ID F6G7F1_RALS8 Unreviewed; 524 AA.
AC F6G7F1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Alkyl hydroperoxide reductase, f52a subunit, fad/nad(P)-binding protein {ECO:0000313|EMBL:AEG70886.1};
GN Name=ahpF {ECO:0000313|EMBL:AEG70886.1};
GN OrderedLocusNames=RSPO_m00245 {ECO:0000313|EMBL:AEG70886.1};
OS Ralstonia solanacearum (strain Po82).
OG Plasmid {ECO:0000313|Proteomes:UP000007953}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1031711 {ECO:0000313|EMBL:AEG70886.1, ECO:0000313|Proteomes:UP000007953};
RN [1] {ECO:0000313|EMBL:AEG70886.1, ECO:0000313|Proteomes:UP000007953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Po82 {ECO:0000313|Proteomes:UP000007953};
RX PubMed=21685279; DOI=10.1128/JB.05384-11;
RA Xu J., Zheng H.J., Liu L., Pan Z.C., Prior P., Tang B., Xu J.S., Zhang H.,
RA Tian Q., Zhang L.Q., Feng J.;
RT "Complete genome sequence of the plant pathogen Ralstonia solanacearum
RT strain Po82.";
RL J. Bacteriol. 193:4261-4262(2011).
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; CP002820; AEG70886.1; -; Genomic_DNA.
DR RefSeq; WP_014618549.1; NC_017575.1.
DR AlphaFoldDB; F6G7F1; -.
DR KEGG; rsn:RSPO_m00245; -.
DR PATRIC; fig|1031711.3.peg.3510; -.
DR HOGENOM; CLU_031864_4_0_4; -.
DR Proteomes; UP000007953; Plasmid megaplasmid.
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 Plasmid {ECO:0000313|EMBL:AEG70886.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000238-2}.
FT DOMAIN 125..194
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 524 AA; 56119 MW; 3C9A730ED6D40230 CRC64;
MLDADVKAQL KSYLERLVQP IELVASIDDS EGSRDMMDLL RDVAGQSSLI ALNEQRDDAE
RKPSFLIRRT GTDVGVRFAA IPTGHEFTSL VLALLQVGGY APKLDDDTIE QIRNLDGDFR
FETYMSLTCQ NCPDVVQALN VMSVINPRIQ HVAIDGGLFQ DEVEARKIMA VPTLFMNGEV
FSQGRMGVEE ILAKIDTGAA ERDAEKLNAR APYDVLIVGG GPAGAAAAVY AARKGVRTGV
VAERFGGQVL DTLAIENFVS VQETEGPKFA AALEQHVRQY GVDIMNAQRA VKLVPADEPG
GLSEVTLANG AVLKGRSIIL STGARWRNVN VPGEQEYRNR GVAYCPHCDG PLFKGKRVAV
IGGGNSGVEA AIDLAGIVSH VTLLEFGDQL KADAVLVRKL ESLPNATILT NAQTTEITGN
GEKVNGLRYK NRTSGVEHNV ALEGVFVQIG LVPNTEWLDG VVERNRFGEV IVDARGHTSV
PGVFAAGDST TVPFKQIIIA TGEGAKAALS AFDHLIRVPL AEAA
//
