ID C1E489_MICCC Unreviewed; 444 AA.
AC C1E489;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=MICPUN_57951 {ECO:0000313|EMBL:ACO62682.1};
OS Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO62682.1, ECO:0000313|Proteomes:UP000002009};
RN [1] {ECO:0000313|EMBL:ACO62682.1, ECO:0000313|Proteomes:UP000002009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; CP001325; ACO62682.1; -; Genomic_DNA.
DR RefSeq; XP_002501424.1; XM_002501378.1.
DR AlphaFoldDB; C1E489; -.
DR GeneID; 8242710; -.
DR KEGG; mis:MICPUN_57951; -.
DR eggNOG; KOG3710; Eukaryota.
DR InParanoid; C1E489; -.
DR OMA; YSDEVEH; -.
DR OrthoDB; 298324at2759; -.
DR Proteomes; UP000002009; Chromosome 4.
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; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR12907; EGL NINE HOMOLOG-RELATED; 1.
DR PANTHER; PTHR12907:SF26; HIF PROLYL HYDROXYLASE, ISOFORM C; 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:UP000002009}.
FT DOMAIN 323..430
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 444 AA; 47158 MW; 0F475A357EACD9D4 CRC64;
MRHNAAHALA RVVQASVSRE VASGTLRIAP LAPRRLKRSM SSITEDDQQR LLEHYALGLR
GILAEHDDLT DPALTAKMRA LRDDAPVRLE HRFWGAQFLA MAFGHELGFA AAHPPALRAV
FNLGVVAAEN GLVPFQAMRS AHGQLARLGV LRCDRVDPGA DGGDGWSLAT PRAATPWELF
ASDRLRVAAR EAAAGLVARG SAVVDGALGP RLAEAASAAL TRHVASERHL FSAGQLDQTG
RSDSSTRGDI ISWISGDEGA DEALRLGAGI WGGHVPGSSE GLLGRCPPAV VSPGAVAQMF
RSCLSDHVIS AMPAGVLMSS DNYVTNAMMS VYAPGAPGFV PHTDHCGGHD LRRVTAVYYP
ASNGDWDVDR DGGALVLRPG EDGAGGRRET IAPEGDRLVV FYSDEVEHEV VGVSEGASRE
RLALSFWYLK PPPGRFDPSL MSRS
//
