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Database: UniProt
Entry: S4RTW2_PETMA
LinkDB: S4RTW2_PETMA
Original site: S4RTW2_PETMA 
ID   S4RTW2_PETMA            Unreviewed;       244 AA.
AC   S4RTW2;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=hypoxia-inducible factor-proline dioxygenase {ECO:0000256|ARBA:ARBA00039004};
DE            EC=1.14.11.29 {ECO:0000256|ARBA:ARBA00039004};
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000008652.1, ECO:0000313|Proteomes:UP000245300};
RN   [1] {ECO:0000313|Ensembl:ENSPMAP00000008652.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; S4RTW2; -.
DR   STRING; 7757.ENSPMAP00000008652; -.
DR   Ensembl; ENSPMAT00000008691.1; ENSPMAP00000008652.1; ENSPMAG00000007868.1.
DR   GeneTree; ENSGT00940000155704; -.
DR   HOGENOM; CLU_022206_0_1_1; -.
DR   OMA; NKMNDNG; -.
DR   Proteomes; UP000245300; 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:SF4; EGL NINE HOMOLOG 1; 1.
DR   PANTHER; PTHR12907; EGL NINE HOMOLOG-RELATED; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245300}.
FT   DOMAIN          114..212
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   244 AA;  27041 MW;  6F08C4387DAAE267 CRC64;
     PNGQPARPSM AQRAASYVVP CMEKLGICMV EDFLGEETGS AILAEVKRLH GSGKFCDGQL
     VGQPRAKPSA IRGDKIAWIS GSEPGCEKIA YLMSQMDELI RHCAGRLGIY NINGRTKAMV
     ACYPGKGAGY VRHVDNPNGD GRCVTCIYYL NKNWDSKVHG GVLRIFPEGK PQFADIEPIF
     DRLLLFWSDR RNPHEVQASY STRYAITVWY FDKEERAQAI KRHSLESNSS NIYVKNLAGP
     SAPA
//
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