ID A4S7T0_OSTLU Unreviewed; 309 AA.
AC A4S7T0;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=OSTLU_42939 {ECO:0000313|EMBL:ABO99619.1};
OS Ostreococcus lucimarinus (strain CCE9901).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO99619.1, ECO:0000313|Proteomes:UP000001568};
RN [1] {ECO:0000313|EMBL:ABO99619.1, ECO:0000313|Proteomes:UP000001568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCE9901 {ECO:0000313|EMBL:ABO99619.1,
RC ECO:0000313|Proteomes:UP000001568};
RX PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA Van de Peer Y., Moreau H., Grigoriev I.V.;
RT "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT of plankton speciation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000594; ABO99619.1; -; Genomic_DNA.
DR RefSeq; XP_001421326.1; XM_001421289.1.
DR AlphaFoldDB; A4S7T0; -.
DR STRING; 436017.A4S7T0; -.
DR EnsemblPlants; ABO99619; ABO99619; OSTLU_42939.
DR GeneID; 5005300; -.
DR Gramene; ABO99619; ABO99619; OSTLU_42939.
DR KEGG; olu:OSTLU_42939; -.
DR eggNOG; KOG1591; Eukaryota.
DR HOGENOM; CLU_058132_1_0_1; -.
DR OMA; NIWTHER; -.
DR OrthoDB; 313389at2759; -.
DR Proteomes; UP000001568; Chromosome 14.
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:SF207; P4HA_N DOMAIN-CONTAINING PROTEIN-RELATED; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001568};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..309
FT /note="Fe2OG dioxygenase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002673108"
FT DOMAIN 161..293
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REGION 114..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 34010 MW; 97760F169F1F9392 CRC64;
MPRGGASRVA VLALIALATS AAPRRATADR ARLPRDARDE RLDDDDARLR AEEHVAYASD
ARSRVGLRRD GADARQWIER ISESPRAYVY RNFLTREEAE ATIAAARRTM RRSEVVNEAD
GTSKTSDERT SSGGWVSGED SEVMANIERR VAAWTMLPRN RGETTQVMRY EAGQEYAAHD
DYFHDEVNVK NGGQRAATVL MYLSDVEEGG ETVFPRGTPL GGAAPEKSGV TQGNACERAL
RGDPNVLAVK PRRGDALLFF NVHLNGEVDE RARHAGCPVV RGTKWTATRW QHVGALNIGS
FARTDSQTT
//