ID A0A2T0BE09_9CLOT Unreviewed; 566 AA.
AC A0A2T0BE09;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Coenzyme A disulfide reductase {ECO:0000313|EMBL:PRR82104.1};
DE EC=1.8.1.14 {ECO:0000313|EMBL:PRR82104.1};
GN Name=cdr_2 {ECO:0000313|EMBL:PRR82104.1};
GN ORFNames=CLVI_20390 {ECO:0000313|EMBL:PRR82104.1};
OS Clostridium vincentii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=52704 {ECO:0000313|EMBL:PRR82104.1, ECO:0000313|Proteomes:UP000239471};
RN [1] {ECO:0000313|EMBL:PRR82104.1, ECO:0000313|Proteomes:UP000239471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10228 {ECO:0000313|EMBL:PRR82104.1,
RC ECO:0000313|Proteomes:UP000239471};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium vincentii DSM 10228.";
RL Submitted (MAR-2018) 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:PRR82104.1}.
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DR EMBL; PVXQ01000020; PRR82104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0BE09; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000239471; Unassembled WGS sequence.
DR GO; GO:0050451; F:CoA-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR CDD; cd00158; RHOD; 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:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 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 Oxidoreductase {ECO:0000313|EMBL:PRR82104.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239471}.
FT DOMAIN 464..548
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 566 AA; 62292 MW; 4A4313E36FBDB26A CRC64;
MKKKILIIGG VAGGASAAAR LRRHSEEDQI IMFEKGPHVS FSNCSLPYHL SGIIETADKL
VLMSPEKFMA QYKIEAKINS EVISINRDKK EVMVKNILTD KTYIESYDKL ILSPGAKPIV
PNFPGIDKVN VFTVRNVVDI DRLNRFVKSM DSKDVTVIGG GFIGIEVAEN LKDAGYNVTL
IEAMEQILRP FDYDMVQILH KELYDHGINL IFGDKVSGFE ENKVVLASGK KIDAKAVIMA
IGVAPETDLA REAGIELGET KAIKVDQNYR TNDRDIYAVG DAVEVYNSLT HSMTKLSLAG
PALKQARAVA DHINGISVLN TGYIGSSAIK VFDYNGASTG LNESLIKVLG LKINYEIVRV
ILSDKVGIMP DSSPIHFKLL FEVPTGKILG AQAIGKGNVD KRIDVIATAI KFGGTVNSLK
DLELCYAPPF STAKDVVNYA GYVASNLLRG DFKQVNVDKV RELIESGAYI VDVREKVEFD
RGHLKVAVNI PLSELRDRAA EIPKDVPVYL HCRTGQRSYN AVLALQNMGY KNVANITGSF
LGISLYEYFN DITTGREKIV TEYNFK
//
