ID K9AL95_9STAP Unreviewed; 440 AA.
AC K9AL95;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Coenzyme A disulfide reductase {ECO:0000313|EMBL:EKU48069.1};
DE EC=1.8.1.14 {ECO:0000313|EMBL:EKU48069.1};
GN ORFNames=C273_06403 {ECO:0000313|EMBL:EKU48069.1};
OS Staphylococcus massiliensis S46.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1229783 {ECO:0000313|EMBL:EKU48069.1, ECO:0000313|Proteomes:UP000009885};
RN [1] {ECO:0000313|EMBL:EKU48069.1, ECO:0000313|Proteomes:UP000009885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S46 {ECO:0000313|EMBL:EKU48069.1,
RC ECO:0000313|Proteomes:UP000009885};
RX PubMed=23929469;
RA Srivastav R., Singh A., Jangir P.K., Kumari C., Muduli S., Sharma R.;
RT "Genome Sequence of Staphylococcus massiliensis Strain S46, Isolated from
RT the Surface of Healthy Human Skin.";
RL Genome Announc. 1:e00553-13(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:EKU48069.1}.
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DR EMBL; AMSQ01000008; EKU48069.1; -; Genomic_DNA.
DR RefSeq; WP_009383496.1; NZ_AMSQ01000008.1.
DR AlphaFoldDB; K9AL95; -.
DR STRING; 1229783.C273_06403; -.
DR PATRIC; fig|1229783.3.peg.1294; -.
DR eggNOG; COG0446; Bacteria.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000009885; 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 GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR017758; CoA_disulphide_reductase.
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 NCBIfam; TIGR03385; CoA_CoA_reduc; 1.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EKU48069.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009885}.
FT DOMAIN 3..283
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 326..424
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 440 AA; 49438 MW; 8B797300A0A3D9B0 CRC64;
MSKIVVVGAV AGGATCASQI RRLNDENAIT IYEKDRDMSF ANCGLPYYLG DVIEKRESVL
AIEPKDFKDK KNIDVHTYHE VIAVDSQAKT VTVKNHQTGE TFEDTYDYLI LSPGCRAKSL
GFDADFIFTL RNMEDTDRIN DYIEAHDVKR VLLVGAGYIS LEMLENMYHR GLKPTLIHRS
DQVNKLMDQD MNQVILDAMD ERDIPYYLNE EIDSIEGHDV TFKSGKTESF DMIIEGVGVA
PNSEFLKGSG VERDDKGYVP VNEKFETNAD GIYALGDVIT SFYRHVDLKA HVPLAFGAHR
AASIIAEQLE GRSEIVFKGF VGANIVKFFQ YTLASTGVTV KDLDQFDYDV VNHTSNTHAG
YYPDNSKMHI RVYFEKSSRK ILRAAAVGEK GVDKRIDVIT MAIIGEQTID DLTEFEVAYA
PPYSHPKDII NMVGYKARNK
//
