ID   OGFD3_XENTR             Reviewed;         317 AA.
AC   Q5XGE0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 3;
GN   Name=ogfod3;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00805};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the OGFOD3 family. {ECO:0000305}.
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DR   EMBL; BC084502; AAH84502.1; -; mRNA.
DR   RefSeq; NP_001011105.1; NM_001011105.1.
DR   AlphaFoldDB; Q5XGE0; -.
DR   PaxDb; Q5XGE0; -.
DR   DNASU; 496518; -.
DR   GeneID; 496518; -.
DR   KEGG; xtr:496518; -.
DR   CTD; 79701; -.
DR   Xenbase; XB-GENE-6457975; ogfod3.
DR   eggNOG; ENOG502QR2P; Eukaryota.
DR   InParanoid; Q5XGE0; -.
DR   OrthoDB; 674380at2759; -.
DR   Proteomes; UP000008143; Chromosome 10.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   InterPro; IPR039210; OGFOD3.
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; PTHR14650; PTHR14650; 1.
DR   Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR   SMART; SM00702; P4Hc; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Glycoprotein; Iron; Membrane; Metal-binding; Oxidoreductase;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Vitamin C.
FT   CHAIN           1..317
FT                   /note="2-oxoglutarate and iron-dependent oxygenase domain-
FT                   containing protein 3"
FT                   /id="PRO_0000325888"
FT   TOPO_DOM        1..39
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..317
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          205..307
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        296
FT                   /evidence="ECO:0000255"
FT   BINDING         228
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         230
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         286
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         296
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   317 AA;  35565 MW;  C69C1B4D45EE90C8 CRC64;
     MATRHRRRGG SAPSWAKPGK PGERPGGPKK SRGRTSWKSL LIWGVFGVTL GLMAGYYLWG
     ELITDDSVTE VLAAQRDAVA QRFFHVPCSQ DYESLKQFEA CTPRKCGRAV TDSVITLQEA
     EKMRRLAEAG LSLGGSDGGA SILDLHSGAL SMGKKFVNMY RFFGDKLKDV MSDEDFNLYR
     EVRLKIQHEI ARTFNISVSS LHLTKPTFFS RMNSSEAKTA HDEYWHPHID KVTYGSFDYT
     SLLYLSDYSQ DFGGGRFVFI DEGANRTVEP RTGRLSFFTS GSENLHRVEK VSWGTRYAIT
     ISFTCNPEHA IGDPTWT