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Database: UniProt
Entry: V5WM46_9SPIO
LinkDB: V5WM46_9SPIO
Original site: V5WM46_9SPIO 
ID   V5WM46_9SPIO            Unreviewed;       522 AA.
AC   V5WM46;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Alkyl hydroperoxide reductase protein F {ECO:0000313|EMBL:AHC16713.1};
GN   ORFNames=L21SP2_3375 {ECO:0000313|EMBL:AHC16713.1};
OS   Salinispira pacifica.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Salinispira.
OX   NCBI_TaxID=1307761 {ECO:0000313|EMBL:AHC16713.1, ECO:0000313|Proteomes:UP000018680};
RN   [1] {ECO:0000313|EMBL:AHC16713.1, ECO:0000313|Proteomes:UP000018680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-RPul-D2 {ECO:0000313|EMBL:AHC16713.1,
RC   ECO:0000313|Proteomes:UP000018680};
RX   PubMed=26203324; DOI=10.1186/1944-3277-10-7;
RA   Ben Hania W., Joseph M., Schumann P., Bunk B., Fiebig A., Sproer C.,
RA   Klenk H.P., Fardeau M.L., Spring S.;
RT   "Complete genome sequence and description of Salinispira pacifica gen.
RT   nov., sp. nov., a novel spirochaete isolated form a hypersaline microbial
RT   mat.";
RL   Stand. Genomic Sci. 10:7-7(2015).
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}.
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DR   EMBL; CP006939; AHC16713.1; -; Genomic_DNA.
DR   RefSeq; WP_024269601.1; NC_023035.1.
DR   AlphaFoldDB; V5WM46; -.
DR   STRING; 1307761.L21SP2_3375; -.
DR   KEGG; slr:L21SP2_3375; -.
DR   PATRIC; fig|1307761.3.peg.3364; -.
DR   eggNOG; COG3634; Bacteria.
DR   HOGENOM; CLU_031864_1_0_12; -.
DR   OrthoDB; 9806179at2; -.
DR   Proteomes; UP000018680; Chromosome.
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; 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:UP000018680}.
FT   DOMAIN          124..190
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13192"
FT   DOMAIN          215..506
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         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   522 AA;  55555 MW;  355D52D104233CD8 CRC64;
     MLNSKIQEQL KDVFSELEGR VALEYASSEH SKEDELVTML EDVASLSDQI EAVQGDFSHD
     APWFRIVHND TDTGIRFTGV PGGHEFTSLI LAILHSDGKG KLPDSPSIRR IGAIQGPVSI
     RTFVSLSCTN CPDVVQALNL AAVYNPDIEH HTIVGDFAQD EIERLGVQGV PAVFHGDTLI
     HSGRSSLAEL LPVLENTFGR KESGPMEAVE IPAVEVAVIG GGPAGCAAAI YSGRKGLKTA
     IIASRIGGQV NDTADISNFI SVSETTGSKL SADLRKHSGE YDIQIFEGRN VHSVETAGTN
     GSEFHRIFSD SGEVFSAEQL IITSGASWRK LGVPGEDEYI GRGVAFCPHC DGPFFAGKDV
     AVIGGGNSGV EAAIDLAGTC KSITLIEFLD ELKADSVLTA KLKSLDNVEI ITSARTTEIL
     GDGKAVTGIK LEDRSSGEVR SLNLHGAFVQ IGLLPNSSEY HDHVKVNRYG EIEVDTHGRT
     SVPGMYAAGD VTTSPYKQIV IAMGDGAKAA LTAFDDRIRG RV
//
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