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Database: UniProt
Entry: I3TQQ6_TISMK
LinkDB: I3TQQ6_TISMK
Original site: I3TQQ6_TISMK 
ID   I3TQQ6_TISMK            Unreviewed;       219 AA.
AC   I3TQQ6;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Oxidoreductase domain protein {ECO:0000313|EMBL:AFK55094.1};
GN   OrderedLocusNames=TMO_3256 {ECO:0000313|EMBL:AFK55094.1};
OS   Tistrella mobilis (strain KA081020-065).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK55094.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK55094.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK55094.1,
RC   ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
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DR   EMBL; CP003236; AFK55094.1; -; Genomic_DNA.
DR   RefSeq; WP_014746771.1; NC_017956.1.
DR   AlphaFoldDB; I3TQQ6; -.
DR   STRING; 1110502.TMO_3256; -.
DR   KEGG; tmo:TMO_3256; -.
DR   eggNOG; COG3128; Bacteria.
DR   HOGENOM; CLU_106572_0_0_5; -.
DR   Proteomes; UP000005258; 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   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:UP000005258};
KW   Vitamin C {ECO:0000256|ARBA:ARBA00022896}.
FT   DOMAIN          117..215
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   219 AA;  23624 MW;  2D70CB693E01699B CRC64;
     MGPADRLDLS VPAFRPAPLR DEAVYPASGL RPAGFAALDG VFDDALCDAL IAAFDAVGGH
     TASLVKGVQS AGIRRSRVLW FDAESSPDPD LTAAVDRRMA EVTALLNRTR FGFALDGFDE
     AFQIARYDAE IAGGYIRHVD RGEGPRARRR KLGISIQLSA PEEYEGGDLI LEPQAVPITG
     PRRRGTAIAF PSYVVHEVTP VTRGCRYSFV AWVHGPGFV
//
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