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Database: UniProt
Entry: X7EAU6_9GAMM
LinkDB: X7EAU6_9GAMM
Original site: X7EAU6_9GAMM 
ID   X7EAU6_9GAMM            Unreviewed;       515 AA.
AC   X7EAU6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Alkyl hydroperoxide reductase subunit F {ECO:0000256|ARBA:ARBA00020059};
GN   ORFNames=MUS1_01635 {ECO:0000313|EMBL:ETX12326.1};
OS   Marinomonas ushuaiensis DSM 15871.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=1122207 {ECO:0000313|EMBL:ETX12326.1, ECO:0000313|Proteomes:UP000054058};
RN   [1] {ECO:0000313|EMBL:ETX12326.1, ECO:0000313|Proteomes:UP000054058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15871 {ECO:0000313|EMBL:ETX12326.1,
RC   ECO:0000313|Proteomes:UP000054058};
RA   Lai Q., Shao Z.S.;
RT   "Marinomonas ushuaiensis DSM 15871 Genome Sequencing.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:ETX12326.1}.
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DR   EMBL; JAMB01000001; ETX12326.1; -; Genomic_DNA.
DR   RefSeq; WP_036158167.1; NZ_JAMB01000001.1.
DR   AlphaFoldDB; X7EAU6; -.
DR   STRING; 1122207.MUS1_01635; -.
DR   PATRIC; fig|1122207.3.peg.339; -.
DR   eggNOG; COG3634; Bacteria.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000054058; 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:UP000054058}.
FT   DOMAIN          121..196
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13192"
FT   DOMAIN          214..494
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   BINDING         215..230
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         475..485
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   515 AA;  54943 MW;  FD7EA57F2B22D241 CRC64;
     MLEANIKQQL GAYLKNIVNP IEITVSTNGS EKAEELVGLA REITELQSDK ITLSVESNSA
     ERAPQMAIGP KDQAPRVRFA GIPMGHEFTS LILALLQAGG HPSKAAPELL EQIKTLDTEL
     NFEVYISLSC HNCPDIVQAT NLMAALNPKV TATMIDGALF QDEVNGLNIM AVPSVYLNGE
     HFGQGRMTLE EILNKVDTGA ADKQAAALAE KDPYDVLVVG GGPAGAAAAI YAARKGIRTG
     VVAERFGGQV SDTMAIENFI SVKATDGPKL VAGLEQHVLD YDVDLMKTQK AVRLEKKEFV
     EVELENGAIL KSKTVILATG ARWREMNVPG EHEYRGKGVA YCPHCDGPLF KGKKTAVIGG
     GNSGIEAAID LAGIVEHVTV LEFGDTLRAD DVLVRKAESL PNVTIIKEAM TTEVIGDGER
     VIGLKYTDRK TDESHLVDVA GIFVQIGLVP NSEFLKDTLT LSNRGEIVID GHGQTSIPGV
     FAAGDVTTTP YKQIIISMGG GATAALGAFD YLIRN
//
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