ID   A0A168PSK3_9BACL        Unreviewed;       822 AA.
AC   A0A168PSK3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:OAB47032.1};
GN   ORFNames=PBAT_08205 {ECO:0000313|EMBL:OAB47032.1};
OS   Paenibacillus antarcticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=253703 {ECO:0000313|EMBL:OAB47032.1, ECO:0000313|Proteomes:UP000077355};
RN   [1] {ECO:0000313|EMBL:OAB47032.1, ECO:0000313|Proteomes:UP000077355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5836 {ECO:0000313|EMBL:OAB47032.1,
RC   ECO:0000313|Proteomes:UP000077355};
RA   Shin S.-K., Yi H.;
RT   "Draft genome sequence of Paenibacillus antarcticus CECT 5836.";
RL   Submitted (MAR-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}.
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:OAB47032.1}.
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DR   EMBL; LVJI01000012; OAB47032.1; -; Genomic_DNA.
DR   RefSeq; WP_068648405.1; NZ_LVJI01000012.1.
DR   AlphaFoldDB; A0A168PSK3; -.
DR   OrthoDB; 9802028at2; -.
DR   Proteomes; UP000077355; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase 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; 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   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; 1.
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:UP000077355}.
FT   DOMAIN          464..551
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   822 AA;  89851 MW;  92B30F8F862D10FB CRC64;
     MSNKVLIVGG VAGGASAAAR LRRLDEEAHI VMFERDPYIS FANCGLPYYI GDAIKDRSKL
     LVQTPEAMHQ RFNIDVRIQS EVISINPIDK TVRVQSKERG IYEESYDHLI LSPGAKPIQP
     NLPGIESSRI YKVRNIPDTD RIKQKVTGEG TRSAIVIGGG FIGVEMAENL KKIGLDVTLV
     EAGSHILAPF DAEVSNILMK ELEDHHVNLY LSNSVQSFHE TQDQIEVHLA NGDVLTSDMV
     ILAIGVTPDT NFLKDSGLHL GPRGHIIVNE KLETNLENVY AVGDAIEVID YVNGSTTAIP
     LAGPANKQGR IAADNVCGLG TVYKGTQGTS IIKIFGLTGA STGNNEKTLQ RLNIPYRVIY
     VHPSSHASYY PGASPITIKL LFNDEGTVLG AQAVGFDGVD KRIDAIATVI HFHGTVTDLA
     ELELAYAPPY SSAKDPVNMA GYTAENLLTD RTSVFVPKDI ETRDIENTIL VDVRSEIEHV
     NGHIPDSLLI PVDDLRNRLQ ELDRNKEIWV YCQVGLRGYT ASRILTQRGF KVRNLTGGYK
     TYQMSQYTPQ SPNKPLLASV HSDVQEKMAA TFERAIHADV VLDACGLSCP GPLIQLKSTM
     DQLKDGEVLH VTASDPGFYG DVQAWAQMSS QQVLQVNKTS TGMIEAYLRK QAIPLLPTSE
     RVVSPTSEGT SMIVFSGDLD KAIASFIIAN GAAASGKKVT MFFTFWGLNI IRKQNKISVD
     KTFIGRMFGA MMPRGSRKLS MSKMNMMGMG SKMIRGIMKK NNVSSLEELI ESAIEQGVEI
     VACQMSMDIM GLAREELIDK IEIGGVGYYL GKADQSGINL FI
//