ID A0A0D6DX25_9LACT Unreviewed; 509 AA.
AC A0A0D6DX25;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Alkyl hydroperoxide reductase protein F AhpF {ECO:0000313|EMBL:CEN28508.1};
GN Name=ahpF {ECO:0000313|EMBL:CEN28508.1};
GN ORFNames=LACPI_1308 {ECO:0000313|EMBL:CEN28508.1};
OS Lactococcus piscium MKFS47.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=297352 {ECO:0000313|EMBL:CEN28508.1, ECO:0000313|Proteomes:UP000033166};
RN [1] {ECO:0000313|Proteomes:UP000033166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MKFS47 {ECO:0000313|Proteomes:UP000033166};
RA Andreevskaya M.;
RL Submitted (JAN-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}.
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DR EMBL; LN774769; CEN28508.1; -; Genomic_DNA.
DR RefSeq; WP_047915631.1; NZ_LN774769.1.
DR AlphaFoldDB; A0A0D6DX25; -.
DR STRING; 1364.LP2241_30307; -.
DR KEGG; lpk:LACPI_1308; -.
DR HOGENOM; CLU_031864_4_2_9; -.
DR Proteomes; UP000033166; Chromosome I.
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}.
FT DOMAIN 124..195
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 209..495
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 210..225
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 349..363
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 469..479
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 337..340
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 509 AA; 55103 MW; ACA092E619906613 CRC64;
MLEENLKTQL KQYLELLEND IVLRLNADIN ETNGKKVHDF VTEIADMSPK ISIEKTTAIK
SPGFSVDQKD TISGIVFAGL PLGHEFNSLV LALLQVSGRA PKIEDELKER IQSIRQPYHF
ETYVSLTCHN CPDVVQALNI MSVLNQNVSH TMIEGGMFQD EVNSRGVMAV PTVFVNDEEF
SSGRMSLEEI LNKLIGQAGS EAFEEKDPYD VLVVGGGPAG ASAAIYAARK GIRTGILAEK
FGGQPLETLG IENFIGTTYT EGPKLAAQLE EHVKSYPVDV MKTQKAIKLA KNELVEVTLE
NGAVLQSKTV VLSTGARWRS LGIPGEETFK NKGIAYCPHC DGPLFAGKKI AVVGGGNSGI
EAAIDLAGVV EHVTVLEFLP ELKADKVLQD KLYSLDNVTV LTNVETKAIY GQDKVDSLAY
MDRDTQEVLT LELAGVFILI GLVPNTEWLE GSVDRTARGE IIVDKQGATN LPGVYAAGDC
TDSVYKQIII AMGSGATAAL GAFDYIIRH
//
