ID F8AIZ6_PYRYC Unreviewed; 442 AA.
AC F8AIZ6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:AEH24474.1};
GN OrderedLocusNames=PYCH_07890 {ECO:0000313|EMBL:AEH24474.1};
OS Pyrococcus yayanosii (strain CH1 / JCM 16557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=529709 {ECO:0000313|EMBL:AEH24474.1, ECO:0000313|Proteomes:UP000008386};
RN [1] {ECO:0000313|EMBL:AEH24474.1, ECO:0000313|Proteomes:UP000008386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH1 / JCM 16557 {ECO:0000313|Proteomes:UP000008386};
RX PubMed=21705594; DOI=10.1128/JB.05345-11;
RA Jun X., Lupeng L., Minjuan X., Oger P., Fengping W., Jebbar M., Xiang X.;
RT "Complete genome sequence of the obligate piezophilic hyperthermophilic
RT archaeon Pyrococcus yayanosii CH1.";
RL J. Bacteriol. 193:4297-4298(2011).
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}.
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DR EMBL; CP002779; AEH24474.1; -; Genomic_DNA.
DR RefSeq; WP_013905531.1; NC_015680.1.
DR AlphaFoldDB; F8AIZ6; -.
DR STRING; 529709.PYCH_07890; -.
DR GeneID; 10837364; -.
DR KEGG; pya:PYCH_07890; -.
DR eggNOG; arCOG01069; Archaea.
DR HOGENOM; CLU_003291_1_3_2; -.
DR OMA; ATEWVSH; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000008386; Chromosome.
DR GO; GO:0050451; F:CoA-disulfide reductase (NADP) activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR017758; CoA_disulphide_reductase.
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 NCBIfam; TIGR03385; CoA_CoA_reduc; 1.
DR PANTHER; PTHR43429:SF1; NAD(P)H SULFUR OXIDOREDUCTASE (COA-DEPENDENT); 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 5..285
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 327..429
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 442 AA; 48439 MW; C11FE6C0AD53D319 CRC64;
MGKKTVVVIG GGAAGMSAAS RIKRLKPEWD VKVFEATEWV SHAPCGIPYV VEGISPMEKL
MHYPPEVFIK KRGIDLHMKA EVMEVDTGHV RVRESDGEHT YEWDYLVFAN GASPQVPPIE
GIDLPGVFTA DLPPDALAIR EYMEKNNVRN VVVIGTGYIA IEMAEAFVAQ GKSVTLIGRS
ERILRKTFDK EVTDIVEEKL KESLNLRLEE MTLRIEGQGK VEKVVTDADE YPADLVVIAT
GIKPNVELAR ELGVKIGETG AIWTNDKMQT SVENVYAAGD VAETRHIITG RRVWNPLAPA
GNKMGYVAGS NIAGKEMHFP GVLGTSVTKF LDLEIGKTGL TESEAVNEGF DVRTAFIKAK
TKPHYYPGSK EIWLKGVVDN ETNKLLGVQA VGAEVLPRID TAAAMLMAGF TTKDVFFTDL
AYAPPFAPVW DPLVVLARVL KF
//