ID A0A1B1S9F7_9BACT Unreviewed; 519 AA.
AC A0A1B1S9F7; A0A1Z2XJ81;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000313|EMBL:ANU63427.1};
GN ORFNames=A4V02_06630 {ECO:0000313|EMBL:ANU63427.1};
OS Muribaculum intestinale.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae;
OC Muribaculum.
OX NCBI_TaxID=1796646 {ECO:0000313|EMBL:ANU63427.1, ECO:0000313|Proteomes:UP000186351};
RN [1] {ECO:0000313|Proteomes:UP000186351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL27 {ECO:0000313|Proteomes:UP000186351};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-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}.
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DR EMBL; CP015402; ANU63427.1; -; Genomic_DNA.
DR RefSeq; WP_068960754.1; NZ_PUEE01000019.1.
DR AlphaFoldDB; A0A1B1S9F7; -.
DR STRING; 1796646.A4V02_06630; -.
DR GeneID; 65536527; -.
DR KEGG; pary:A4V02_06630; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000186351; Chromosome.
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:UP000186351}.
FT DOMAIN 126..196
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 215..502
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 216..231
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 355..369
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 476..486
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 343..346
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 519 AA; 54750 MW; 5E9295F003D48BD9 CRC64;
MLDKDIIEQL KSIFGNLKSD IVFLLQQSDN AAQSSEMKSF LDDVASTSPH LSVVESNDKA
EAPTFEIVKN GQPTGVKFCG IPNGHEFTTL LLAILNSDGQ GKNLPDETLA SRIKVLKGPI
DLQTFVSLTC TNCPDVAQAL NIIAILNPSV QNTVIDGAVV PELVQPLNIQ SVPSVYADGK
PFSVGRSSLG DLLEKLESVY GFSDNTALQP VTREYDVIIL GGGPAGAAAA VYCARKGFNT
AVIAKSVGGQ VRETMDIENL ISVPKTTGPQ LAADLKTHLS QYAIDIFEDR NVDSADVTGS
EKTLVCGNET FKGKALIIAT GAGWRKLSIP GESEHIGHGV AFCTHCDGPF YAGKRVAVIG
GGNSGIEAAI DLAAMCPHVD VFEFLDTLKA DGVLQSKSAD MNNIDIHVSS QVTEIIGDGK
NVSGIKVKDR VSGAETVYPV SGVFVQIGLV PNSSLFKDSI AITRSGEIIV DERCRTSVNG
VYAAGDVTTV PYKQIVVAMG EGAKAALSVF EDSMRGMLG
//
