ID I6TAD0_ENTHA Unreviewed; 551 AA.
AC I6TAD0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Coenzyme A disulfide reductase {ECO:0000313|EMBL:AFM70214.1};
GN OrderedLocusNames=EHR_06365 {ECO:0000313|EMBL:AFM70214.1};
OS Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=768486 {ECO:0000313|EMBL:AFM70214.1, ECO:0000313|Proteomes:UP000002895};
RN [1] {ECO:0000313|EMBL:AFM70214.1, ECO:0000313|Proteomes:UP000002895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB
RC 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R
RC {ECO:0000313|Proteomes:UP000002895};
RX PubMed=22933757; DOI=10.1128/JB.01075-12;
RA Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT a model organism for the study of ion transport, bioenergetics, and copper
RT homeostasis.";
RL J. Bacteriol. 194:5126-5127(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP003504; AFM70214.1; -; Genomic_DNA.
DR RefSeq; WP_010737035.1; NZ_KB946228.1.
DR AlphaFoldDB; I6TAD0; -.
DR KEGG; ehr:EHR_06365; -.
DR PATRIC; fig|768486.10.peg.506; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_003291_1_2_9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000002895; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; 1.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000002895}.
FT DOMAIN 460..546
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 551 AA; 59803 MW; AA7DE7973CAC0109 CRC64;
MKIVIVGGVA GGMSAATRLR RLKEDAEIVV FEKGPYVSFA NCGLPYYLSG EISERENLLV
QTPESLAARF QLDVRPNHEV TAVYPDEKKV EVLSDGKKWQ ESYDVLLLSP GAKPVRPAIS
GLAEAKNVYT VRNVPDIDMV MNALEEQPKK AVVVGAGFIG LEMAENLKKR GLAVSIVELA
PHVLPSLDEE MAVHIQNELI KQGVHVQTKR SVTAFEHGGK QLRLDDGTTI DSDLTILSVG
VQPDSTLAKM AGLETGLRGG IVVNEHYQTS DPSIYAVGDA IVVKQQITGA DALISLASPA
NRQGRQAADN IAGIVRNNRG SLGTSIVRVF DLAAASTGLT ERMAQQANLP FSVVHVSGKD
HASYYPEATD ILLKLIFHPK TGEIYGAQGV GAKGVDKRID SLATAIKGQL TIFDLPELEF
TYAPPFGSAK DPVNMLGYVA MNVAEGLSET IQWHELPEAL AQGKILLDVR NEGELQNGAF
KDALNIPLND LRCRLAELDR EKEYIVSCHS GLRSYLAERI LKQAGFHVQN LDGAFALYHA
VRPEDLIYPE K
//
