ID C2EJU8_9LACO Unreviewed; 451 AA.
AC C2EJU8;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=NADH peroxidase {ECO:0000313|EMBL:EEJ73249.1};
DE EC=1.11.1.1 {ECO:0000313|EMBL:EEJ73249.1};
GN Name=npr {ECO:0000313|EMBL:EEJ73249.1};
GN ORFNames=HMPREF0545_1920 {ECO:0000313|EMBL:EEJ73249.1};
OS Ligilactobacillus salivarius DSM 20555 = ATCC 11741.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1423799 {ECO:0000313|EMBL:EEJ73249.1, ECO:0000313|Proteomes:UP000003531};
RN [1] {ECO:0000313|EMBL:EEJ73249.1, ECO:0000313|Proteomes:UP000003531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11741 {ECO:0000313|EMBL:EEJ73249.1,
RC ECO:0000313|Proteomes:UP000003531};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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:EEJ73249.1}.
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DR EMBL; ACGT01000044; EEJ73249.1; -; Genomic_DNA.
DR RefSeq; WP_003700812.1; NZ_GG693224.1.
DR AlphaFoldDB; C2EJU8; -.
DR HOGENOM; CLU_003291_1_0_9; -.
DR Proteomes; UP000003531; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016692; F:NADH peroxidase activity; IEA:UniProtKB-EC.
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:EEJ73249.1};
KW Peroxidase {ECO:0000313|EMBL:EEJ73249.1}.
FT DOMAIN 1..306
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 329..431
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 451 AA; 49932 MW; 139EB9643AD7FBC2 CRC64;
MKVIVVGSSH GGYEAVEGLL KDYPDAEIQW YEQGDFLSFL SCGMQLFLEG KVDSADKVRY
MTPEAIRSRG VSLFEQTQVI ALHSADHEIE VKDLQTGEVR TENYDKLILS PGAVPMELDV
PGKNLENVYY MRGHDWAVKL KEKVLDNNVK NVVVIGSGYI GIEAAEVFAK AGKSVEVLDM
LPRPLATYLD KELTDVIEPE LTQNNVHVHG NQLVQEYLGE DTVTGVKTDK GEYPADLVIV
AAGVKPNTAW LKGELAMYPN GIVKTDNFMR SSADDVFVVG DATLLKYNPG NTLLNIALAT
NARKQGRFAV KNLEAPLHPF PGVQGTSALS VFDYKFASSG LNATNAQKLG KQVRSVVVED
DFRMDFVPEE ENAHVWFKLT YDPDTKAILG GQILSKHDLT AYINVISLAI KTKQTIYDLA
YEDFFFQPGF DKPWNILNLA GLAAEKQEDE D
//
