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Database: UniProt
Entry: S0L2L7_9ENTE
LinkDB: S0L2L7_9ENTE
Original site: S0L2L7_9ENTE 
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
//
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