ID A0A2S0N237_9BURK Unreviewed; 522 AA.
AC A0A2S0N237;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000313|EMBL:AVO42212.1};
GN ORFNames=C6571_13760 {ECO:0000313|EMBL:AVO42212.1};
OS Simplicispira suum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=2109915 {ECO:0000313|EMBL:AVO42212.1, ECO:0000313|Proteomes:UP000239326};
RN [1] {ECO:0000313|EMBL:AVO42212.1, ECO:0000313|Proteomes:UP000239326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC1-8 {ECO:0000313|EMBL:AVO42212.1,
RC ECO:0000313|Proteomes:UP000239326};
RA Kim S.-J., Heo J., Kwon S.-W.;
RT "Genome sequencing of Simplicispira sp.";
RL Submitted (MAR-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 ---------------------------------------------------------------------------
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; CP027669; AVO42212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0N237; -.
DR KEGG; simp:C6571_13760; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000239326; 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; 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 Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000238-2}.
FT DOMAIN 126..192
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 213..504
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 214..229
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 357..371
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 345..348
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 522 AA; 55627 MW; 8A2C360AF5E63E65 CRC64;
MLDDNLKTQL KAYLERLQRP VELVATLDDS ATSNELRELL QDIRAQSDKI TVVENNALDV
RKPSFLITNP GQDSGVRFAG VPLGHEFTSL VLALLQVGGH PSKEAADLLE QIKALEGDFH
FETYYSLSCH NCPDVVQALN LMSVLNPRIT HTAIDGGVFQ KEIEAREVMG VPTVFLNGER
FGQGRMELAE VVAKLDTGAG ARDAARLNAK EPFDVLIVGG GPAGAAAAVY AARKGIRTGV
AAERFGGQVL DTVGIDNFLS VQHTEGPQFA AAMERHVRDY EVDIMNLQRA TALVPASTEG
GLIEVQFENG ASLKSRTVIV STGARWRNMN VPGEEEYRTK GVTNCPHCDG PLFKGKHVAV
IGGGNSGVEA AIDLAGVVAR VTVLEFAPEL KADAVLQRKL LSMPNVTVIT NAQTTQVVGD
GSKVTGLNYT DRATGEAQDI ALEGIFVQIG LLPSTDWLKG TVELSRFGEV QIDGHGRTDV
PGVFAAGDCT TVPFKQIVIA AGDGAKAALS AFDHLIRTTA PA
//
