ID A0A0R2CUH6_9LACO Unreviewed; 522 AA.
AC A0A0R2CUH6;
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:KRM95457.1};
GN ORFNames=FC24_GL002131 {ECO:0000313|EMBL:KRM95457.1};
OS Loigolactobacillus rennini DSM 20253.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=1423796 {ECO:0000313|EMBL:KRM95457.1, ECO:0000313|Proteomes:UP000051638};
RN [1] {ECO:0000313|EMBL:KRM95457.1, ECO:0000313|Proteomes:UP000051638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20253 {ECO:0000313|EMBL:KRM95457.1,
RC ECO:0000313|Proteomes:UP000051638};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM95457.1}.
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DR EMBL; AYYI01000068; KRM95457.1; -; Genomic_DNA.
DR RefSeq; WP_057874463.1; NZ_AYYI01000068.1.
DR AlphaFoldDB; A0A0R2CUH6; -.
DR STRING; 1423796.FC24_GL002131; -.
DR PATRIC; fig|1423796.3.peg.2160; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000051638; 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:UP000051638}.
FT DOMAIN 126..192
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 212..498
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 213..228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 352..366
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 472..482
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 340..343
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 522 AA; 55426 MW; 63D41CBCEF7605A6 CRC64;
MAIEQTVKQQ LAAYLKLLEQ DVVLTADLGD DTHSQKVSDF IKEVAAMSPK ISVAKGHLKR
QPSFTIDQAN QPSSGIEFAG VPLGHEFTSF VLALLQVSGH APKISATLKQ QIQSIDAELH
FETFASLSCH NCPDVVQALN IMSVLNPKIS HTMIEGGMYQ DEATQKNVMA VPTVFLNGEE
WHTGRATLEE LVDKASGGAP QALTDDWTDQ QFDVVIVGGG PAAGSAAIYA ARKGVATAIV
ADHFGGQPLD TAGIENLAGI DHIEGEKLMA NVQAQVEKYG VHVLTGQHVT AVRKEDQVKI
DLASGNTLTA RTVIIATGAQ WKHIGVPGET EFKNKGVAYC PHCDGPLYAG KDVAVIGGGN
SGIEAAIDMA GICKHVTVLE FSANFGADSV LQAKARDLDN VTLIANAATK EITGDGRVNG
LTYTDRETQE THHLDLEGVF IQIGLQPNTD WVTAPIELNA RHEIMTDTKQ ATDVPGIFAA
GDCTDSAYKQ IIVAMGSGAT AALSAFDYLV RNDVAAKQPV TN
//
