AHPF_PSEPK
ID AHPF_PSEPK Reviewed; 520 AA.
AC P0A155; O82864;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE EC=1.8.1.-;
GN Name=ahpF; OrderedLocusNames=PP_2440;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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 (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE015451; AAN68052.1; -; Genomic_DNA.
DR RefSeq; NP_744588.1; NC_002947.4.
DR RefSeq; WP_010953390.1; NC_002947.4.
DR AlphaFoldDB; P0A155; -.
DR SMR; P0A155; -.
DR STRING; 160488.PP_2440; -.
DR EnsemblBacteria; AAN68052; AAN68052; PP_2440.
DR KEGG; ppu:PP_2440; -.
DR PATRIC; fig|160488.4.peg.2585; -.
DR eggNOG; COG3634; Bacteria.
DR HOGENOM; CLU_031864_4_2_6; -.
DR OMA; VTVFEFM; -.
DR PhylomeDB; P0A155; -.
DR BioCyc; PPUT160488:G1G01-2607-MON; -.
DR Proteomes; UP000000556; 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; cd03026; AhpF_NTD_C; 1.
DR CDD; cd02974; AhpF_NTD_N; 1.
DR Gene3D; 3.50.50.60; -; 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 Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF13192; Thioredoxin_3; 1.
DR PIRSF; PIRSF000238; AhpF; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF52833; SSF52833; 2.
DR TIGRFAMs; TIGR03140; AhpF; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; FAD; Flavoprotein; NAD; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..520
FT /note="Alkyl hydroperoxide reductase subunit F"
FT /id="PRO_0000166775"
FT BINDING 213..228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 355..369
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 476..486
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 343..346
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 520 AA; 55350 MW; 08FB3DE0D75C8A27 CRC64;
MLDATLKSQL KTYLERVTQP IEIVASLDDG AKSRELHDLL VEIASLSNLI TFSADGTDAR
RPSFSLNRPG ADISLRFAGI PMGHEFTSLV LALLQVGGHP SKASAEVIEQ IQALEGEFNF
ETYFSLSCQN CPDVVQALNL MAVLNPNVRH VAIDGALFQD EVESRKIMAV PSIYLNGEVF
GQGRMGLEEI LGKIDTNAGA RQAEKINAKE AFDVLVVGGG PAGAAAAIYA ARKGIRTGVA
AERFGGQVLD TLAIENFISV QETEGPKLAT ALEEHVKQYD VDIMNLQRGE ALIPAAEGGL
HEVRLAGGAS LKAKTVILAT GARWREMNVP GEQEYRGRGV AYCPHCDGPL FKGKRVAVIG
GGNSGVEAAI DLAGIVAQVT LIEFDSQLRA DAVLQRKLRS LPNVNVITSA LTTEVLGNGE
KVTGLRYKDR STDEQHEVAL EGIFVQIGLL PNTDWLKGTV ELSPRGEIIV DAKGQTSIPG
VFAAGDVTTV PYKQIVIAVG EGAKASLAAF DHLIRTSAPA