ID A0A239SPA9_9BURK Unreviewed; 530 AA.
AC A0A239SPA9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000313|EMBL:SNU87237.1};
DE EC=1.8.1.- {ECO:0000313|EMBL:SNU87237.1};
GN Name=ahpF {ECO:0000313|EMBL:SNU87237.1};
GN ORFNames=SAMEA4530655_03748 {ECO:0000313|EMBL:SNU87237.1};
OS Pandoraea sputorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=93222 {ECO:0000313|EMBL:SNU87237.1, ECO:0000313|Proteomes:UP000215126};
RN [1] {ECO:0000313|EMBL:SNU87237.1, ECO:0000313|Proteomes:UP000215126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13161 {ECO:0000313|EMBL:SNU87237.1,
RC ECO:0000313|Proteomes:UP000215126};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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}.
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DR EMBL; LT906435; SNU87237.1; -; Genomic_DNA.
DR RefSeq; WP_039400414.1; NZ_LT906435.1.
DR AlphaFoldDB; A0A239SPA9; -.
DR STRING; 93222.NA29_22815; -.
DR KEGG; pspu:NA29_22815; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000215126; Chromosome 1.
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 ECO:0000313|EMBL:SNU87237.1};
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..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 530 AA; 56604 MW; 380042657BA76AD0 CRC64;
MLDANLKAQL QTYLQKVTRP IEIAVWLDDS PKSAEMKALV EEIAPLSDKI AVVARTDADE
RRPSFAIGTP GEAPRIRFAG LPMGHEFTSL VLALLQVGGH PLKLDDDTIE QVRALDGDFR
FETYISLSCQ NCPEVVQALN VMALINPRIQ QVTIDGALFQ SEVEARQVMA VPTVFLNGES
FTQGRTSVKE LLAKLDTGAT ARAAKALENK PVYDMLIVGG GPAGAAAAIY AARKGIATGV
VAERFGGQVL DTMAIENFVS VTHTEGPKFA TALEQHVKTY DVDVIDTQRA EALIPGKIHE
VHLASGAVLK ARAVVLATGA RWREIGAPGE REYRNRGVAY CPHCDGPLFK GKRVAVVGGG
NSGVEAAIDL AGIVKDVTLI EYGTQLRADE VLQRKLRSLP NVRVLMNAQT TEIVGDGQKV
NGLTYLNRAT GERSTIALEG VFVQIGLVPN TEWLKGTVSL SRHGEIEVDA KGTTSVPGVF
AAGDVTTVPF KQIVIAVGEG AKASLGAFEH LMLSSVDDEV DAERNEAAVA
//
