ID A0A0V8HDQ9_9BACI Unreviewed; 449 AA.
AC A0A0V8HDQ9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase {ECO:0000313|EMBL:SCC26605.1};
GN ORFNames=GA0061094_3589 {ECO:0000313|EMBL:SCC26605.1};
OS [Bacillus] enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Rossellomorea.
OX NCBI_TaxID=1402860 {ECO:0000313|EMBL:SCC26605.1, ECO:0000313|Proteomes:UP000181997};
RN [1] {ECO:0000313|EMBL:SCC26605.1, ECO:0000313|Proteomes:UP000181997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGD-1123 {ECO:0000313|EMBL:SCC26605.1,
RC ECO:0000313|Proteomes:UP000181997};
RA Seilhamer J.J.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR EMBL; FMAU01000004; SCC26605.1; -; Genomic_DNA.
DR RefSeq; WP_058299505.1; NZ_KQ758485.1.
DR AlphaFoldDB; A0A0V8HDQ9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000181997; 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 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 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857}.
FT DOMAIN 1..304
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 330..427
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 449 AA; 49153 MW; 0713965CF5865A10 CRC64;
MKIAVIGSTH AGTAAVTNMA NMYPEADITV YEKNDNVSFL SCGLALYVGG VVEDPQGLFY
SSPEQLRNLG ITMKMQHAVQ EIDTARKQIK AVNLVTGEEV NDSYDKLVMS TGSWPIIPPI
DGIKLDNVLL AKNFNQANTI IEKSRDAKHV TIVGAGYIGV ELVEAFQQAG KKVTLIDGVD
RILNKYLDQE FTDQVEQEFI DRGVELRLGE TVTRFEGETS VESVVTNKGR VETDMVIMCV
GFRPNTELLK GKVDMLSNGA ITVDDYMRTS DPDILAAGDC CAVKYNPTGQ AAYIPLATNA
VRMGTLVARN LIEPVMKNVG TQGTSGLHIY DLNMASTGLT ETSARAMDIH VKSITISEKH
RPEFMPTAEN VLLKVSYLPE SRKIIGAQVL SKADVTQSIN TLSVCIQTGM TIDELAFVDF
FFQPHFNQPW NFLNKAGLAA ADTRKLELV
//
