ID   A0A2U3P4P5_9MYCO        Unreviewed;       462 AA.
AC   A0A2U3P4P5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase {ECO:0000313|EMBL:SPM38723.1};
GN   ORFNames=MNAB215_903 {ECO:0000313|EMBL:SPM38723.1};
OS   Mycobacterium numidiamassiliense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1841861 {ECO:0000313|EMBL:SPM38723.1, ECO:0000313|Proteomes:UP000240424};
RN   [1] {ECO:0000313|EMBL:SPM38723.1, ECO:0000313|Proteomes:UP000240424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB215 {ECO:0000313|EMBL:SPM38723.1,
RC   ECO:0000313|Proteomes:UP000240424};
RG   Urmite Genomes;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; FUEZ01000003; SPM38723.1; -; Genomic_DNA.
DR   RefSeq; WP_077077639.1; NZ_FUEZ01000003.1.
DR   AlphaFoldDB; A0A2U3P4P5; -.
DR   STRING; 1841861.GCA_900157365_05106; -.
DR   OrthoDB; 4213189at2; -.
DR   Proteomes; UP000240424; 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; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000240424}.
FT   DOMAIN          11..314
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          340..409
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
FT   REGION          434..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..462
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   462 AA;  49884 MW;  905F053020AC8240 CRC64;
     MSPNGFKDTG RIVIVGASLA GLRAAEALRE EGFRGQLTIV GDEPDEPYDR PPLSKQVLKG
     WVAADHTKLP RLRAVDAQWR LGVPATALDR ANQLVRLADG SEVPGDRLLI ATGVRSRRWP
     NAEEAALQGV HTVRTSTDAA RLQAALGARP RRVLIIGSGF IGSEVASVCR ELDLEVTVTE
     RGPAPLCGPL GGVIGAIAAE MQRAAGVDLR TGVSVLALEG DADGHVRRAR LSDGSTLDVD
     VVVTSLGSIR NVEWLEGAGL AAGFWGVGCD AGCRAFDINA VVTDHVFVAG DIARAPHVLY
     DYEFLAMEHW DNAVLGARVA AHNMVCDEVD RWAHLLIPQF WSAQFGVNIK SVGVPSFGDE
     IVFTQGSVQQ RRFAAAYGRR GRIVGAVTFN HAKWIDYYRD QIAHSGPFPP HPPGFDFPES
     MRVMPADFPA RGVPTEAPDV VLTGHDPSER RAEFRPRHQM SE
//