ID A0A147GVY9_9BURK Unreviewed; 520 AA.
AC A0A147GVY9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Alkyl hydroperoxide reductase {ECO:0000313|EMBL:KTT21857.1};
GN ORFNames=NS331_10855 {ECO:0000313|EMBL:KTT21857.1};
OS Pseudacidovorax intermedius.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Pseudacidovorax.
OX NCBI_TaxID=433924 {ECO:0000313|EMBL:KTT21857.1, ECO:0000313|Proteomes:UP000072741};
RN [1] {ECO:0000313|EMBL:KTT21857.1, ECO:0000313|Proteomes:UP000072741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS331 {ECO:0000313|EMBL:KTT21857.1,
RC ECO:0000313|Proteomes:UP000072741};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTT21857.1}.
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DR EMBL; LDSL01000064; KTT21857.1; -; Genomic_DNA.
DR RefSeq; WP_058642000.1; NZ_LDSL01000064.1.
DR AlphaFoldDB; A0A147GVY9; -.
DR PATRIC; fig|433924.3.peg.4178; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000072741; 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:UP000072741}.
FT DOMAIN 120..195
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 213..499
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 354..368
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 342..345
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 520 AA; 55377 MW; 8509D8E25F1EB825 CRC64;
MLDAATKAQL SSYLERISQP IEIVAVLDDS PASAQTRELL QDIASTSKLV TVIDQPGSSA
RKPSFSVNKP GQTDGPRFAG LPMGHEFTSL ILAMLQQGGY PPKVEQAILD QIKQLDGDFE
FEVYVSLTCH NCPDVVQALN LMAVQNPRIK ATMIEGGTFQ KEIEDRQIMG VPTVFMNGQM
FGSGRMSLEE ILAKIDTSGV EREAKKLSAK EAFDVLIVGG GPAGAAAAVY AARKGIRTGV
AAERFGGQVL DTLGIENFIS VKETQGPHFA LALDEHVRHY DVDVMNLQRA SALVPGDGLV
EVQMESGATL KAKTVILSTG ARWRNINVPG EQEFKNKGVA YCPHCDGPLF KGKRVAVIGG
GNSGVEAAID LAGIVGHVTL IEYDTQLRAD AVLQRKLTSL PNVTVLTNAQ TTSITGTDKV
NGLTYKDRAT GEEKRVDLEG VFIQIGLVPN TDWLKGTVEL SRHGEIIVDA KGQTSVPGVF
AAGDCTTVPY KQIIIAAGDG AKAALSAFDH LIRTSAPVAA
//
