ID M7P281_9BACL Unreviewed; 447 AA.
AC M7P281;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Coenzyme A disulfide reductase {ECO:0000313|EMBL:EMR07990.1};
DE EC=1.8.1.14 {ECO:0000313|EMBL:EMR07990.1};
GN Name=cdr {ECO:0000313|EMBL:EMR07990.1};
GN ORFNames=C772_00319 {ECO:0000313|EMBL:EMR07990.1};
OS Bhargavaea cecembensis DSE10.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Bhargavaea.
OX NCBI_TaxID=1235279 {ECO:0000313|EMBL:EMR07990.1, ECO:0000313|Proteomes:UP000011919};
RN [1] {ECO:0000313|EMBL:EMR07990.1, ECO:0000313|Proteomes:UP000011919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE10 {ECO:0000313|EMBL:EMR07990.1,
RC ECO:0000313|Proteomes:UP000011919};
RX PubMed=23766406;
RA Shivaji S., Ara S., Begum Z., Ruth M., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Bhargavaea cecembensis Strain DSE10T, Isolated
RT from a Deep-Sea Sediment Sample Collected at a Depth of 5,904 m from the
RT Chagos-Laccadive Ridge System in the Indian Ocean.";
RL Genome Announc. 1:e00346-13(2013).
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:EMR07990.1}.
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DR EMBL; AOFT01000001; EMR07990.1; -; Genomic_DNA.
DR RefSeq; WP_008296811.1; NZ_AOFT01000001.1.
DR AlphaFoldDB; M7P281; -.
DR STRING; 1235279.C772_00319; -.
DR PATRIC; fig|1235279.3.peg.330; -.
DR eggNOG; COG0446; Bacteria.
DR OrthoDB; 9792592at2; -.
DR Proteomes; UP000011919; Unassembled WGS sequence.
DR GO; GO:0050451; F:CoA-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000313|EMBL:EMR07990.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011919}.
FT DOMAIN 1..293
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 327..425
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 447 AA; 48124 MW; A2B9445D7AE90765 CRC64;
MKIVVIGAVA GGATVSSQIR RFLPDAHITL IGKDSELGFG TCGMPYVLGG VIGSADDLVH
ATPEGFGKEK SIDVRLLHEA TKIDRAKKEV HVCNMETGKT DILPYDKLIL SPGGRARKPA
VPGKPGIPLF TLRHFGDLEQ FGNFLDEEKP ASCIVVGGGF IGVELAENFR HRGIETALIE
HNEHVMPIGD KDMSELLAEE MERNGVTLHL GRELRMIEGR TVTLDDGTEM EADFIATAVG
LEPNTLLAKE AGLEIGPTGG IATDPFMRTN DPDIYAIGDA AEGRDWFTGK PKRVPLSWPA
HRASFIVANH LAGGDTEMDG LLGTSITKLF SLTAGMTGMT EKMLKEEGMN YETVIHKSRS
NAGYYPDSGK LVLKVHYDPD TRAIYGAQAV GEKGADKRID VIATAIRGGL TVDDLSAIET
AYAPPYGSPK DPVNMLGYRA MKSSNQH
//
