ID A0A1M4TIW0_9BACE Unreviewed; 516 AA.
AC A0A1M4TIW0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000313|EMBL:SHE44217.1};
GN ORFNames=SAMN05444349_102131 {ECO:0000313|EMBL:SHE44217.1};
OS Bacteroides faecichinchillae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=871325 {ECO:0000313|EMBL:SHE44217.1, ECO:0000313|Proteomes:UP000184436};
RN [1] {ECO:0000313|EMBL:SHE44217.1, ECO:0000313|Proteomes:UP000184436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26883 {ECO:0000313|EMBL:SHE44217.1,
RC ECO:0000313|Proteomes:UP000184436};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQVD01000002; SHE44217.1; -; Genomic_DNA.
DR RefSeq; WP_073349088.1; NZ_SSTN01000011.1.
DR AlphaFoldDB; A0A1M4TIW0; -.
DR STRING; 871325.SAMN05444349_102131; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000184436; 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; 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:UP000184436}.
FT DOMAIN 124..184
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 212..498
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 353..367
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 474..484
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 341..344
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 516 AA; 55416 MW; 4A05238AE8D2D403 CRC64;
MLDSALKEQL KDIFAGLGAN FTFDINVSSQ HEDRNELLEL LEDVAACSDH LTCSVNEGDG
LEFTILKNGA RTGITFRGIP NGHEFTSLLL AILNLDGKGK NFPDEGVCNR VKALKGPIHL
TTYVSLTCTN CPDVVQALNA MTTLNPSISH EMVDGALNQE EVETLKIQGV PSVFADGKLI
HVGRGEFGEL LAKLEEQYGV DEASLSTEEK LYDVIVAGGG PAGVSAAIYS ARKGLKVAIV
AERVGGQVKE TVGIENLISV PETTGSELAD NLKTHLLRYP VDLLEHRKIE KVELVGKEKQ
VTTSVGEKLT TPALIIATGA SWRKLNVPGE TEYIGRGVAF CSHCDGPFYV GKHVAVVGGG
NSGIEAAIDL ASICSRVTVF EFMDELKADQ VLQEKLRSLS NVEVFVSSQT TEVIGNGDKL
TALRVKDRKT EEERVIELDG VFVQIGLTAN SGVFRDLVET NRPGEIVIDA FCRTNVPGIY
AAGDVSTVPY KQIIISMGEG AKAALSAFDD RVRGNI
//
