ID A0A0F3RUF2_9LACO Unreviewed; 470 AA.
AC A0A0F3RUF2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:KJW12387.1};
GN ORFNames=VC81_07700 {ECO:0000313|EMBL:KJW12387.1};
OS Levilactobacillus spicheri.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=216463 {ECO:0000313|EMBL:KJW12387.1, ECO:0000313|Proteomes:UP000033491};
RN [1] {ECO:0000313|EMBL:KJW12387.1, ECO:0000313|Proteomes:UP000033491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP38 {ECO:0000313|EMBL:KJW12387.1,
RC ECO:0000313|Proteomes:UP000033491};
RA Zheng J., Ganezle M.;
RL Submitted (MAR-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:KJW12387.1}.
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; JZCR01000019; KJW12387.1; -; Genomic_DNA.
DR RefSeq; WP_045807489.1; NZ_JZCR01000019.1.
DR AlphaFoldDB; A0A0F3RUF2; -.
DR STRING; 216463.VC81_07700; -.
DR PATRIC; fig|216463.3.peg.651; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000033491; 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; 3.30.390.30; -; 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; 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;
KW Oxidation {ECO:0000256|ARBA:ARBA00023097}.
FT DOMAIN 1..305
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 331..429
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 451..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 51931 MW; C1DA97607FB96E53 CRC64;
MKVIIVGSTH AGTNAALQIL RDHPDTDVTI YERHTNVSFL SCGISLFLDG QVKHLEDMFY
SSPEQLTKLG ATIKTRYNVL KIDAEAKTLE AVNMDSGDLV NDTYDKLIMA TGSTVTVPPI
FGIDEDKVLL CKNYDQAKAI YETAKTNKRI AIIGAGYVGT ELAESYARTD HDVQLFQSRD
IILNHYVDKN FSDRIVDMLE DKGVKVYMNR RVTSFTGDDD GQLIIETTDG DFTADLAIVC
TGFVPNTELL RGQVDMDKHG AIIINDYVQS SNPDIYACGD ACVVNFNPTG KPAYTPLATN
AVRQGMLAGM NVFGNVQQYM GTQATSAMNI FGYTLASTGL TLEHAKKSGF EHADMVTFEG
TWRPEYMPST DKLSINLVYD TQSRLILGAQ LYSKHEVAQS ANALSIAIQN RNTIDDLAFV
DMLFQPNFDD PFNYLNLVAQ MAVEKEIERG NNHPRLTAPA NMVPDTADEK
//