ID   A0A0C2FIG9_9ACTN        Unreviewed;       397 AA.
AC   A0A0C2FIG9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LP52_09450 {ECO:0000313|EMBL:KIH99074.1};
OS   Streptomonospora alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Streptomonospora.
OX   NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH99074.1, ECO:0000313|Proteomes:UP000031675};
RN   [1] {ECO:0000313|Proteomes:UP000031675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX   PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA   Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA   Severinov K., Mitchell D.A.;
RT   "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT   unusual lasso Peptide from an understudied halophilic actinomycete.";
RL   Chem. Biol. 22:241-250(2015).
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:KIH99074.1}.
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DR   EMBL; JROO01000016; KIH99074.1; -; Genomic_DNA.
DR   RefSeq; WP_040272533.1; NZ_JROO01000016.1.
DR   AlphaFoldDB; A0A0C2FIG9; -.
DR   STRING; 183763.LP52_09450; -.
DR   Proteomes; UP000031675; 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:UP000031675}.
FT   DOMAIN          3..299
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          318..384
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   397 AA;  42882 MW;  7B0F538F7315060F CRC64;
     MRRIAVVGGS LAGVHAAEAL REHGFDGDVT LISAENELPY DRPPLSKEAL LNGMPMERLS
     LRAPEWYEDN AVTTRLGNAA VRLDTARRTV LLDDGTTVAY DGLVIATGSR ARRLSSTENA
     PPVQILRSIE DSLRLRERLR PGQHLVLIGA GFIGLEIAAT ARQLGLDVTI VEVGRVPLGR
     ALGDEVGAWF RALHARNGVE IVCTCTVEAI ERLGEGAVLT LSNGRVFNAD VVVAGIGASP
     VTEWLDGSGV QTTDGVVCRS DLSTSVPGVA AAGDVARWYN PLFDEEIRVE HWTNAVEQGR
     RAAHTLLGHG EAFSAVPYFW TDQYDARMRF VGRASAASEV VVKESGDDRL VALYGRDDRI
     RGAVCVNAPR ELVRYRTAIR DQVRWGDVTE TPSAIGG
//