ID A0A2K8VGN4_9FLAO Unreviewed; 491 AA.
AC A0A2K8VGN4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN ORFNames=BTO06_15470 {ECO:0000313|EMBL:AUC16463.1};
OS Tenacibaculum sp. SZ-18.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=754423 {ECO:0000313|EMBL:AUC16463.1, ECO:0000313|Proteomes:UP000232695};
RN [1] {ECO:0000313|EMBL:AUC16463.1, ECO:0000313|Proteomes:UP000232695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZ-18 {ECO:0000313|EMBL:AUC16463.1,
RC ECO:0000313|Proteomes:UP000232695};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-2016) 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; CP019335; AUC16463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8VGN4; -.
DR OrthoDB; 269774at2; -.
DR Proteomes; UP000232695; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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 Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19849; PHOSPHOLIPASE A-2-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR19849:SF0; PHOSPHOLIPASE A-2-ACTIVATING PROTEIN; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00702; P4Hc; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 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:UP000232695};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Vitamin C {ECO:0000256|ARBA:ARBA00022896};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 95..196
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT REPEAT 249..282
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ SEQUENCE 491 AA; 57197 MW; 97C46A995250FAC7 CRC64;
MKKIIDIFPD KNYYCKIIKG AFSDDFCNAL ITKNKNSFLQ ATTHYPVSYR NNERQVIDDY
ELSDYLFSTI KDFIPVNISV KAISDKEIGS WKLKKLNSKI RFCRYLPNQY FHKHLDGVFY
LSSYEQSKLT FMIYLNGCDE FEGGRTLFFN SKDNDDIIAS YKPVKGDLLI FDHNIWHSGE
RVESGEKYVL RSDIIYSKTE DDINYEVPFG EGHLGYIWQA VNFNNKLITS GRDRFLKTWG
LDGVKISEVE THSNSVTTLM RFDQKTLISG SRDYLVKLWR INEKFDYDCF LTLGDGKSTV
LSLCKINSDE FICADASGEL RIYNLKGNLI KRIKAHNDWI WSVIKISDNI VVTVSEDGTM
VFRDLNSNEV LMFWKGINIP INSIAFDGFN FIYIGLYDGT IVKFRFDTEN KELEKEYVKS
CHRGIIRKLV YEKGKLYSAG EDNALNVWDT DNFENLYRYN HKNFVQDVAL FTDCFVSVSY
DGRIIKHKKI L
//
