ID D0MJ45_RHOM4 Unreviewed; 219 AA.
AC D0MJ45;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=2OG-Fe(II) oxygenase {ECO:0000313|EMBL:ACY48503.1};
GN OrderedLocusNames=Rmar_1617 {ECO:0000313|EMBL:ACY48503.1};
OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS obamensis).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC Rhodothermus.
OX NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY48503.1, ECO:0000313|Proteomes:UP000002221};
RN [1] {ECO:0000313|EMBL:ACY48503.1, ECO:0000313|Proteomes:UP000002221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43812 / DSM 4252 / R-10
RC {ECO:0000313|Proteomes:UP000002221};
RX PubMed=21304669; DOI=10.4056/sigs.46736;
RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL Stand. Genomic Sci. 1:283-291(2009).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; CP001807; ACY48503.1; -; Genomic_DNA.
DR RefSeq; WP_012844114.1; NC_013501.1.
DR AlphaFoldDB; D0MJ45; -.
DR STRING; 518766.Rmar_1617; -.
DR KEGG; rmr:Rmar_1617; -.
DR eggNOG; COG3751; Bacteria.
DR HOGENOM; CLU_022206_1_0_10; -.
DR Proteomes; UP000002221; Chromosome.
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 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:UP000002221};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 111..211
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 219 AA; 25474 MW; C87D8F6C5B39C2BF CRC64;
MERARPIDRR RMASWIDPFI ETLARQGWAT TTEAFTPAQI QALYREAQEL DRVGAFRPAA
IGHGAEQTLR RDIRGDRIYW LDPEHPTPAQ EVYWQVVDQL RRRLNETLFL SLHDAEAHLA
IYPPGSFYRR HLDQHRGRAL RLITLVLYLN PDWRPEDGGQ LRIYPDPEAP DEGIDLLPEG
GLLVGFRSDT IPHEVLPARR ARYSLTGWLR RFDPLALLR
//
