ID A0A0Q8AP58_9MICO Unreviewed; 340 AA.
AC A0A0Q8AP58;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KQZ82261.1};
GN ORFNames=ASD56_15440 {ECO:0000313|EMBL:KQZ82261.1};
OS Microbacterium sp. Root166.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736478 {ECO:0000313|EMBL:KQZ82261.1, ECO:0000313|Proteomes:UP000051650};
RN [1] {ECO:0000313|Proteomes:UP000051650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root166 {ECO:0000313|Proteomes:UP000051650};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ82261.1, ECO:0000313|Proteomes:UP000051650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root166 {ECO:0000313|EMBL:KQZ82261.1,
RC ECO:0000313|Proteomes:UP000051650};
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:KQZ82261.1}.
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DR EMBL; LMGL01000004; KQZ82261.1; -; Genomic_DNA.
DR RefSeq; WP_055967899.1; NZ_LMGL01000004.1.
DR AlphaFoldDB; A0A0Q8AP58; -.
DR STRING; 1736478.ASD56_15440; -.
DR OrthoDB; 21825at2; -.
DR Proteomes; UP000051650; 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:UP000051650}.
FT DOMAIN 172..274
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 340 AA; 37529 MW; 748A552F1E0DBD18 CRC64;
MSDLNLPILD LSQLDEGPEA AARFRDDLRA ATHDVGFFYL TGTGIPAELE ARLERAARDF
FALPDADKLA IENVKSPHFR GYTRVGGERT QGKVDWREQI DIGPEREAVT DSDAPDFSRL
IGPNLWPDAQ PELREVVSQW HDHLSGVARK LLRAWALSLG APETYFDEHF GEPSTLIKIV
RYPGKEDPTP QQGVGAHKDS GVLTLLWVEP GKGGLQVERD GEWVDAPPVP GAFVVNIGEL
LEYATQGYLI ATKHRVISPR YPDDRISVPF FFNPALDKRL PLIELPEELA SEARGVTKDP
GNPIHALYGE NALKSRLRAH PDVAELHHAD LLAARAAASA
//
