ID   A0A1M5SAL4_9FIRM        Unreviewed;       820 AA.
AC   A0A1M5SAL4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:SHH35490.1};
GN   ORFNames=SAMN02744040_01694 {ECO:0000313|EMBL:SHH35490.1};
OS   Tepidibacter thalassicus DSM 15285.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Tepidibacter.
OX   NCBI_TaxID=1123350 {ECO:0000313|EMBL:SHH35490.1, ECO:0000313|Proteomes:UP000242520};
RN   [1] {ECO:0000313|Proteomes:UP000242520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15285 {ECO:0000313|Proteomes:UP000242520};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the sulfur carrier protein TusA family.
CC       {ECO:0000256|ARBA:ARBA00008984}.
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DR   EMBL; FQXH01000018; SHH35490.1; -; Genomic_DNA.
DR   RefSeq; WP_072725525.1; NZ_FQXH01000018.1.
DR   AlphaFoldDB; A0A1M5SAL4; -.
DR   STRING; 1123350.SAMN02744040_01694; -.
DR   OrthoDB; 9802028at2; -.
DR   Proteomes; UP000242520; Unassembled WGS sequence.
DR   GO; GO:0050451; F:CoA-disulfide reductase (NADP) activity; IEA:InterPro.
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   CDD; cd01524; RHOD_Pyr_redox; 1.
DR   Gene3D; 3.40.1260.10; DsrEFH-like; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   Gene3D; 3.30.110.40; TusA-like domain; 1.
DR   InterPro; IPR017758; CoA_disulphide_reductase.
DR   InterPro; IPR032836; DsrE2-like.
DR   InterPro; IPR027396; DsrEFH-like.
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   InterPro; IPR001455; TusA-like.
DR   InterPro; IPR036868; TusA-like_sf.
DR   NCBIfam; TIGR03385; CoA_CoA_reduc; 1.
DR   PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR43031:SF7; NITRIC OXIDE REDUCTASE FLRD-NAD(+) REDUCTASE; 1.
DR   Pfam; PF13686; DrsE_2; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF01206; TusA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF75169; DsrEFH-like; 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   SUPFAM; SSF64307; SirA-like; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS01148; UPF0033; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000242520}.
FT   DOMAIN          465..552
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   820 AA;  89934 MW;  8D61BAD1468700E0 CRC64;
     MNKKIVIVGG VAGGASTAAR LRRLDENAQI IMFERGEYIS FANCGLPYYI GGTITERESL
     LVQTVEGMSK KFNMDIRNLS EVTKINRDKK TVTVKNLKTG EIYEENYDYL VLSPGASPIK
     PPIPGIEETD NLFTLRNIPD TDNIKEFIDT KKPKKAVVIG GGFIGIEMAE NLHDKGIEVT
     LVEMANQIMA PVDFEMACIL HSHIKDKGVN LILEDGVKEF KNKGKKILLS SGKEINTDMI
     ILSIGVRPES SLAKDAGLEL GERGTIKVDE TLRTSDKSIY ALGDAVEVKD YINGKPTMIP
     LAWPANRQGR LVADHINGKN VKYNGTMGTS IAKVFDMTVA STGNNEKTLK KLGIKYKSIH
     IHPGSHAGYY PGSFPITLKL IFDPENGKIF GAQAVGYDGV DKRIDVIATA IKGNLTVFDL
     PDLELAYAPP YSSAKDPVNM AGYVASNIIE GLVDIVYWNE IDEIIKNGGI LIDVRDEIER
     DMGYIEGSIN IPLGELRNRL NEIPKDKEIY VTCQVGLRGY LAARILMQNG YKVKNLDGGY
     KTYSSVFSSD FENNCTPDID DSGVAHIDTS CLEEIVPKIS LNACGLQCPG PIMKVYQNIE
     NMSEGEVLEV TASDPGFAKD IKSWCEKTGN TLLKSNFENK VFKALIQKGK KNNINNNTNI
     LQKNKDGATM VVFSGDLDKA IASFIIASGA ASMGKKVTMF FTFWGLNVLR KENSPKVEKD
     ILEKMFSMMM PKGPSKLPLS KMNMAGMGPK MINYVMEKKN VDSLETLIKN AMDLGVRIVA
     CAMSMDIMGI KKEELIDGVE LGGVASYLGA AEDSGINLFI
//