ID A0A3E0H8T0_9GAMM Unreviewed; 523 AA.
AC A0A3E0H8T0;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000256|ARBA:ARBA00020059};
GN ORFNames=DFR26_0230 {ECO:0000313|EMBL:REH40033.1};
OS Paraperlucidibaca baekdonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Paraperlucidibaca.
OX NCBI_TaxID=748120 {ECO:0000313|EMBL:REH40033.1, ECO:0000313|Proteomes:UP000256774};
RN [1] {ECO:0000313|EMBL:REH40033.1, ECO:0000313|Proteomes:UP000256774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26022 {ECO:0000313|EMBL:REH40033.1,
RC ECO:0000313|Proteomes:UP000256774};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2018) 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:REH40033.1}.
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DR EMBL; QUNR01000001; REH40033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E0H8T0; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000256774; 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};
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:UP000256774}.
FT DOMAIN 124..193
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 212..499
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 473..483
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 340..343
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 523 AA; 55371 MW; 25149166A2982F29 CRC64;
MLDAELKTQL AAYLQRLVSP IELVASLDER AESQELLALL HDIAALNPQI AVREDGSDAR
RPSFAVNKPG EESGVCFAGI PLGHEFTSLV LALLQVSGYA PKVSDDVLAQ IRELPAGLHF
ETFISLSCHN CPDVVQAFNL MAVVNPGISH TMIDGALFQD EVERKQIMSV PSVHLNGESF
GQGRMTLEEI LAKVDINAGA RDAEKLNAKA PYDVLIVGGG PAGAAAAIYA ARKGIRTGVV
AERFGGQVLD TMGIENFISV SQTEGPKLVA ALEQHVKDYD VDVMNTQRAT ALSAGKQVSI
TLANGAVLES KSVIIATGAR WREMNVPGEQ EYRGRGVAYC PHCDGPLFKG KQVGVIGGGN
SGVEAAIDLA GIVAHVTLIE FDKELRADAV LQKKLRSLSN VTIITSALTT EVLGNGDKMT
GLTYKNRLDD SAHELALDGV FVQIGLLPNT DWLKGSVALS PRGEIEVDAK GQTSVPGVFA
AGDATTSPYK QIIIAMGEGS KAALSAFDHL IRSSVSEDEV EAA
//
