ID   A0A2S8WQL5_9MICC        Unreviewed;       408 AA.
AC   A0A2S8WQL5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:PQZ92846.1};
GN   ORFNames=CQ018_10210 {ECO:0000313|EMBL:PQZ92846.1};
OS   Arthrobacter sp. MYb227.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1848601 {ECO:0000313|EMBL:PQZ92846.1, ECO:0000313|Proteomes:UP000239972};
RN   [1] {ECO:0000313|EMBL:PQZ92846.1, ECO:0000313|Proteomes:UP000239972}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MYb227 {ECO:0000313|EMBL:PQZ92846.1,
RC   ECO:0000313|Proteomes:UP000239972};
RA   Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA   Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA   Kaleta C., Schulenburg H.;
RT   "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT   from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:PQZ92846.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; PCPT01000004; PQZ92846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8WQL5; -.
DR   OrthoDB; 1145at2; -.
DR   Proteomes; UP000239972; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000239972}.
FT   DOMAIN          6..303
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          323..408
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   408 AA;  44119 MW;  31B450A989C4EDAE CRC64;
     MSQTQRVVVV GGGLAGVKTA EALRTSGFKG SICIVAAEDQ LPYERPPLSK GYLMGKTEFS
     AQVVHPEEWF TENAVELRRK TRVTAIDRIA KRVELSDGTR LHYDTLVLAT GSRPRRIPLL
     GAEAQGVHYL RTKNNADALR SVFGEGKRVV FVGGGWIGLE VAAAARAAGC TVTILERLSL
     PLLPILGEEV AQVFADLHRS HGVDLHTAVD VKSIQTQDGV VTGVELGTGE VFPADAVVIA
     VGAIPSVELA QEAGLEVENG VLVDESLRSS DPSIFAVGDI ANQQHPFLGR RLRVEHWATA
     LNQPKTVAAA IMGEPASYTD LPYFFTDQYD LGMEYIGNAQ PGSYDQVVLR GDLAKREFLA
     FWLSQGVVIA GMNVNIWDVS ESIQKLIRSQ KQVDLKKLAD PSVALETL
//