ID   Q8KS25_THENE            Unreviewed;       443 AA.
AC   Q8KS25;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=NADH:polysulfide oxidoreductase {ECO:0000313|EMBL:AAM76054.1};
GN   Name=npo {ECO:0000313|EMBL:AAM76054.1};
OS   Thermotoga neapolitana.
OC   Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC   Thermotoga.
OX   NCBI_TaxID=2337 {ECO:0000313|EMBL:AAM76054.1};
RN   [1] {ECO:0000313|EMBL:AAM76054.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NS-E {ECO:0000313|EMBL:AAM76054.1};
RA   Childers S.E., White C.S., Borges K.M., Zhaxybayeva O.A., Gogarten J.P.,
RA   Noll K.M.;
RT   "Identification of a Gene Encoding an NADH:Polysulfide Oxidoreductase (npo)
RT   in Thermotoga Species.";
RL   Submitted (JUN-2002) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF520782; AAM76054.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KS25; -.
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; 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          3..298
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          328..429
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   443 AA;  48035 MW;  EE607601A81CA6D8 CRC64;
     MKYDVVIVGG GPAGLVAAFT TKRFYKDKKI LVVKKTEKET VPCGIPYIFH TLSGVENDYM
     GIEERFKSAG IDLLIDVVVD GNTDEKKLLT KTGKEIFYEK LIIATGSTPN VPNIPGVDLE
     GVFTVPKDAN YLKMLYEKIK DSKNVVIIGG GFIGVEVADE LKKSGKNVTL VEIMDSLLPV
     SFDPDFGEIA RKEIEAENLK VLTGRKVTEI YGSKRVEGVR LDNAETILAD AVILATGYRP
     NSDLARKLGL KVTEYGFIET DEYMRTSKPD VFAAGDCVQH RDFLTGRPSR LMLASAAVLD
     ARIAASNLYG LKVIRANKGS LNAYSTVIGS KAFGSVGITE RVAKEEGFEI VVGRAEAPDR
     HPGKFEDTTK LIVKLIFSED SKILLGAQVC GGKSVGEIVN ILSLGMQKGI TANDLFTMQI
     GTHPLLTSAP TVYPLAKAAE MVL
//