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Database: UniProt
Entry: W0HXR0_9GAMM
LinkDB: W0HXR0_9GAMM
Original site: W0HXR0_9GAMM 
ID   W0HXR0_9GAMM            Unreviewed;       338 AA.
AC   W0HXR0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Putative 2OG-Fe(II) oxygenase {ECO:0000313|EMBL:AHF76985.1};
GN   ORFNames=Sant_1933 {ECO:0000313|EMBL:AHF76985.1};
OS   Sodalis praecaptivus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=1239307 {ECO:0000313|EMBL:AHF76985.1, ECO:0000313|Proteomes:UP000019028};
RN   [1] {ECO:0000313|EMBL:AHF76985.1, ECO:0000313|Proteomes:UP000019028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS1 {ECO:0000313|EMBL:AHF76985.1,
RC   ECO:0000313|Proteomes:UP000019028};
RX   PubMed=24407854; DOI=10.1093/gbe/evt210;
RA   Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA   Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA   Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT   "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL   Genome Biol. Evol. 6:76-93(2014).
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|RuleBase:RU003682}.
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DR   EMBL; CP006569; AHF76985.1; -; Genomic_DNA.
DR   RefSeq; WP_038668452.1; NZ_CP006569.1.
DR   AlphaFoldDB; W0HXR0; -.
DR   KEGG; sod:Sant_1933; -.
DR   PATRIC; fig|1239307.3.peg.2129; -.
DR   HOGENOM; CLU_010119_6_3_6; -.
DR   OrthoDB; 21825at2; -.
DR   Proteomes; UP000019028; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019028}.
FT   DOMAIN          179..280
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   338 AA;  37591 MW;  EECFA17AB4388026 CRC64;
     MRSSALPDTL PMLDLALFDA AGQERDAFLA RLRLAAHDIG FFYLTGHGID PDLLRQVQAV
     ALRFFALPAA DKQAVAMIHS PHFRGYNRAA SERTRGQPDW REQFDLGAER AALPRDATLP
     AWTRLQGPNL WPAALPEMQP LLTRWQQEMT RMALRLLRAF AESLSLPGGA FDPLYGEKPN
     EHVKLIRYPG RKEGESRQGV GPHKDSGFLS FLLQDENKGL QVEIAPGKWI DVEPKTGTLV
     VNIGELLELA TNGYLRATVH RVVSPPAERE RLSIAFFLGA QLDAVVPIYP LPPALSIEAP
     GAASDPDNPL LRDVGWNYLK GRLRSHPDVA ERYYSDLL
//
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