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Database: UniProt
Entry: A0A0Q8PP02_9ACTN
LinkDB: A0A0Q8PP02_9ACTN
Original site: A0A0Q8PP02_9ACTN 
ID   A0A0Q8PP02_9ACTN        Unreviewed;       404 AA.
AC   A0A0Q8PP02;
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=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KRB75388.1};
GN   ORFNames=ASE03_15480 {ECO:0000313|EMBL:KRB75388.1};
OS   Kitasatospora sp. Root187.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1736486 {ECO:0000313|EMBL:KRB75388.1, ECO:0000313|Proteomes:UP000051829};
RN   [1] {ECO:0000313|EMBL:KRB75388.1, ECO:0000313|Proteomes:UP000051829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root187 {ECO:0000313|EMBL:KRB75388.1,
RC   ECO:0000313|Proteomes:UP000051829};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB75388.1, ECO:0000313|Proteomes:UP000051829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root187 {ECO:0000313|EMBL:KRB75388.1,
RC   ECO:0000313|Proteomes:UP000051829};
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:KRB75388.1}.
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DR   EMBL; LMHX01000003; KRB75388.1; -; Genomic_DNA.
DR   RefSeq; WP_057229130.1; NZ_LMHX01000003.1.
DR   AlphaFoldDB; A0A0Q8PP02; -.
DR   STRING; 1736486.ASE03_15480; -.
DR   Proteomes; UP000051829; 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:UP000051829}.
FT   DOMAIN          5..296
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          316..400
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   404 AA;  43316 MW;  32DD271D1F315A1B CRC64;
     MKTGYVVVGA SLAGAKAVET LRAEGFEGSI TLIGAETERP YERPPLSKGY LMGKTAREKI
     YVHPAEWYAE HRVDLVLGAV ATAIDPAGHT VSLADGSRLG YAKLLLTTGS SPRRLTVPGA
     DGEQVLYLRT VQDSERIKAA IRPGARIVVI GAGWIGLETA AAAREAGAEV TVLEAAELPL
     LRVLGREAAQ VFAELHRAHG VELRFGVQVT ELTGDGVRLA DGELVPADAV VVGIGITPNT
     ELAEAAGLTV DNGIRTDQYL ATSAPDIYAA GDVANALHPL YGRPIRVEHW ANALHQPRTA
     ARSMLGQEAV HDRVPYFFTD QYELGMEYTG YVQPDGFDRV VFRGDRAGRE FIAFWLDGGR
     VLAGMNVNVW DVTDPIRELV RSGRQVDPDA LADPAVPLDR VGLG
//
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