ID A0A081N6W7_9GAMM Unreviewed; 560 AA.
AC A0A081N6W7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:KEQ14190.1};
GN ORFNames=GZ77_07060 {ECO:0000313|EMBL:KEQ14190.1};
OS Endozoicomonas montiporae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Endozoicomonas.
OX NCBI_TaxID=1027273 {ECO:0000313|EMBL:KEQ14190.1, ECO:0000313|Proteomes:UP000028006};
RN [1] {ECO:0000313|EMBL:KEQ14190.1, ECO:0000313|Proteomes:UP000028006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24815 {ECO:0000313|EMBL:KEQ14190.1,
RC ECO:0000313|Proteomes:UP000028006};
RA Neave M.J., Apprill A., Voolstra C.R.;
RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL Submitted (JUN-2014) 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:KEQ14190.1}.
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DR EMBL; JOKG01000002; KEQ14190.1; -; Genomic_DNA.
DR RefSeq; WP_034873943.1; NZ_JOKG01000002.1.
DR AlphaFoldDB; A0A081N6W7; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR Proteomes; UP000028006; Unassembled WGS sequence.
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:SF7; NITRIC OXIDE REDUCTASE FLRD-NAD(+) REDUCTASE; 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:UP000028006}.
FT DOMAIN 464..547
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 560 AA; 60663 MW; 090F9989699617B5 CRC64;
MKIVIIGGVA GGASAAAKAR RLSEDAEIIL FERGEQISFA NCGLPYHIGG DIQDRDALLI
QTPEKMHHRF NIDVRVETEI TDINPAKKTV VAKHTLTGEE YEETYDRLIL SPGAAPFIPP
IEGIESPEVM TLRNMSDMDR ILATLDNTHT RRAAVIGGGF IGLEMAEALV HRNLSVSLIE
QAPQVMAPLD AEMAEPLHDT LRQQNVDLRL NTGVKRFTLE DRGITLTLMD DSLLKVDLVI
LAIGVRPETT LATSAGLEIG KTGGIAVNRR METSEQDIFA VGDAVEINEF VSGDPALIPL
AGPANRQGRI AAINALGGKA EYRGSQGTAV CKLFDLTVAS TGLNEKALKR QGTAYEKVYI
HANNHAGYYP GASKINFKLL FSSEGKVLGA QATGLSGVDK RIDVIATAIQ ADLSVYDLEE
VELTYAPPYG SAKDVVNYAG FVAANVLNKS MTQLYSENLP DALEDPQAIL LDVRNPDEIT
QSGAIPGSIN IPLDSLRQNL QQLPKNKTII VYCAVGLRGY LACRVLGQNG YNTRNLAGGY
YMWQQSKHCR PVSNTERKVA
//
