ID A0A0Q8RLS0_9BURK Unreviewed; 526 AA.
AC A0A0Q8RLS0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000313|EMBL:KRB97092.1};
GN ORFNames=ASE26_03400 {ECO:0000313|EMBL:KRB97092.1};
OS Duganella sp. Root198D2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736489 {ECO:0000313|EMBL:KRB97092.1, ECO:0000313|Proteomes:UP000051728};
RN [1] {ECO:0000313|EMBL:KRB97092.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRB97092.1,
RC ECO:0000313|Proteomes:UP000051728};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB97092.1, ECO:0000313|Proteomes:UP000051728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root198D2 {ECO:0000313|EMBL:KRB97092.1,
RC ECO:0000313|Proteomes:UP000051728};
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:KRB97092.1}.
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DR EMBL; LMIC01000012; KRB97092.1; -; Genomic_DNA.
DR RefSeq; WP_055938876.1; NZ_LMIC01000012.1.
DR AlphaFoldDB; A0A0Q8RLS0; -.
DR Proteomes; UP000051728; 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:UP000051728}.
FT DOMAIN 126..194
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 214..501
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 354..368
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 475..485
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 342..345
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 526 AA; 56121 MW; 3E38B025270B43CA CRC64;
MLDADLKAQL SSYLERVVHP IEIVANTDAS AKSQEMSALL QDIVSAGHGK ITIVAGADDK
ARKPSFDITR KGSDIGVSFA GIPMGHEFTS LVLALLQVGG HPIKLDEKVI EQIRNLDGDF
VFETFISLSC HNCPEVVQAL NAMSVINPRI KVVAVDGGVF PKEVEERQVM AVPMMYLNGQ
HFGQGRTNVE EILAKLDTGA SARAAAELSK KDVFDVLIVG GGPAGAAAAI YTARKGIRTG
VIADRFGGQV LDTLSIENFV SVKETDGQKF AVALEQHVKE YDVDIMNTQR ASKIVPGKIK
EVHTESGAVL KARSVIISTG ARWREINVPG EKEYRNHGVA YCPHCDGPLF KGKRVAVIGG
GNSGVEAAID LAGIVEHVTL IEFGAELRAD AVLQRKLATL RNVKVIKSAQ TSEVHGDGKK
VNGLSYTDRE SGQSHRIELE GVFVQIGLVP NTEWLKGTID LSKHGEIEVD AKGQTSETGV
FAAGDVTTVP YKQIVIAVGE GAKAALGSFD YLIRSSADDE PAAIAA
//
