OGFD2_DANRE
ID OGFD2_DANRE Reviewed; 345 AA.
AC A3KGZ2; A1A5Z6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2;
DE EC=1.14.11.-;
GN Name=ogfod2; ORFNames=si:dkey-21k4.1, zgc:158437;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2006) 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 -!- SIMILARITY: Belongs to the OGFOD2 family. {ECO:0000305}.
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DR EMBL; AL929297; CAM46973.1; -; Genomic_DNA.
DR EMBL; BC128872; AAI28873.1; -; mRNA.
DR RefSeq; NP_001307103.1; NM_001320174.1.
DR AlphaFoldDB; A3KGZ2; -.
DR SMR; A3KGZ2; -.
DR STRING; 7955.ENSDARP00000073125; -.
DR PaxDb; A3KGZ2; -.
DR Ensembl; ENSDART00000078664; ENSDARP00000073125; ENSDARG00000115533.
DR Ensembl; ENSDART00000133641; ENSDARP00000116458; ENSDARG00000056211.
DR GeneID; 790923; -.
DR KEGG; dre:790923; -.
DR CTD; 79676; -.
DR ZFIN; ZDB-GENE-061215-54; ogfod2.
DR eggNOG; KOG1971; Eukaryota.
DR GeneTree; ENSGT00940000153974; -.
DR HOGENOM; CLU_045835_1_0_1; -.
DR InParanoid; A3KGZ2; -.
DR OMA; FYTCSCF; -.
DR OrthoDB; 756511at2759; -.
DR PhylomeDB; A3KGZ2; -.
DR TreeFam; TF329650; -.
DR PRO; PR:A3KGZ2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000056211; Expressed in testis and 21 other tissues.
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; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Vitamin C.
FT CHAIN 1..345
FT /note="2-oxoglutarate and iron-dependent oxygenase domain-
FT containing protein 2"
FT /id="PRO_0000288980"
FT DOMAIN 207..301
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 229
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 282
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 292
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CONFLICT 117
FT /note="Q -> E (in Ref. 2; AAI28873)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="S -> P (in Ref. 2; AAI28873)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="S -> P (in Ref. 2; AAI28873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 39820 MW; 91D463FBB270CA5C CRC64;
MERFYTCSCF FTDNIFLEEY KLHVRFVSEN QFRKDYQNIL RSLGCESESQ FRDVIGKIQA
EIERRQNHKL KSTERAAVIK EIYTPLHQHV YHLQESFLAP ELLEMVKYCA SSEANVQGLL
KLIQTEAASR VFRFQVFRKE FCKDLLEELE HFEQSDAPKG RPNTMNNYGI VLNELGFDEG
FITPLREVYL RPLTALLYSD CGGNCLDSHK AFVVKYDMHE DLNLSYHYDN SEVTLNVSLG
KDFTEGNLFF GDMRQVPLSE TECVEVEHRV TEGLLHRGQH MHGALSISSG TRWNLIIWMR
ASRQRNKLCP MCGKRPTLVE SDGFSDGFTM DSDGDARANV SCSLT
