ID W9EGU9_9LACO Unreviewed; 452 AA.
AC W9EGU9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=NADH peroxidase Npx {ECO:0000313|EMBL:ETO40240.1};
GN ORFNames=B808_851 {ECO:0000313|EMBL:ETO40240.1};
OS Fructilactobacillus florum 8D.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Fructilactobacillus.
OX NCBI_TaxID=1221538 {ECO:0000313|EMBL:ETO40240.1, ECO:0000313|Proteomes:UP000019474};
RN [1] {ECO:0000313|EMBL:ETO40240.1, ECO:0000313|Proteomes:UP000019474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8D {ECO:0000313|EMBL:ETO40240.1,
RC ECO:0000313|Proteomes:UP000019474};
RA Kim E.B., Marco M.L.;
RT "Genome sequencing of Lactobacillus florum 8D.";
RL Submitted (AUG-2012) 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:ETO40240.1}.
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DR EMBL; ALXG01000035; ETO40240.1; -; Genomic_DNA.
DR RefSeq; WP_009166378.1; NZ_ALXG01000035.1.
DR AlphaFoldDB; W9EGU9; -.
DR PATRIC; fig|1221538.3.peg.859; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000019474; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
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 Oxidoreductase {ECO:0000313|EMBL:ETO40240.1};
KW Peroxidase {ECO:0000313|EMBL:ETO40240.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019474}.
FT DOMAIN 1..309
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 333..434
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 452 AA; 49183 MW; 392B22D3FC87B82F CRC64;
MKVAVIGSSH GGYEAVRGVL HDFPDAQIDW YEKGDFVSFL SCGMELYLQG VVKDVNSVSY
ATVPGMEAKG VHVHINSEVT AIDPDAHRMT VVEVQSGRDT TAEYDKLILA VGAVPFKLPV
PGKELKNVYA MRGRDWAIKL KQASVDPTIK NVTVVGSGYI GIEAAESFAK AGMHVTIIDL
NPTILGTYLD SEFTDILQDE LTAQNVELRL SQSVKEYVGN DHGAVKSVIS TTGSTWPADL
VIETAGIRPA TKWLADVIDL DEHGMIKTNE YQQTSQPDIF AAGDATEVEF APTGKKQLIA
LATNARRQGR SAAYNLEEQR RKTTAVSGSS ALHVFSYKFA STGVKDVTAA TVGAKIESVF
LKDTVVPPFV PESHNAPVYF KLSFDPETRT IMGAQIMSTM DVTANINAIS LALQQHLTID
DLAYADFFFQ PGFDRPWNIM NVAAQKAQDK LD
//
