ID A0A089L7U6_9BACL Unreviewed; 454 AA.
AC A0A089L7U6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:AIQ55238.1};
GN ORFNames=R70331_29635 {ECO:0000313|EMBL:AIQ55238.1};
OS Paenibacillus sp. FSL R7-0331.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ55238.1, ECO:0000313|Proteomes:UP000029487};
RN [1] {ECO:0000313|EMBL:AIQ55238.1, ECO:0000313|Proteomes:UP000029487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ55238.1,
RC ECO:0000313|Proteomes:UP000029487};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-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}.
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DR EMBL; CP009284; AIQ55238.1; -; Genomic_DNA.
DR RefSeq; WP_042181402.1; NZ_CP009284.1.
DR AlphaFoldDB; A0A089L7U6; -.
DR STRING; 1536773.R70331_29635; -.
DR KEGG; paee:R70331_29635; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_0_9; -.
DR Proteomes; UP000029487; Chromosome.
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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000029487}.
FT DOMAIN 1..305
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 334..428
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 454 AA; 49874 MW; D3C8661C127EC23F CRC64;
MKVAVIGCTH AGTAAIVNTA QLYPDAEITV YERNDNISFL SCGIALYVGG VVKDPQGLFY
SSPEKLAELG VTTKMRHEVI KVDTAAKTLR ARNLATGEEF NDTYDKLIMT TGSWPIIPKL
EGMDLDGILL SKNYNHSNTI IERAEQVKRI TVVGAGYIGV ELVEAFQMNG KQVTLIDGEE
RILSKYLDEE FTAPIQKSLE DHGIKLALGE KVSSFAGENG KVTKVITSKG EHETDLVILC
IGFRPNTELL KGQVDMLPNG AIMVNDYMQT SLPDVFAAGD SCAIHYNPTG QHAYIPLATN
AVRMGTLVAR NLVSNTIPYM GTQGTSGIKI YEDNIAGTGL TEEAAKAEGM EVESVMITDN
YRPEFMPTVE EVQLKVVYAR GTRRILGAQI MSKMDLTQSI NTVSVCIQNR MTVDQLAFID
FFFQPHYNKP WNFLNTAGLQ ALPKTVERKE PVTV
//
