ID U5LJE0_9BACI Unreviewed; 509 AA.
AC U5LJE0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:AGX06737.1};
GN ORFNames=N288_24510 {ECO:0000313|EMBL:AGX06737.1};
OS Bacillus infantis NRRL B-14911.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1367477 {ECO:0000313|EMBL:AGX06737.1, ECO:0000313|Proteomes:UP000017805};
RN [1] {ECO:0000313|EMBL:AGX06737.1, ECO:0000313|Proteomes:UP000017805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-14911 {ECO:0000313|EMBL:AGX06737.1,
RC ECO:0000313|Proteomes:UP000017805};
RA Massilamany C., Smith T.P.L., Loy J.D., Barletta R., Reddy J.;
RT "Complete genome sequence of Bacillus infantis NRRL B-14911 that has
RT potential to induce cardiac disease by antigenic mimicry.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000238-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000238-1};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009333}.
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DR EMBL; CP006643; AGX06737.1; -; Genomic_DNA.
DR RefSeq; WP_009794428.1; NC_022524.1.
DR AlphaFoldDB; U5LJE0; -.
DR STRING; 1367477.N288_24510; -.
DR GeneID; 85554507; -.
DR KEGG; bif:N288_24510; -.
DR PATRIC; fig|1367477.3.peg.4898; -.
DR HOGENOM; CLU_031864_4_2_9; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000017805; Chromosome.
DR GO; GO:0008785; F:alkyl hydroperoxide reductase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0000302; P:response to reactive oxygen species; IEA:InterPro.
DR CDD; cd03026; AhpF_NTD_C; 1.
DR CDD; cd02974; AhpF_NTD_N; 1.
DR Gene3D; 3.40.30.80; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR044141; AhpF_NTD_C.
DR InterPro; IPR044142; AhpF_NTD_N.
DR InterPro; IPR012081; Alkyl_hydroperoxide_Rdtase_suF.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR03140; AhpF; 1.
DR PANTHER; PTHR48105:SF6; ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF13192; Thioredoxin_3; 1.
DR PIRSF; PIRSF000238; AhpF; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000238-2}; FAD {ECO:0000256|PIRSR:PIRSR000238-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000238-1};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000238-1};
KW NADP {ECO:0000256|PIRSR:PIRSR000238-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000238-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000017805}.
FT DOMAIN 124..192
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 209..494
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 210..225
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 349..363
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 469..479
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 337..340
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 509 AA; 54723 MW; BEE5F4E116F6E6C8 CRC64;
MVLDADIKAQ LAQYLQLMES EVLLKVSAGS DDVSRDMLAL VDELASMSSS IKVEKAELHR
TPSFSVNRIG EDTGVTFAGI PLGHEFTSLV LALLQVSGRA PKADQKVIDQ IKNIKGEYRF
ESYISLSCHN CPDVVQALNL MSVLNPNITH TMIDGAAFKE EVESRDIMAV PTVFLNGESF
GSGRMSLEEI LGKMGSGPDA SELSDKDPYD VLVVGGGPAG ASAAIYAARK GIRTGIVAER
FGGQVMDTLG IENFISVKHT EGPKLVASLE EHVKEYGIDV MNLQRAKSLE KKDLIELELE
NGAVLKSKSV ILSTGARWRN VNVPGEAEFK NKGVAYCPHC DGPLFEGKDV AVIGGGNSGI
EAAIDLAGIV KHVTVLEFMP ELKADAVLQD RLYSLPNVTV LKNVQTKEIT GTDKVNGISY
IDRETGEEHH VELQGVFVQI GLVPNTDWLG DSIERTRFGE IIVDKHGATN VPGVFAAGDC
TDSAYKQIII SMGSGATASL GAFDYLIRN
//
