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Database: UniProt
Entry: A0A0F3RUF2_9LACO
LinkDB: A0A0F3RUF2_9LACO
Original site: A0A0F3RUF2_9LACO 
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}.
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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
//
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