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Database: UniProt
Entry: A0A0L0MBT2_9BURK
LinkDB: A0A0L0MBT2_9BURK
Original site: A0A0L0MBT2_9BURK 
ID   A0A0L0MBT2_9BURK        Unreviewed;       527 AA.
AC   A0A0L0MBT2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Alkyl hydroperoxide reductase protein F {ECO:0000313|EMBL:KND59736.1};
GN   ORFNames=BVER_00405c {ECO:0000313|EMBL:KND59736.1};
OS   Candidatus Burkholderia verschuerenii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=242163 {ECO:0000313|EMBL:KND59736.1, ECO:0000313|Proteomes:UP000036959};
RN   [1] {ECO:0000313|Proteomes:UP000036959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot4 {ECO:0000313|Proteomes:UP000036959};
RA   Carlier A., Eberl L., Pinto-Carbo M.;
RT   "Comparative genomics of Burkholderia leaf nodule symbionts.";
RL   Submitted (JUN-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:KND59736.1}.
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DR   EMBL; LFJJ01000105; KND59736.1; -; Genomic_DNA.
DR   RefSeq; WP_050454422.1; NZ_LFJJ01000105.1.
DR   AlphaFoldDB; A0A0L0MBT2; -.
DR   PATRIC; fig|242163.4.peg.528; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000036959; 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:UP000036959}.
FT   DOMAIN          125..193
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13192"
FT   DOMAIN          213..500
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         353..367
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT   BINDING         474..484
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT   DISULFID        341..344
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ   SEQUENCE   527 AA;  56394 MW;  7D85FEF18EF5E898 CRC64;
     MLDANLKTQL KAYLEKVTRP IELVAFLDGS DKSKELKSLL DEIASLTTQI SVVEKDDAGA
     RRPSFSIGEP GKTPGITFAG IPMGHEFTSL VLALLQTGGH PIKLDDATIE QIKRLDGDFS
     FETYFSLSCQ NCPEVVQALN VMALINPRIK HIAIDGALFQ AEVDERQVMA VPMMFLNGQN
     FGSGRTGVKE ILAKLDLGSA ERAAKELENK PVFDTLIVGG GPAGAAAAIY SARKGIATGV
     VAERFGGQVL DTMSIENFVS IKETEGPKFA VALEQHVKEY EVDVMDVQRA EKLVPGRINE
     IHLASGAVLK AKTIILATGA RWREIGAPGE REYRGRGVAY CPHCDGPLFK GKRVAVIGGG
     NSGVEAAIDL ANIVAHVTLI EFGAELRADA VLQKKLRSLS NVVIITQGQT TEVTGDGKRV
     NGIVYKDRAT NEEKRIELEG VFVQIGLVPN TEWLKGSIEL SKFGEIVVDA KGATSIPGVF
     AAGDVTTVSY KQIVIAVGEG AKASLSAFDH LIRSSVEDEV VEEAVTA
//
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