ID A0A0X3VDZ6_9ACTN Unreviewed; 477 AA.
AC A0A0X3VDZ6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:KUL42834.1};
GN ORFNames=ADL12_09380 {ECO:0000313|EMBL:KUL42834.1};
OS Streptomyces regalis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68262 {ECO:0000313|EMBL:KUL42834.1, ECO:0000313|Proteomes:UP000053923};
RN [1] {ECO:0000313|Proteomes:UP000053923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3151 {ECO:0000313|Proteomes:UP000053923};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) 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}.
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:KUL42834.1}.
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DR EMBL; LLZG01000047; KUL42834.1; -; Genomic_DNA.
DR RefSeq; WP_062700476.1; NZ_LLZG01000047.1.
DR AlphaFoldDB; A0A0X3VDZ6; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000053923; 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; 3.50.50.60; 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 Reference proteome {ECO:0000313|Proteomes:UP000053923}.
FT DOMAIN 5..321
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 343..448
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 477 AA; 50413 MW; 3F31B8D2E5AC1D1D CRC64;
MARKRIVAIG GSDAGISAAL RARELDPDSE VTVVVADAYP NFSICGIPYY VSGEVGHWSD
LAHRTLADLK ATGMQVRTDT LATGIDVASK RLAVRDADGR TEELPYDALI IGTGAVSVRP
PIEGLTGPGA LGPQDGVHLL HSMGDTFEVM QSIAERRPRS AVVIGAGYIG LEMAEALTTR
GLRVTQIEAL PEVLPTVDPE LGALVHAELT SHGVEVMTGT QVTEIARSHS GETPHVRAAG
PDGTTFTQTA DLVLVVVGVH PDTKLVTTAG AKLGAKGAID VDEHMRTSLP DVYAAGDCAV
THHRLLGKTW LPLGTTAHKQ GRIAGENALG GYRWFAGSLG TQVVKVFDLV AARTGLRDHE
ARAAARDWAP ATTGSRPDDH KAYYPGATPI SIRVTGDTSS GLLLGAQLVG RLGAEISKRV
DTYATALFHG MPVDGLNELD LSYTPPLGSP WDAVQVAAQA WMSEHQLDVQ RRMLRTP
//
