ID A0A154R335_9GAMM Unreviewed; 537 AA.
AC A0A154R335;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000256|ARBA:ARBA00020059};
GN ORFNames=RhoFW510R10_12415 {ECO:0000313|EMBL:KZC32518.1};
OS Rhodanobacter sp. FW510-R10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1524462 {ECO:0000313|EMBL:KZC32518.1, ECO:0000313|Proteomes:UP000076310};
RN [1] {ECO:0000313|EMBL:KZC32518.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW510-R10 {ECO:0000313|EMBL:KZC32518.1};
RX PubMed=27048805; DOI=10.1128/mBio.02234-15;
RA Hemme C.L., Green S.J., Rishishwar L., Prakash O., Pettenato A.,
RA Chakraborty R., Deutschbauer A.M., Van Nostrand J.D., Wu L., He Z.,
RA Jordan I.K., Hazen T.C., Arkin A.P., Kostka J.E., Zhou J.;
RT "Lateral Gene Transfer in a Heavy Metal-Contaminated-Groundwater Microbial
RT Community.";
RL MBio 7:e02234-e02215(2016).
CC -!- FUNCTION: Serves to protect the cell against DNA damage by alkyl
CC hydroperoxides. It can use either NADH or NADPH as electron donor for
CC direct reduction of redox dyes or of alkyl hydroperoxides when combined
CC with the AhpC protein. {ECO:0000256|ARBA:ARBA00024806}.
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:KZC32518.1}.
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DR EMBL; LVJU01000020; KZC32518.1; -; Genomic_DNA.
DR RefSeq; WP_068091710.1; NZ_LVJU01000020.1.
DR AlphaFoldDB; A0A154R335; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000076310; 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}.
FT DOMAIN 129..196
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13192"
FT DOMAIN 217..509
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 218..233
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 362..376
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT BINDING 483..493
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-1"
FT DISULFID 350..353
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000238-2"
SQ SEQUENCE 537 AA; 56997 MW; 9D33B41634EC1FE1 CRC64;
MLDANLKTQL KAYLEKVTQP IEIVASLDDS AKSAELNELL EEIAALSDRI SLVRRDDDAR
KPSFAINRVG SDISVRFAGI PLGHEFTSLV LALLQVGGHP SKAAADVIEQ VKNLDGPAPD
GVFRFETYFS LSCQNCPDVV QALNLMSVLN PKIRHVAIDG ALYQDEVETR QVMSVPTVFL
NGEVFDQGRM SLEQILARLD TGAAQREAEK IEAKDAFDVL VVGGGPAGAA AAIYAARKGI
RTGVAAERFG GQVLDTMAIE NFISVTATDG PKMGAALEQH VKEYDVDVMN LQSAEKLVPA
SDATGGLVEV RLANGATLKS KTVILSTGAR WRQMGVPGED EYRNKGVAYC PHCDGPLFKG
KRVAVIGGGN SGVEAAIDLA GIVAHVTLVE FDGKLRADEV LQRKLRSLPN VDVVVSAQST
EVLGDGQKVT GLVYKDRVDG VMHSLELEGI FVQIGLLPNT EWLKGTLELS PRGEIVIDAR
GQTSLPGVFA AGDATTVPYK QIVIAMGAGS TAALGAFDHL IRSPVAAAKP EKQAVAA
//
