ID   A0A0D3FCC0_9ORYZ        Unreviewed;       241 AA.
AC   A0A0D3FCC0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
OS   Oryza barthii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART02G37990.2};
RN   [1] {ECO:0000313|EnsemblPlants:OBART02G37990.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART02G37990.2};
RX   DOI=10.1007/s12284-009-9025-z;
RA   Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA   Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA   Knight J., Niazi F., Egholm M., Wing R.A.;
RT   "De novo next generation sequencing of plant genomes.";
RL   Rice 2:35-43(2009).
RN   [2] {ECO:0000313|EnsemblPlants:OBART02G37990.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate +
CC         trans-4-hydroxy-L-prolyl-[collagen]; Xref=Rhea:RHEA:18945, Rhea:RHEA-
CC         COMP:11676, Rhea:RHEA-COMP:11680, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:50342, ChEBI:CHEBI:61965; EC=1.14.11.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00024151};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004648}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004648}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
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DR   AlphaFoldDB; A0A0D3FCC0; -.
DR   EnsemblPlants; OBART02G37990.2; OBART02G37990.2; OBART02G37990.
DR   Gramene; OBART02G37990.2; OBART02G37990.2; OBART02G37990.
DR   HOGENOM; CLU_058132_1_2_1; -.
DR   Proteomes; UP000026960; Chromosome 2.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; IPR045054; P4HA-like.
DR   InterPro; IPR006620; Pro_4_hyd_alph.
DR   InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR   PANTHER; PTHR10869:SF237; PROLYL 4-HYDROXYLASE 8; 1.
DR   PANTHER; PTHR10869; PROLYL 4-HYDROXYLASE ALPHA SUBUNIT; 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   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          117..238
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   241 AA;  27301 MW;  6A598A4DFF238E6B CRC64;
     MAPSRPLMRG IRPPRVFPTR DLSEGLGERG AQWTEVISWE PRAFVYHNFL SKEECDYLIG
     LAKPHMVKST VVDSTTGKSK DSRVRTSSGM FLQRGRDKVI RAIEKRIADY TFIPMEHGEG
     LQVLHYEVGQ KYEPHFDYFL DEYNTKNGGQ RMATLLISDV EEGGETIFPD ANVNSSSLPW
     YNELSECARK GLAVKPKMGD ALLFWSMKPD ATLDPLSLHG GCPVIKGNKW SSTKWMHTTE
     E
//