ID A0A0U2WK52_9ENTE Unreviewed; 550 AA.
AC A0A0U2WK52;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:ALS35606.1};
GN ORFNames=ATZ35_00045 {ECO:0000313|EMBL:ALS35606.1};
OS Enterococcus rotai.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=118060 {ECO:0000313|EMBL:ALS35606.1, ECO:0000313|Proteomes:UP000067523};
RN [1] {ECO:0000313|EMBL:ALS35606.1, ECO:0000313|Proteomes:UP000067523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26678 {ECO:0000313|EMBL:ALS35606.1,
RC ECO:0000313|Proteomes:UP000067523};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP013655; ALS35606.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U2WK52; -.
DR STRING; 118060.ATZ35_00045; -.
DR Proteomes; UP000067523; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd01524; RHOD_Pyr_redox; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
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 InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF7; NITRIC OXIDE REDUCTASE FLRD-NAD(+) REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
FT DOMAIN 461..549
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 550 AA; 59678 MW; 317E46C7E6E4BAB6 CRC64;
MRVVIIGGVA GGMSAATRLR RLSEEIEIIV LEKGPYVSFA NCGLPYYVSG EISERSELIL
QTPEQLKKRF NINVYPETEA ININRKNKTV LSNSKGKEEV ISYDKLILSP GAQPVIPTIK
GLDEATNVYT LRNVPDVDKI VATVKNEQPK RAVVIGAGFI GLEMAENLQH LGIDVTIVEA
APQILPPLDE EMAAFVEKEL KEKGITVFTG AGATEFKESG NVIELSSGES ISSDFTILSI
GVKPSSDLAV AADLKTGLRG GIVVDETYQT NDPDIYAVGD AIVVKQQITK EDALISLASP
ANRQGRQVAD VIVGVTRKNK GSISTAIVRV FDLAAASTGL SERQLRSSNL EYKAVHTTSK
SHAGYFPGSH PIVMKLLFHP MSGKIYGAQA IGQDGVDKRI DIIATAIKAD MTVMDLPELE
FTYAPPFGSA KDPVNMIGYA AANIVEGFSE NIQYYELKET IENGAILLDV RNPGELKNNG
SLPHAENIPL DELRDRLSEL PGNKEIIVSC QSGQRSYLAE RILKNNGFDV KNLDGAFQIY
STIYPQEVIK
//
