ID A0A0P7Y224_9GAMM Unreviewed; 518 AA.
AC A0A0P7Y224;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000256|ARBA:ARBA00020059};
GN Name=ahpF {ECO:0000313|EMBL:KPQ24176.1};
GN ORFNames=HLUCCA13_10345 {ECO:0000313|EMBL:KPQ24176.1};
OS Halomonas sp. HL-48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1479235 {ECO:0000313|EMBL:KPQ24176.1, ECO:0000313|Proteomes:UP000050569};
RN [1] {ECO:0000313|EMBL:KPQ24176.1, ECO:0000313|Proteomes:UP000050569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-48 {ECO:0000313|EMBL:KPQ24176.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serves to protect the cell against DNA damage by alkyl
CC hydroperoxides. It can use either NADH or NADPH as electron donor for
CC direct reduction of redox dyes or of alkyl hydroperoxides when combined
CC with the AhpC protein. {ECO:0000256|ARBA:ARBA00024806}.
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:KPQ24176.1}.
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DR EMBL; LJZS01000011; KPQ24176.1; -; Genomic_DNA.
DR RefSeq; WP_027336234.1; NZ_LJZS01000011.1.
DR AlphaFoldDB; A0A0P7Y224; -.
DR STRING; 1479235.GCA_000686925_01247; -.
DR PATRIC; fig|1479235.4.peg.3245; -.
DR eggNOG; COG3634; Bacteria.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000050569; 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 ECO:0000313|EMBL:KPQ24176.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000238-2}.
FT DOMAIN 125..193
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 212..504
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 213..228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 356..370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 478..488
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 344..347
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 518 AA; 55358 MW; 1E0D0119C986B99C CRC64;
MLDANLKNQL KAYLENVTQP LEIVASLDDG NKSHELLGLL QEICGLSDKL SLSTEGHDAR
TPSFAINRPG EETGVVFAGI PMGHEFTSLV LALLQVGGHP PKTSDEVLDQ IRALDRELVF
ETYYSLSCQN CPDVVQALNL MAIFNPQIRH VAIDGALFQN EVEAREIMSV PSIYLNGEPF
DQGRMTLEQI LAKVDTGAAE REAKKLSEKA AFDTLVIGGG PAGAAAAIYS ARKGINTGIA
AERFGGQVAD TLGIENFISI SHTEGPKLVS ALEEHVKDYE VDVMNLQHAT SLKAADTNGG
LHEVTLASGA TLKSKTLVLA TGARWREMNV PGEQQYRNKG VAYCPHCDGP LFKGKHVAVI
GGGNSGVEAA IDLAGIVGHV TLIEFMGEMR ADAVLQKKLK SLANVDIILN AQTTEVNGDG
SRVNGLTYKD RSSDEIKHLT LEGIFVQIGL VPNTEWLKGS PVEMSPHGEI IVDGHGMTSV
PGIFAAGDVT TVPYKQIVIA MGEGAKASLG AFDYLIRQ
//
