ID A0A3A1QRC0_9BACI Unreviewed; 509 AA.
AC A0A3A1QRC0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000313|EMBL:RIW28813.1};
GN ORFNames=D3H55_20600 {ECO:0000313|EMBL:RIW28813.1};
OS Bacillus salacetis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2315464 {ECO:0000313|EMBL:RIW28813.1, ECO:0000313|Proteomes:UP000265801};
RN [1] {ECO:0000313|EMBL:RIW28813.1, ECO:0000313|Proteomes:UP000265801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKP7-4 {ECO:0000313|EMBL:RIW28813.1,
RC ECO:0000313|Proteomes:UP000265801};
RA Daroonpunt R., Tanasupawat S., Yiamsombut S.;
RT "Bacillus saliacetes sp. nov., isolated from Thai shrimp paste (Ka-pi).";
RL Submitted (SEP-2018) 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:RIW28813.1}.
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DR EMBL; QXIR01000039; RIW28813.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A1QRC0; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000265801; 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:UP000265801}.
FT DOMAIN 124..193
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; 54680 MW; AF4528BE92D4A21E CRC64;
MLLDADVKAQ LAQYLELLEG DILLKVSAGE DETSRDMLLL VDELATMSSH IKVEHADLKR
TPSFSVNRIG EDTGVTFAGI PLGHEFTSLI LALLQVSGRA PKVDDSVLEQ VKNLDGEYHF
ESYISLSCHN CPDVVQALNL MSIFNEGVTH TMIDGASFKE EVESKEIMAV PTVFLNGEEF
GSGRMSIEEI LGKLGGGPDA SELSGKDPYD VLVVGGGPAG ASAAIYAARK GIRTGIVAER
FGGQVMDTLG IENFISVKHT EGPKLVASLE EHVKDYGIDV MNLQRASRLE KKDMIELELE
NGAVLKSKSL ILSTGARWRK VGVPGEDEFK NKGVAYCPHC DGPLFEGKHV AVIGGGNSGV
EAAIDLAGIV KHVTVIEFNA DLKADAVLQD RLYSLPNVTV IKNAQTKEIT GTDKVNGLTY
VERDTETEQH INLEGVFVQI GLVPNTDWLG NALDRNRMGE IVIDKQGATS MPGVFAAGDC
TDSAYKQIII SMGSGATAAL GAFDYLIRN
//
