ID A0A3D8TRU9_9LIST Unreviewed; 508 AA.
AC A0A3D8TRU9;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:RDX01334.1};
GN ORFNames=UR08_10475 {ECO:0000313|EMBL:RDX01334.1};
OS Listeria kieliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1621700 {ECO:0000313|EMBL:RDX01334.1, ECO:0000313|Proteomes:UP000257055};
RN [1] {ECO:0000313|Proteomes:UP000257055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kiel-L1 {ECO:0000313|Proteomes:UP000257055};
RA Schardt J., Mueller-Herbst S., Scherer S., Huptas C.;
RL Submitted (APR-2015) 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}.
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:RDX01334.1}.
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DR EMBL; LARY01000002; RDX01334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8TRU9; -.
DR Proteomes; UP000257055; Unassembled WGS sequence.
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};
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:UP000257055}.
FT DOMAIN 123..194
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 208..493
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 209..224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 468..478
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 336..339
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 508 AA; 54947 MW; FA4FD466770A6AA9 CRC64;
MLDAEIKKQL AGYLELLEGD LVLRVGLDSS ENSKKLSDFV EEITAMSPKI TMTEGAFSRK
PSFSVDQKDQ ESGIVFSGIP LGHEFTSLVL ALLQVSGRAP KVSEKVIKQI QSIKEELHFE
TYVSLSCHNC PDVVQALNIM SVLNPSISHT MIEGGMFQSE IEAKNVMGVP TVFLNGEEFS
NGRMTIEQIL EKIVGTVDIS EFENKDPYDV LVVGGGPAGA SAAIYAARKG IRTGIVAETF
GGQVLETLGI ENVIGTKYIE GPELMRTVEE HVNEYDVDIM KTVRAAKLEK KDLAELTLNN
GAVLKSKTVI LSTGARWRNI NVPGEKEFKN KGVAYCPHCD GPLFAGKNVA VVGGGNSGIE
AAIDLAGLVK HVTVLEFMSE LKADKILQER LHSLPNVTVL TNVQTKEITG TEKVNGLTYV
DRETNEEVHL DLEGVFILIG LVPNTEWLEG TVERAKTGEI IVDKRGATNV PGVFAAGDCT
DSAYKQIIIS MGSGATASLG AFDYLIRN
//
