ID A0A1L8WSJ8_9ENTE Unreviewed; 509 AA.
AC A0A1L8WSJ8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000313|EMBL:OJG83976.1};
GN ORFNames=RV14_GL000153 {ECO:0000313|EMBL:OJG83976.1};
OS Enterococcus ratti.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=150033 {ECO:0000313|EMBL:OJG83976.1, ECO:0000313|Proteomes:UP000182152};
RN [1] {ECO:0000313|EMBL:OJG83976.1, ECO:0000313|Proteomes:UP000182152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15687 {ECO:0000313|EMBL:OJG83976.1,
RC ECO:0000313|Proteomes:UP000182152};
RA Zhong Z., Sun Z., Liu W., Zhang W., Zhang H.;
RT "Draft genome sequences of 29 type strains of Enterococci.";
RL Submitted (DEC-2014) 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:OJG83976.1}.
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DR EMBL; JXLB01000001; OJG83976.1; -; Genomic_DNA.
DR RefSeq; WP_071854447.1; NZ_JXLB01000001.1.
DR AlphaFoldDB; A0A1L8WSJ8; -.
DR STRING; 150033.RV14_GL000153; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000182152; 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, 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:UP000182152}.
FT DOMAIN 123..193
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 208..495
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 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; 55412 MW; BCC99844E2EED37D CRC64;
MLDNETKQNL TQYLELLETP VIFSVSTDET SNSQQVLDFV NEVANMSEKI SIEKKQLART
PSFEINSLQQ TSGIVFAGIP LGHEFSSFLL ALLQVSGRPP KISEAMIQSV QQIKQPLHFE
TYVSLTCHNC PDVVQALNIL AVLNPFISHT MIEGSMYQKE VEEKQIMAVP TVYLNGKEFD
SGRMTIEQIL EKITGPSEKE ELNKKEPFDV LVIGGGPAAS SAAIYAARKG IRTGLVADVL
GGQVVETLGI ENMIGTLYTE GPQLMKQVEE HLRSYPVDLI TNQQVTSLKK QADYFEIDLK
SGNRLKTKTA VIATGAHWRS INVPGEKEFK NKGIAYCPHC DGPLFAGKEI AVIGGGNSGI
EAAIDLAGLA KHVYVLEFLP ELKADKVLQD KLASFANVTV ILNAQTKEIA GHTHVESLTY
TDRLTHSEHH LAVSGVFILI GLVPNTSWLA NTLELNNRGE VITDAHGATN VEGLFAAGDC
TNSAYKQIII AMGSGATAAL GAFDYLMRK
//
