ID   A0A0M0BS50_9ARCH        Unreviewed;       460 AA.
AC   A0A0M0BS50;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AC482_00850 {ECO:0000313|EMBL:KON31417.1};
OS   miscellaneous Crenarchaeota group-15 archaeon DG-45.
OC   Archaea; Candidatus Bathyarchaeota; MCG-15.
OX   NCBI_TaxID=1685127 {ECO:0000313|EMBL:KON31417.1, ECO:0000313|Proteomes:UP000037210};
RN   [1] {ECO:0000313|EMBL:KON31417.1, ECO:0000313|Proteomes:UP000037210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG-45 {ECO:0000313|EMBL:KON31417.1};
RA   Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA   Teske A.P.;
RT   "New insights into the roles of widespread benthic archaea in carbon and
RT   nitrogen cycling.";
RL   Submitted (JUN-2015) 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:KON31417.1}.
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DR   EMBL; LFWZ01000005; KON31417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0BS50; -.
DR   PATRIC; fig|1685127.3.peg.147; -.
DR   Proteomes; UP000037210; 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          13..315
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          342..438
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   460 AA;  48942 MW;  52BA1E1FE38759D8 CRC64;
     MSSRGVSGAS SRRIVIIGLG TGGLYASRAA TRVDRRAEVT LIERRDYDMF SPCGLPYAIE
     GKVESFEDLK HTVPTTRNIR KLLRHEALSI DTEGKRVEVK NLESGEVLWL DYDSLIIATG
     SSPILLPVPG AEEFIGRGIH FVTNPENARE LKEAALRSKA AVMVGGGAIG LEIALALKRL
     GVEVYVTKRT PPPLPRNLDP DMGEIITAYL ESQGLHILFG KGIDNINGGD RVESVVIAGE
     TIPADLVVMA VGVRPESKIA EKSGIATGRG GIVVDERMRT SAEDVYAIGD CAATFSGIDG
     EEVSPNLATT AFHHAAVAGV NAAGGEAAYD GSLGTFVSFM GELEVACTGY NSSTAEERGF
     KVVTGRANMT VKPRWMPDAR EISVKLVVDA ETGRILGGQA IGEEGAACRI NVVALAIKRR
     ATLEEFTSIE LAYCPAVSDL YDPLLVAADA ALRRFKRTAG
//