ID A0A3N1X664_9BURK Unreviewed; 532 AA.
AC A0A3N1X664;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000313|EMBL:ROR21551.1};
GN ORFNames=EC845_2373 {ECO:0000313|EMBL:ROR21551.1};
OS Comamonas sp. BIGb0124.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=2485130 {ECO:0000313|EMBL:ROR21551.1, ECO:0000313|Proteomes:UP000267274};
RN [1] {ECO:0000313|EMBL:ROR21551.1, ECO:0000313|Proteomes:UP000267274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIGb0124 {ECO:0000313|EMBL:ROR21551.1,
RC ECO:0000313|Proteomes:UP000267274};
RA Samuel B.;
RT "Genomic analyses of the natural microbiome of Caenorhabditis elegans.";
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:ROR21551.1}.
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DR EMBL; RJVF01000010; ROR21551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1X664; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000267274; 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:UP000267274}.
FT DOMAIN 127..195
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 215..504
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 216..231
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 356..370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 478..488
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 344..347
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 532 AA; 56214 MW; 00B01F74C362D665 CRC64;
MLDANLKAQL KTYLERVSQP IEIVASLDDT PKSQETLGLL QDIDGLSDRI TLVVRRGEDA
DVRKPSFSIS QPGGVPGIRF AGLPMGHEFT SLVLALLQVG GHPSKAAQEV IEQVRNLQGP
LHFETYFSLS CQNCPDVVQA LNLMAVLNPN VRHVAIDGGV FPKEVEQRQV MSVPTVYLNG
EPFAQGRMGL EEILGKVDTG AAARGAEKLN AQAPFDVLVV GGGPAGAAAA IYAARKGIRT
GVAAERFGGQ VLDTLGIENF ISVKETEGPK LAAALEEHVK AYDVDIMNLQ RAESLRRTAQ
GVEVQFASGA RLTGKTVVIA TGARWREMNV PGEAEYRNKG VAYCPHCDGP LFKGKRVAVV
GGGNSGVEAA IDLAGLVAHV TLLEFGAELR ADAVLQRKLR SLANVEVITQ AQTTEVTGDG
TKVNGLVYTD RATGASHRVA LEGVFVQIGL VPNSSWLKDS GVELSKFGEI VVNARGETTL
PGVFAAGDVT TTPYKQIIIA MGEGSKAALS AFDHLIRETA PADAVAAEAV TA
//
