ID R2SVM6_9ENTE Unreviewed; 550 AA.
AC R2SVM6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Coenzyme A disulfide reductase {ECO:0000313|EMBL:EOH99290.1};
GN ORFNames=UAW_00440 {ECO:0000313|EMBL:EOH99290.1};
OS Enterococcus haemoperoxidus ATCC BAA-382.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158608 {ECO:0000313|EMBL:EOH99290.1, ECO:0000313|Proteomes:UP000013858};
RN [1] {ECO:0000313|EMBL:EOH99290.1, ECO:0000313|Proteomes:UP000013858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-382 {ECO:0000313|EMBL:EOH99290.1,
RC ECO:0000313|Proteomes:UP000013858};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus haemoperoxidus BAA-382.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EOH99290.1}.
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DR EMBL; AJAR01000010; EOH99290.1; -; Genomic_DNA.
DR RefSeq; WP_010760652.1; NZ_KE136479.1.
DR AlphaFoldDB; R2SVM6; -.
DR STRING; 155618.RV06_GL002632; -.
DR PATRIC; fig|1158608.3.peg.417; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000013858; Unassembled WGS sequence.
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; 59682 MW; 2564972CB161318E CRC64;
MRVVIIGGVA GGMSAATRLR RLSEEIEIIV LEKGPYVSFA NCGLPYYVSG EISERSELIL
QTPEQLKKRF NIDVYPETEA VKIDRKNKTV LTNANGKEDT ISYDKLILSP GAQPVLPTIE
GLNEATNVYT LRNVPDVDKI VATVKNEHPK KAVVIGAGFI GLEMAENLSH LGIDVTIVEA
APQILPPLDE EMAAFVEKEL KEKGITVYTG SGATEFKKAG KQIKLSSGET ISSDFTVLSI
GVKPSSDLAV VADLKTGIRG GIVVDETYQT TDPDIYAVGD AIIVKQQITQ EDALILLASP
ANRQGRQVAD VIAGVARKNQ GSIGTAIVRV FDLAAASTGL SERQLRNNNL EYKAVHTTSK
SHAGYFPGSH PIVMKLLFHP VSGKIYGAQA IGQDGVDKRI DIIATAIKAD MTVMDLPELE
FTYAPPFGSA KDPVNMIGYA ATNIVEGFSD TIQYYELKKA IENGAFLLDV RNPGELKSNG
SLPQAENIPL DELRSRLTEL PSDKEIIVSC QSGQRSYLAE RILKNNDFNV KNLDGAFQLY
STIYPQEVIK
//