ID A0A3N2M125_9BACT Unreviewed; 524 AA.
AC A0A3N2M125;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000313|EMBL:ROT03184.1};
GN Name=ahpF {ECO:0000313|EMBL:ROT03184.1};
GN ORFNames=EEL33_18385 {ECO:0000313|EMBL:ROT03184.1};
OS Muribaculaceae bacterium Isolate-037 (Harlan).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486461 {ECO:0000313|EMBL:ROT03184.1, ECO:0000313|Proteomes:UP000275399};
RN [1] {ECO:0000313|EMBL:ROT03184.1, ECO:0000313|Proteomes:UP000275399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-037 (Harlan) {ECO:0000313|Proteomes:UP000275399};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
RL Submitted (NOV-2018) 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:ROT03184.1}.
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DR EMBL; RIAZ01000032; ROT03184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2M125; -.
DR Proteomes; UP000275399; 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; 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; 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:UP000275399}.
FT DOMAIN 128..190
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 218..506
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 219..234
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 359..373
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 480..490
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 347..350
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 524 AA; 55595 MW; DC64103E751A85C1 CRC64;
MLDKDIITQL KGIFANLETA FTFVVSGVSS REETRQMVEF VNDFASSSAA FSVKEEDTPT
EENAPTLAIW RDGNPTGVSF CGIPNGHEFT SLILAVLNAA GQGKNLPDEA LRRRIASLQG
PVDMFTFVSL TCTNCPEVVQ SLNIIALINP SFRHVTIDGA VVPEMVKSYN VQSVPTVYAN
GELLSVGRAE LGDLVALLEK KFGSTPNPGE VSDVTLGFDV IVAGGGPAGA AAAIYLSRKG
LRTAIVAGRI GGQVKDTMDI ENLISVPHTT GPELASDLRR HLESYDIAIY DNRRIVDVAL
DGFPKRITTD SGETFEAPQI VIATGASWRR LNIPGENEYI GRGVAFCTHC DGPFFAGKRV
AVIGGGNSGI EAAIDLAAIC EHVDVFEFLD ELKADMVLQK RLTEFDNVAV HLSSAAEEVI
GNGTKVTGIK VKDRKSGESA LYDLDGVFVQ IGLTANSSPF SNQLPVNKAG EIIMKGAGRT
GIPGVYAAGD VTDIPYKQIV IAMGDGATAA LSAVDDRMRG VTPS
//
