ID K1LV07_9LACT Unreviewed; 380 AA.
AC K1LV07;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=NADH peroxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9706_00005 {ECO:0000313|EMBL:EKB56022.1};
OS Facklamia hominis CCUG 36813.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX NCBI_TaxID=883111 {ECO:0000313|EMBL:EKB56022.1, ECO:0000313|Proteomes:UP000004465};
RN [1] {ECO:0000313|EMBL:EKB56022.1, ECO:0000313|Proteomes:UP000004465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 36813 {ECO:0000313|EMBL:EKB56022.1,
RC ECO:0000313|Proteomes:UP000004465};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Facklamia hominis CCUG 36813.";
RL Submitted (JUL-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:EKB56022.1}.
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DR EMBL; AGZD01000001; EKB56022.1; -; Genomic_DNA.
DR AlphaFoldDB; K1LV07; -.
DR STRING; 883111.HMPREF9706_00005; -.
DR PATRIC; fig|883111.3.peg.5; -.
DR HOGENOM; CLU_003291_1_0_9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000004465; 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; 3.50.50.60; 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 Reference proteome {ECO:0000313|Proteomes:UP000004465}.
FT DOMAIN 5..231
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 254..354
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 380 AA; 41383 MW; 863B485E31AC6517 CRC64;
MHSSSQVIAL DPDKKELTVK TDHGEEKHDY DKLLLSPGGY APKPPFEGID LHNVDTFRGP
EDTAAFKAGM ADTKHLVVIG SGYIGIEVAT AYAQAGIDVL VIDQQEHVLP SYLCNQMADR
LEKYLLDKGI RFKGNETVKQ LKGKAGSVSA VVTDQGEYPA DRVLVAVGVK PGTDWLKDIL
SMDDRGFILV DDFLQTSAED VYAGGDATYV PYAPTGKSAS VALATIARRQ GIVAALNAVG
KKVKMPPVSG TSALKVFDYT LVSTGLSHSN LDTYDGIVES KYVEERVYPD FMRKEGSVYM
NILFDKETHV ILGGQLMSTF DVADSINVLS SLINAGYTLE QLALLDFFFQ PNYDRPWHYL
NVLAIEALGN TVGGADKLLF
//
