OGFD1_OSTTA
ID OGFD1_OSTTA Reviewed; 514 AA.
AC Q01F03;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Prolyl 3,4-dihydroxylase OGFOD1;
DE Short=otOGFOD1;
DE EC=1.14.11.- {ECO:0000269|PubMed:24550462};
DE AltName: Full=uS12 prolyl 3,4-dihydroxylase;
GN Name=Ogd; OrderedLocusNames=Ot02g01720;
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595;
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24550462; DOI=10.1073/pnas.1311750111;
RA Loenarz C., Sekirnik R., Thalhammer A., Ge W., Spivakovsky E.,
RA Mackeen M.M., McDonough M.A., Cockman M.E., Kessler B.M., Ratcliffe P.J.,
RA Wolf A., Schofield C.J.;
RT "Hydroxylation of the eukaryotic ribosomal decoding center affects
RT translational accuracy.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4019-4024(2014).
CC -!- FUNCTION: Prolyl 3,4-dihydroxylase that catalyzes 3,4-dihydroxylation
CC of 'Pro-61' of small ribosomal subunit uS12 (RPS23), thereby regulating
CC protein translation termination efficiency.
CC {ECO:0000269|PubMed:24550462}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 =
CC [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate;
CC Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC Evidence={ECO:0000269|PubMed:24550462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [ribosomal protein uS12]-(3S)-3-hydroxy-L-
CC proline + O2 = [ribosomal protein uS12]-(3S)-3,4-dihydroxy-L-proline
CC + CO2 + succinate; Xref=Rhea:RHEA:54160, Rhea:RHEA-COMP:13817,
CC Rhea:RHEA-COMP:13818, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85428,
CC ChEBI:CHEBI:138052; Evidence={ECO:0000269|PubMed:24550462};
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:0000305};
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000250|UniProtKB:P40032}.
CC -!- SIMILARITY: Belongs to the TPA1 family. {ECO:0000305}.
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DR EMBL; CAID01000002; CAL52098.1; -; Genomic_DNA.
DR RefSeq; XP_003074838.1; XM_003074790.1.
DR AlphaFoldDB; Q01F03; -.
DR SMR; Q01F03; -.
DR STRING; 70448.Q01F03; -.
DR GeneID; 9832551; -.
DR KEGG; ota:OT_ostta02g00870; -.
DR eggNOG; KOG3844; Eukaryota.
DR InParanoid; Q01F03; -.
DR OMA; YMAGDDD; -.
DR OrthoDB; 623539at2759; -.
DR Proteomes; UP000009170; Chromosome 2.
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:0031543; F:peptidyl-proline dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0018188; P:peptidyl-proline di-hydroxylation; IDA:UniProtKB.
DR Gene3D; 3.60.130.20; -; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR043044; TPA1/Ofd1_C.
DR InterPro; IPR039558; TPA1/OFD1_N.
DR Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR Pfam; PF10637; Ofd1_CTDD; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Vitamin C.
FT CHAIN 1..514
FT /note="Prolyl 3,4-dihydroxylase OGFOD1"
FT /id="PRO_0000429172"
FT DOMAIN 114..221
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 132
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 146
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P40032"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:P40032,
FT ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 212
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 514 AA; 58416 MW; 1A25D25890FE77B4 CRC64;
MPDHIYSHSF AQFLRNADNS VVNINPYPYV AFEDVFDDTF LRECLKELKS YLTAHFKETD
LFKVFQTTDL ANLEDCIRDA HTNVPNLIRL REHLYSPGFR GFVSTVTGTG PLDGAVDCSC
NIYTSGCHLL CHDDVIGTRK ISYIIYLSDP DCDWLAVDGG QLELYASDRR TVPTHTPVVS
ILPSWNSMVM FEVSPGRSFH AVREVSAEMK TRVSISGWFH TKERHIKRNQ RETSTLDQLH
SMIPATHAEW AVLHVNRVLS PSYSLVQDLT KWINPEYLRS ESVKRVRQVF EADGSVQLFN
FLLPHIAEPI KRKLNREDCR NSRHRCMYDH GYGDSWVVQG PPHVQRYLSY QPLECTLANK
RSNSGELLKK LMCDLFESSS FQNWVRAVTG SVCDLAHSEV RRFRPGFDYT LAHAGTKRCS
SEIDVTLCLT SGPNPAEWLS GDLGGFKCFI PIGSKSDRAD VYEEIGEEQN MRSVTPSFNC
LSLVKVNTGI GDFVKYVSTS AKSSRWDIVC RYST
