ID A0A1L8QNU1_9ENTE Unreviewed; 454 AA.
AC A0A1L8QNU1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=RU93_GL001208 {ECO:0000313|EMBL:OJG09137.1};
OS Enterococcus aquimarinus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=328396 {ECO:0000313|EMBL:OJG09137.1, ECO:0000313|Proteomes:UP000182149};
RN [1] {ECO:0000313|EMBL:OJG09137.1, ECO:0000313|Proteomes:UP000182149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17690 {ECO:0000313|EMBL:OJG09137.1,
RC ECO:0000313|Proteomes:UP000182149};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-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 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:OJG09137.1}.
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DR EMBL; JXKD01000020; OJG09137.1; -; Genomic_DNA.
DR RefSeq; WP_071875646.1; NZ_JXKD01000020.1.
DR AlphaFoldDB; A0A1L8QNU1; -.
DR STRING; 328396.RU93_GL001208; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000182149; 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; 3.30.390.30; -; 1.
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;
KW Oxidation {ECO:0000256|ARBA:ARBA00023097};
KW Reference proteome {ECO:0000313|Proteomes:UP000182149}.
FT DOMAIN 1..308
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 337..435
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 454 AA; 50619 MW; 60A7E19CD6839731 CRC64;
MRVLIIGGSH GGIATARHLK KINPSVEVII IEQSNVLGYI GSSLNLYLEK YVPTLEVCRT
TSPSQLLTEG INVMIHSKVT AVCPESKSIT VTMQDGETKI EDTISYDFLV LAMGSSQYQT
SFSEEMEDQV TNYKSLSQAK KAAVTLEASQ KVIIIGAGLI GFELAETLSQ MNKEVILLDR
MNRGLFRYFD DEITSILLRD LPANVQLKLN RNVQSVEIDE NNHFKGVQLT HDDLIEGDAL
IYAINPRPNI ELVADIVSVN ADGTIETNEY MQTSDPFIYA VGDLVSVYFS QSNTPSYIPL
VTNAYRTGII AATNILLDVK IPFPVVQRTI ASELFAYYLA STGINEDEAP YYGLSVQSVS
KTYEKSALFS LETDFEITIK FVFDQHSKQL LGGQIISNYE KSLELINTLS GLITKQTTLD
EMLTMDFYFN PKFSNPLHFF NDLALEGILK VNRR
//
