ID A0A0R2M254_9LACO Unreviewed; 451 AA.
AC A0A0R2M254;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Nadh peroxidase {ECO:0000313|EMBL:KRO07591.1};
GN ORFNames=IV64_GL001525 {ECO:0000313|EMBL:KRO07591.1};
OS Lactiplantibacillus xiangfangensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=942150 {ECO:0000313|EMBL:KRO07591.1, ECO:0000313|Proteomes:UP000051783};
RN [1] {ECO:0000313|EMBL:KRO07591.1, ECO:0000313|Proteomes:UP000051783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26013 {ECO:0000313|EMBL:KRO07591.1,
RC ECO:0000313|Proteomes:UP000051783};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRO07591.1}.
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DR EMBL; JQCL01000103; KRO07591.1; -; Genomic_DNA.
DR RefSeq; WP_057707883.1; NZ_JQCL01000103.1.
DR AlphaFoldDB; A0A0R2M254; -.
DR STRING; 942150.IV64_GL001525; -.
DR PATRIC; fig|942150.3.peg.1575; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000051783; 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:KRO07591.1};
KW Peroxidase {ECO:0000313|EMBL:KRO07591.1}.
FT DOMAIN 1..307
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 331..433
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 451 AA; 48616 MW; 169C3BC163253030 CRC64;
MKVIVVGSSH GGYETVRGIL AAQPDTEIQW YEKGDFLSFL SCGMQLYLEG VVKDVNKVSY
ATPEGMQAQG VHVFLNSEIA KVQPDQHTVH VIDHASGQER DESYDKLVLS VGAVPFDLPV
PGHDLQNVYA MRGRDWAMKL KAKTVDPSVK NVVVIGSGYI GIEAAEVFAK AGMHVTVIDL
LPRLLSLYLD QEFTDILTKT MTAHGIYPAV GQGIKSFEGQ DGHVTKVVTD QGEYPADLVV
SAAGIRPATG FLKGVVDLDD HGLIKINDHL QTSEPDIYAV GDATLVPFAP TGKDNRIALA
TVARRQGRIA AQNLLGGDFP MVPVSGSSAL SVFDYHFAST GIKEGTSDKL GVKSASVLVT
DTIRPKFVPE SDGNTKVWFK LTFDPEDGRV LGAQIMSKAD VTANINAISV AIQANMTVAD
LAYADFFFQP GFDRPWNIIN VAAQKALVDL K
//
