ID A0A066UTM6_9VIBR Unreviewed; 440 AA.
AC A0A066UTM6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=CoA-disulfide reductase {ECO:0000313|EMBL:KDN29232.1};
GN ORFNames=VFDL14_13660 {ECO:0000313|EMBL:KDN29232.1};
OS Vibrio fortis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=212667 {ECO:0000313|EMBL:KDN29232.1, ECO:0000313|Proteomes:UP000027219};
RN [1] {ECO:0000313|EMBL:KDN29232.1, ECO:0000313|Proteomes:UP000027219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dalian14 {ECO:0000313|EMBL:KDN29232.1,
RC ECO:0000313|Proteomes:UP000027219};
RA Wang Y., Song L., Liu G., Ding J.;
RT "Vibrio fortis Dalian14 Genome Sequencing.";
RL Submitted (FEB-2014) 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 FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:KDN29232.1}.
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DR EMBL; JFFR01000009; KDN29232.1; -; Genomic_DNA.
DR RefSeq; WP_032550164.1; NZ_JFFR01000009.1.
DR AlphaFoldDB; A0A066UTM6; -.
DR STRING; 212667.VFDL14_13660; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000027219; 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 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 PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 1..303
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 327..428
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 440 AA; 47757 MW; B0744486E47C8C0B CRC64;
MKVVVIGGNA AGMSFAAKYK RNQPSDEVIV LDKRNYISFG ACGLPYFAGG MFDDTERMIS
RTPEQAIKSG LDVRIETEMI ALDRIEKQIK VRHQGKESTI DYDMLMIATG ARPIVPSFGE
FNPEHVYTLT SMEDGLAVKE ALKDNSKQRV CVIGGGFIGL EVFDAAHLLG KQVTIIEREQ
HVMSRQFSPE MIEVVEGAIR ESGAELKTSC SVSAIRDAEQ GGYVIETDDG SVEADVVIMS
LGFKPNTEAF ELPKATNGAL LVNEFGATED AYIHAVGDCA VVHHMALGKP VYVPLATTAN
KQARMMADKL AGKDTYMDGF LGSSCLKVLD YELACTGVSE LLAKEHGLDV KVSTISDKNQ
TDYYPGQEDI KVKLVYHPET KVLLGGEIVG KKGAVGRINA LAVAITAKMT TQQLGYMDFC
YAPPFARTWD ALNVAGNVAK
//
