ID E5ESC1_9PHYC Unreviewed; 197 AA.
AC E5ESC1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=BpV1_106c {ECO:0000313|EMBL:ADQ91733.1};
OS Bathycoccus sp. RCC1105 virus BpV1.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Algavirales; Phycodnaviridae; Prasinovirus;
OC Bathycoccus sp. RCC1105 virus BpV.
OX NCBI_TaxID=880159 {ECO:0000313|EMBL:ADQ91733.1, ECO:0000313|Proteomes:UP000202660};
RN [1] {ECO:0000313|EMBL:ADQ91733.1, ECO:0000313|Proteomes:UP000202660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20861243; DOI=10.1128/JVI.01123-10;
RA Moreau H., Piganeau G., Desdevises Y., Cooke R., Derelle E., Grimsley N.;
RT "Marine prasinovirus genomes show low evolutionary divergence and
RT acquisition of protein metabolism genes by horizontal gene transfer.";
RL J. Virol. 84:12555-12563(2010).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; HM004432; ADQ91733.1; -; Genomic_DNA.
DR RefSeq; YP_004061536.1; NC_014765.1.
DR GeneID; 10020016; -.
DR KEGG; vg:10020016; -.
DR OrthoDB; 11494at10239; -.
DR Proteomes; UP000202660; Genome.
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 SUPFAM; SSF51197; Clavaminate synthase-like; 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:UP000202660}.
FT DOMAIN 95..194
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 197 AA; 23256 MW; 89D772009A080AF4 CRC64;
MNKVILFVSF LLIIWFFIPI YEKPRVLKNV LSEDECKHIQ DIASKKLQTS TVSMSRDIDE
KIRKSETAWL KASEDPVVDK LIRKCVSMTD RPLHNCEDLQ VLKYKPGGFY KPHQDCFKND
KNKRMYTFII ALNDEYEGGE TEFPNIKRRY RLEKGDALFF NTLNNYECTT KQALHGGAPV
KSGEKWVCNL WIRKYRY
//
