ID K4IEH4_PSYTT Unreviewed; 213 AA.
AC K4IEH4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=2OG-Fe(II) oxygenase family protein {ECO:0000313|EMBL:AFU68253.1};
GN OrderedLocusNames=P700755_001320 {ECO:0000313|EMBL:AFU68253.1};
OS Psychroflexus torquis (strain ATCC 700755 / ACAM 623).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Psychroflexus.
OX NCBI_TaxID=313595 {ECO:0000313|EMBL:AFU68253.1, ECO:0000313|Proteomes:UP000008514};
RN [1] {ECO:0000313|EMBL:AFU68253.1, ECO:0000313|Proteomes:UP000008514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700755 / ACAM 623 {ECO:0000313|Proteomes:UP000008514};
RA Bowman J., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFU68253.1, ECO:0000313|Proteomes:UP000008514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700755 / ACAM 623 {ECO:0000313|Proteomes:UP000008514};
RA Feng S., Powell S.M., Bowman J.P.;
RT "The complete sequence of Psychroflexus torquis an extreme psychrophile
RT from sea-ice that is stimulated by light.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR EMBL; CP003879; AFU68253.1; -; Genomic_DNA.
DR RefSeq; WP_015023859.1; NC_018721.1.
DR AlphaFoldDB; K4IEH4; -.
DR STRING; 313595.P700755_001320; -.
DR KEGG; ptq:P700755_001320; -.
DR eggNOG; COG3751; Bacteria.
DR HOGENOM; CLU_022206_1_0_10; -.
DR OrthoDB; 9783171at2; -.
DR Proteomes; UP000008514; 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 Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT DOMAIN 110..212
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 213 AA; 25036 MW; 636E3AFD2F8913CD CRC64;
MAHTLLTEDL SFKENPLFEQ LISDLIKQNY SICDNFFELK LVDSLRERLK TLHNHSELKK
AAIGNKVNES ISKAIRGDYI QWIDEQQADS AEHLFFEAFN TFKNYLNMTC FMGILHQEFH
YAVYPVGTFY KRHLDTFQND DRRKLSMVCY LNDDSWNKTN GGELVIYPEN SDEVIIHPLP
GRVVIFESQL LEHEVRPVLN DLRLSITGWF KTR
//
