ID S0L2L7_9ENTE Unreviewed; 511 AA.
AC S0L2L7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Alkyl hydroperoxide reductase, F subunit {ECO:0000313|EMBL:EOT82969.1};
GN ORFNames=I573_02082 {ECO:0000313|EMBL:EOT82969.1};
OS Enterococcus sulfureus ATCC 49903.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1140003 {ECO:0000313|EMBL:EOT82969.1, ECO:0000313|Proteomes:UP000015961};
RN [1] {ECO:0000313|EMBL:EOT82969.1, ECO:0000313|Proteomes:UP000015961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49903 {ECO:0000313|EMBL:EOT82969.1,
RC ECO:0000313|Proteomes:UP000015961};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sulfureus ATCC_49903 (PacBio/Illumina
RT hybrid assembly).";
RL Submitted (MAR-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}.
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:EOT82969.1}.
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DR EMBL; ASWO01000007; EOT82969.1; -; Genomic_DNA.
DR RefSeq; WP_016186431.1; NZ_KE136396.1.
DR AlphaFoldDB; S0L2L7; -.
DR STRING; 1140003.OMY_01999; -.
DR PATRIC; fig|1140003.3.peg.1926; -.
DR eggNOG; COG3634; Bacteria.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000015961; 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:UP000015961}.
FT DOMAIN 124..194
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 210..496
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 211..226
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 351..365
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 471..481
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 339..342
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 511 AA; 55493 MW; 0644C48F3AFEFDBA CRC64;
MSLDLDIKEQ LVQYLALLEN DVVFTASLDD QKESTEVREF IEEIVAMSER LTFVEVKLAY
TPSFRLDQPG KESGVVFAGV PLGHEFTSFV LALLQVSGRA PKVDEDVIRK IKQIDQPLHF
ETFVSLTCHN CPDVVQALNI ISVLNEQVSH TMIEGGMFKD VVDAKGIMAV PNVFLNGEEF
DSGRMSIEQI LDKLAIGESD HEELSAKEPF DVLVVGAGPA GVSAAIYAAR KGIRTGIVAE
RFGGQVLETV GIENLIGTPY TEGEKLAISL EEHAKTYPID IIKTRRVVNI KEEDTLKVVE
LDNGATLKAK VVILATGARW RNVNVPGEAE FKNKGVAYCP HCDGPLFAGK DVAVIGGGNS
GIEAAIDLAG MSSHVTVLEF LPELKADSVL QERVASLPNV TVIKNAQTKE ILGDTKVHAL
TYIDRETNEV HQVDLAGVFV QIGLVPNTEF LDERFEKTRM GELVVDKFGQ TSVPGIFAAG
DCTDSAYKQI IISMGSGATA ALGAFDYMIR Q
//