ID A0A0M3D7P0_9MICO Unreviewed; 466 AA.
AC A0A0M3D7P0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:KKX98659.1};
GN ORFNames=AAY78_04970 {ECO:0000313|EMBL:KKX98659.1};
OS Microbacterium sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1643443 {ECO:0000313|EMBL:KKX98659.1, ECO:0000313|Proteomes:UP000034223};
RN [1] {ECO:0000313|EMBL:KKX98659.1, ECO:0000313|Proteomes:UP000034223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKX98659.1,
RC ECO:0000313|Proteomes:UP000034223};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-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:KKX98659.1}.
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DR EMBL; LBCR01000026; KKX98659.1; -; Genomic_DNA.
DR RefSeq; WP_046747250.1; NZ_LBCR01000026.1.
DR AlphaFoldDB; A0A0M3D7P0; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000034223; 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; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 2..312
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 334..437
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 466 AA; 48989 MW; CAFB42590DC2B1BD CRC64;
MHLVAIGGSD AGISTALRAR ELDPSVDVTV VVADAYPNFS ICGIPYYFSR EVQPWQSLAH
RTHADLEATG MNLRLDTLAT GIDVNSRRLT VRDANGSEST IAYDELMVGT GASPSTAGIA
GLDQLGPDDG VHLLHSMGDT FALEKYLDDH QPETAIIVGA GYVGLEMAEA LTVRGLQVTQ
LQRGPEVLST LDPELGSLVH DELTRHGVDV LTGTRVEAVT REAAWITVTG THDGEALSRT
ADVVLVVVGV RPNTSLLTAA GATTGAGGAV VVDEQMRTGL PNVWAAGDGV VTHHRLLGVT
YLPLGTTAHK QGRVAGENAI GGDTRFAGSL GTQVVKVFDV VAARTGLRDH EATAAGFAPH
SHTAIADDHK RYYPGASPIS IRITGDTNDG RLLGAQLVGT RGAEISKRVD TYATALHHGM
TVAAMSDLDL SYTPPLGSPW DAVQVATQAW ERETRRSASA LRQPAA
//
