ID A0A0Q5Z9Q6_9BURK Unreviewed; 522 AA.
AC A0A0Q5Z9Q6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000313|EMBL:KQT10242.1};
GN ORFNames=ASG30_10325 {ECO:0000313|EMBL:KQT10242.1};
OS Ramlibacter sp. Leaf400.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT10242.1, ECO:0000313|Proteomes:UP000051173};
RN [1] {ECO:0000313|EMBL:KQT10242.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT10242.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT10242.1, ECO:0000313|Proteomes:UP000051173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf400 {ECO:0000313|EMBL:KQT10242.1,
RC ECO:0000313|Proteomes:UP000051173};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQT10242.1}.
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DR EMBL; LMQL01000011; KQT10242.1; -; Genomic_DNA.
DR RefSeq; WP_055897885.1; NZ_LMQL01000011.1.
DR AlphaFoldDB; A0A0Q5Z9Q6; -.
DR STRING; 1736365.ASG30_10325; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000051173; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051173}.
FT DOMAIN 121..195
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 214..500
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 215..230
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 522 AA; 55760 MW; 59BCD87F28CCE4AC CRC64;
MLDAQLKTQL AAYLERISQP VEITAVLDDS PASREMQALL KDIAEASPLM RVVETRDAGP
HRAPSFAVNR PGQNHGPRFA GLPMGHEFTS LVLALLQVGG YPPKVEQELL EQIRAIDQDL
EFEVYVSLTC HNCPDVVQAL NLMAVQNPRI RTTMIEGGLF QDEIEQRQIM GVPTVFLNGT
MFGNGRMTLE EIVAKVDANA GQREAQKISG KDPFDVLIVG GGPAGAAAAV YAARKGIRTG
IASERFGGQV LDTLGIENFV SIKETEGPKF ALALEEHVRH YDVDIMNLQR AKALKPGSGL
IEVELENGAA LKARSVILST GARWRKLGVP GEEQYRNKGV AYCPHCDGPL FKGKRVAVVG
GGNSGVEAAI DLAGIVSHVT LIEFGDQLRA DAVLQSKLAS LPNVTTILNA QTTEVTGDGQ
KVNGLVWQDR ASGESRRVDL EGVFVQIGLV PNTEWLKGTL ELSRHGEIVV DAKGQTSIPG
VFAAGDATTV PFKQIIIAAG DGAKAALGAF DHLIRSPAPV AA
//
