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Database: UniProt
Entry: A0A0T1SHY0_9ACTN
LinkDB: A0A0T1SHY0_9ACTN
Original site: A0A0T1SHY0_9ACTN 
ID   A0A0T1SHY0_9ACTN        Unreviewed;       404 AA.
AC   A0A0T1SHY0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KQX53345.1};
GN   ORFNames=ASD33_09190 {ECO:0000313|EMBL:KQX53345.1};
OS   Streptomyces sp. Root1304.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1736450 {ECO:0000313|EMBL:KQX53345.1, ECO:0000313|Proteomes:UP000051136};
RN   [1] {ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|Proteomes:UP000051136};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQX53345.1, ECO:0000313|Proteomes:UP000051136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1304 {ECO:0000313|EMBL:KQX53345.1,
RC   ECO:0000313|Proteomes:UP000051136};
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   -!- 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:KQX53345.1}.
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DR   EMBL; LMEP01000012; KQX53345.1; -; Genomic_DNA.
DR   RefSeq; WP_056560544.1; NZ_LMEP01000012.1.
DR   AlphaFoldDB; A0A0T1SHY0; -.
DR   STRING; 1736450.ASD33_09190; -.
DR   Proteomes; UP000051136; 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; PR00469; PNDRDTASEII.
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:UP000051136}.
FT   DOMAIN          10..295
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          319..402
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   404 AA;  42215 MW;  674DE23BB66D2BAF CRC64;
     MSEQKQAQQH VVIVGAGMAG VQTAVALREQ GFTGPVTLIG AEPHQPYDRP PLSKAVLLGK
     AEDSAFDIDF EDLRVELRLG LDVTGLRAAD HEVDTEAGPV GYDALVVATG AQPVTLPGSE
     GVPGVHLLRT LDDAVRLGPV LEHRHDVVVV GAGWIGAEFA TAARAAGCAV TVVEAAGLPL
     TGALPAEVAT PMAEWYAANG AELLTHARVA TVEPGRVVLA DGRELPADAV VVGIGARPAT
     GWLAGSGIAL DPGGAVTADE RLRTSLPDVY AVGDCASFPS ARYGERLLVH HWDNALQGPR
     TVAGEITGAG DAPYDPVPYF WSEQFGRFVQ YAGHHAHADE LLWRGDPADE AWSVLWLRDG
     VPVALLAVGR PRDLAQGRKL IETATAVDPA RAADPSVPLK AAVR
//
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