ID A0A0J1KB82_9GAMM Unreviewed; 567 AA.
AC A0A0J1KB82;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:KLV11587.1};
GN ORFNames=ABT57_02345 {ECO:0000313|EMBL:KLV11587.1};
OS Photobacterium ganghwense.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=320778 {ECO:0000313|EMBL:KLV11587.1, ECO:0000313|Proteomes:UP000035909};
RN [1] {ECO:0000313|EMBL:KLV11587.1, ECO:0000313|Proteomes:UP000035909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22954 {ECO:0000313|EMBL:KLV11587.1,
RC ECO:0000313|Proteomes:UP000035909};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) 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:KLV11587.1}.
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DR EMBL; LDOU01000002; KLV11587.1; -; Genomic_DNA.
DR RefSeq; WP_047883546.1; NZ_PYMI01000003.1.
DR AlphaFoldDB; A0A0J1KB82; -.
DR STRING; 320778.ABT57_02345; -.
DR PATRIC; fig|320778.3.peg.497; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000035909; 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; 3.50.50.60; 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; 2.
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:UP000035909}.
FT DOMAIN 483..567
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 567 AA; 61696 MW; A35A87B4E8E6184C CRC64;
MTKILIVGGV AGGASAAARA RRLSEDAEII MFERGKFVSF ANCGLPYHIG GDIQDRSKLL
LQTPDSFLAR FNVDVRVFNE VTGINRENKT VTVKNLIDGQ EYTENYDFLL LSPGAGPIVP
PIPGINNPLT HSLRNIPDMD KIIQTLQMNK PEHATVVGGG FIGLEMMEAF HQLGIPTTLI
EMADQVMTPV DREMAGFVHN EIRNKGIDLR LGVALQSVEF VPSTSVANRN AGETDEHQHL
EGELNLTLNN GDTLTTDILI MAIGVRPDIK LAQDAGLQIG STGGIYTNEY MQTSDPAIYA
VGDAVEETDF VTGKPTLVPL AGPANRQGRI AADNMLGRQE TYQRTQGTAI CKVFDIAVGS
TGKNEKQLQR EGLAYEKAYV HTASHASYYP GAEVVSLKLL FDPHSGKILG AQAVGKDGID
KRIDVLAVAQ RAGMTVEQLQ HLELTYAPPY GSAKDVINQA AFVATNILKG DATPIHYDAI
DQLSDDQILL DVRNPGELSN VGYIDGAINI PVDQLRQRMD ELPKDKEIVI YCQVGLRGNV
AYRQLVNNGY KACNLIGGYR TWLTAKQ
//
