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Database: UniProt
Entry: A0A095UGS2_9GAMM
LinkDB: A0A095UGS2_9GAMM
Original site: A0A095UGS2_9GAMM 
ID   A0A095UGS2_9GAMM        Unreviewed;       200 AA.
AC   A0A095UGS2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Fe2OG dioxygenase domain-containing protein {ECO:0000259|PROSITE:PS51471};
GN   ORFNames=HA49_10305 {ECO:0000313|EMBL:KGD73633.1};
OS   Tatumella morbirosei.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Tatumella.
OX   NCBI_TaxID=642227 {ECO:0000313|EMBL:KGD73633.1, ECO:0000313|Proteomes:UP000029577};
RN   [1] {ECO:0000313|EMBL:KGD73633.1, ECO:0000313|Proteomes:UP000029577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 23360 {ECO:0000313|EMBL:KGD73633.1,
RC   ECO:0000313|Proteomes:UP000029577};
RA   Smits T.H., Palmer M., Venter S.N., Duffy B., Steenkamp E.T., Chan W.Y.,
RA   Coutinho T.A., Coetzee M.P., De Maayer P.;
RT   "The draft genome of the Tatumella morbirosei type strain, LMG23360T
RT   isolated from pineapple rot.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGD73633.1}.
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DR   EMBL; JPKR02000002; KGD73633.1; -; Genomic_DNA.
DR   RefSeq; WP_038019974.1; NZ_JPKR02000002.1.
DR   AlphaFoldDB; A0A095UGS2; -.
DR   STRING; 642227.HA49_10305; -.
DR   eggNOG; COG3751; Bacteria.
DR   Proteomes; UP000029577; Unassembled WGS sequence.
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:UP000029577};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   DOMAIN          95..191
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   200 AA;  23132 MW;  AD0CA670361179C1 CRC64;
     MLDSEVLVQQ LCEQGWFYQQ NVLDAALVSQ LAEICHSRTF LQAGIGQGVK NIINESIRSD
     SISWIDKDEQ LPAIRDYLGL VETIRQLLNR EFYLGLNDFE GHFSRYPSGA YYKPHYDCFA
     NDKRRAVTLI MYINQNWHPQ DGGQLCLHLP EGERLIEPVA GSVICFLSEQ ILHEVKPAHK
     ERMALTGWYI RNNGQDYYYS
//
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