ID A0A0X8GYP1_9FIRM Unreviewed; 553 AA.
AC A0A0X8GYP1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:AMC92842.1};
GN ORFNames=AOC36_02225 {ECO:0000313|EMBL:AMC92842.1};
OS Erysipelothrix larvae.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Erysipelothrix.
OX NCBI_TaxID=1514105 {ECO:0000313|EMBL:AMC92842.1, ECO:0000313|Proteomes:UP000063781};
RN [1] {ECO:0000313|EMBL:AMC92842.1, ECO:0000313|Proteomes:UP000063781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LV19 {ECO:0000313|EMBL:AMC92842.1,
RC ECO:0000313|Proteomes:UP000063781};
RA Lim S., Kim B.-C.;
RT "Erysipelothrix larvae sp. LV19 isolated from the larval gut of the
RT rhinoceros beetle, Trypoxylus dichotomus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP013213; AMC92842.1; -; Genomic_DNA.
DR RefSeq; WP_067630803.1; NZ_CP013213.1.
DR AlphaFoldDB; A0A0X8GYP1; -.
DR STRING; 1514105.AOC36_02225; -.
DR KEGG; erl:AOC36_02225; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000063781; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000063781}.
FT DOMAIN 460..548
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 553 AA; 60948 MW; D493133EE243B053 CRC64;
MNQKRVVVVG GSAGGMSFAT RYRRLNQKDS IIILERGPYV SYANCGLPYY ISQEIPSRED
LFVVDQDVLI NRFKLDLKTE HEVVSLDSKK KVIHCMHHGK PLDIPYDMCV LSPGAKPFDL
KISGSETHPA LFTLRNVEDV DRIVDSLQSN HLKHAVVMGA GFIGLEIVEN LVRKGLTVSV
VEKSSQVLPP LDVEMAQALH QTLIAQGVKV YINHSVVSMD ASSCVLDDGT RLQADLVLSC
VGVVPDTQFA KQSGIICGMR EGIVVDHRYQ TNLDSVYALG DACITQQFSS KKDALIPLAS
PANRQGRHLA DILSGKSKER TLTLGTSILR LFNLSAASTG LNEKQLEGQA YEVFHLSAND
HAGYFPGATP ILLKVLFDPK THLILGAQAI GEKGVDKRID VIATAIKANM KVNELQDLEL
AYAPPFGSAK DIVNMAGYVA ENILDKTTHR IHWNALETLQ QEGAYLLDVR NDEERAELGY
IIGSHHCPLD ALRTHLHTFP KDQCIIVYCQ SSARSYNAEC ILRDAGFNVM NMDGSFGLYR
LIRPDRIVMD GSL
//
