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Database: UniProt
Entry: A0A0Q8LGE5_9MICO
LinkDB: A0A0Q8LGE5_9MICO
Original site: A0A0Q8LGE5_9MICO 
ID   A0A0Q8LGE5_9MICO        Unreviewed;       347 AA.
AC   A0A0Q8LGE5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KRB36044.1};
GN   ORFNames=ASD93_07955 {ECO:0000313|EMBL:KRB36044.1};
OS   Microbacterium sp. Root180.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736483 {ECO:0000313|EMBL:KRB36044.1, ECO:0000313|Proteomes:UP000050802};
RN   [1] {ECO:0000313|EMBL:KRB36044.1, ECO:0000313|Proteomes:UP000050802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root180 {ECO:0000313|EMBL:KRB36044.1,
RC   ECO:0000313|Proteomes:UP000050802};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB36044.1, ECO:0000313|Proteomes:UP000050802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root180 {ECO:0000313|EMBL:KRB36044.1,
RC   ECO:0000313|Proteomes:UP000050802};
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   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
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:KRB36044.1}.
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DR   EMBL; LMHS01000003; KRB36044.1; -; Genomic_DNA.
DR   RefSeq; WP_056121134.1; NZ_LMHS01000003.1.
DR   AlphaFoldDB; A0A0Q8LGE5; -.
DR   STRING; 1736483.ASD93_07955; -.
DR   OrthoDB; 21825at2; -.
DR   Proteomes; UP000050802; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; 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   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
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:UP000050802}.
FT   DOMAIN          172..280
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   347 AA;  38286 MW;  E96668C036B3D6E3 CRC64;
     MTDLNLPILD LSELDHGPEA AARFRDDLRA ATHQVGFFYL TGTGVTPDLE ARLHRAARDF
     FALPEADKLA IENVKSPHFR GYTRIGGERT QGKVDWREQI DIGPEREAIS DPEAADFFRL
     IGPNLWPAAQ PELQDVVSEW HDHLSGVARK LLRAWALSLG APENYFDEHF GEPSTLIKIV
     RYPGKEDPTP QQGVGAHKDS GVLTLLWVEP GKGGLQVQRQ DGATGEWHWV DAPPVPGAFV
     VNIGELLEYA TQGYLVATNH RVISPRYPDD RISVPFFFNP ALDKRLPLIE LPVELAGEAR
     GVTQDPANPI HALYGENALK SRLRAHPDVA AIHHADLVAT RASASTS
//
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