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Database: UniProt
Entry: A0A0Q5LJF7_9BURK
LinkDB: A0A0Q5LJF7_9BURK
Original site: A0A0Q5LJF7_9BURK 
ID   A0A0Q5LJF7_9BURK        Unreviewed;       323 AA.
AC   A0A0Q5LJF7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=2OG-Fe(II) oxygenase {ECO:0000313|EMBL:KQR50381.1};
GN   ORFNames=ASF94_06070 {ECO:0000313|EMBL:KQR50381.1};
OS   Acidovorax sp. Leaf160.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1736280 {ECO:0000313|EMBL:KQR50381.1, ECO:0000313|Proteomes:UP000051403};
RN   [1] {ECO:0000313|EMBL:KQR50381.1, ECO:0000313|Proteomes:UP000051403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf160 {ECO:0000313|EMBL:KQR50381.1,
RC   ECO:0000313|Proteomes:UP000051403};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR50381.1, ECO:0000313|Proteomes:UP000051403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf160 {ECO:0000313|EMBL:KQR50381.1,
RC   ECO:0000313|Proteomes:UP000051403};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|RuleBase:RU003682}.
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:KQR50381.1}.
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DR   EMBL; LMOV01000023; KQR50381.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5LJF7; -.
DR   STRING; 1736280.ASF94_06070; -.
DR   Proteomes; UP000051403; Unassembled WGS sequence.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; 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   PANTHER; PTHR47990:SF27; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
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:UP000051403}.
FT   DOMAIN          178..289
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   323 AA;  36479 MW;  0D4F5899DB0FD4B1 CRC64;
     MIAELEKESR MGGLGRETTA REVRCIDMSD FEARKEEIAE ALWSASVEIG FFQVTGHGIP
     LDDIRAAFAR AERLFALPAE TKAQWPLARN AGWEHKAQIR PSTRTPDQKE SYQVTRPRMA
     GLWPTEEELP GFQEATLRFE AQCWRVAMQL LSCFAWKLGF APDFFTRAHD PSVPAYQSTL
     RMLHYFAVDP ALKDELGLWR AGAHTDFDCL TLLFQRAGQG GLQVLPGKEM EGRAWTPVDP
     VEGVITCNIG DMLTRWSDDA LPSNFHRVRN PLPHEYQGAR YSLAFFAQAN EDAVIAGPAQ
     RHPPISAGDY LRQRISANFS HRY
//
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