ID A0A3R6IJZ5_9BACT Unreviewed; 528 AA.
AC A0A3R6IJZ5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000313|EMBL:RHO67701.1};
GN Name=ahpF {ECO:0000313|EMBL:RHO67701.1};
GN ORFNames=DW083_17125 {ECO:0000313|EMBL:RHO67701.1};
OS Parabacteroides sp. AF48-14.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=2292052 {ECO:0000313|EMBL:RHO67701.1, ECO:0000313|Proteomes:UP000283361};
RN [1] {ECO:0000313|EMBL:RHO67701.1, ECO:0000313|Proteomes:UP000283361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF48-14 {ECO:0000313|EMBL:RHO67701.1,
RC ECO:0000313|Proteomes:UP000283361};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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:RHO67701.1}.
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DR EMBL; QUDI01000041; RHO67701.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R6IJZ5; -.
DR Proteomes; UP000283361; 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; 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; 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; 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}.
FT DOMAIN 124..185
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 216..511
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 217..232
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 364..378
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 485..495
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 352..355
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 528 AA; 56244 MW; 1FCD650967B7188F CRC64;
MLDSAMKSQL SGIFSGLASQ YVFEIEVSPN HESRQELIEL LGDVASCSDH LSCHISDGEG
LQFTIVKDGA PTGIRFRAVP NGHEFTSLLL AILNSDGKGK NIPDESIRAR VSALNGPIKL
TTYVSLTCTN CPDVVQALNV MTTLNSQITH ETVDGAINQK EVEAMKVQGV PSVFADGKLI
HVGRSDFGEL LSKLEAQYGI NEETVDNSVE KPVKNYDVIV VGGGPAGAAS AIYSARKGLS
VAVVAERVGG QVKETVGIEN LVSVPHTTGE QLANDLRTHI NDYPIDILEH RRIVSVSVET
DGRLSPSRST ILTTSTGERF SASAVIVATG ASWRKLNVPG EAEYIGRGVA FCPHCDGPFY
KGKHVAVVGG GNSGIEAAID LAGICSKVTV LEFMDELKAD QVLQEKLKSL PNVEVFLHSQ
SLEVIGNGDK VIGLRVKDRK TEAERVIDLD GIFVQIGLAA NSGAFRDVVE TNKPGEIVID
AHCRTNVPGI YAAGDVSTVP YKQIIIAMGE GAKAALSAFE DRMRGLLS
//
