLFFW SDRRNPHEVQ PSYSTRRRAF INVNRQRETR DMMPSGLWDR NVSCCSMFLI
IL
//
