AHPF_SALTY
ID AHPF_SALTY Reviewed; 521 AA.
AC P19480;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Alkyl hydroperoxide reductase subunit F;
DE EC=1.8.1.-;
DE AltName: Full=Alkyl hydroperoxide reductase F52A protein;
GN Name=ahpF; OrderedLocusNames=STM0609;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2191951; DOI=10.1016/s0021-9258(18)86980-0;
RA Tartaglia L.A., Storz G., Brodsky M.H., Lai A., Ames B.N.;
RT "Alkyl hydroperoxide reductase from Salmonella typhimurium. Sequence and
RT homology to thioredoxin reductase and other flavoprotein disulfide
RT oxidoreductases.";
RL J. Biol. Chem. 265:10535-10540(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP PROTEIN SEQUENCE OF 1-25.
RC STRAIN=oxyR1;
RX PubMed=2643600; DOI=10.1016/s0021-9258(18)94214-6;
RA Jacobson F.S., Morgan R.W., Christman M.F., Ames B.N.;
RT "An alkyl hydroperoxide reductase from Salmonella typhimurium involved in
RT the defense of DNA against oxidative damage. Purification and properties.";
RL J. Biol. Chem. 264:1488-1496(1989).
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.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; J05478; AAA16432.1; -; Unassigned_DNA.
DR EMBL; AE006468; AAL19560.1; -; Genomic_DNA.
DR PIR; B35441; B35441.
DR RefSeq; NP_459601.1; NC_003197.2.
DR RefSeq; WP_000887644.1; NC_003197.2.
DR PDB; 1HYU; X-ray; 2.00 A; A=1-521.
DR PDB; 1ZYN; X-ray; 2.30 A; A/B=1-202.
DR PDB; 1ZYP; X-ray; 2.40 A; A/B=1-202.
DR PDBsum; 1HYU; -.
DR PDBsum; 1ZYN; -.
DR PDBsum; 1ZYP; -.
DR AlphaFoldDB; P19480; -.
DR BMRB; P19480; -.
DR SMR; P19480; -.
DR DIP; DIP-2906N; -.
DR STRING; 99287.STM0609; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR PaxDb; P19480; -.
DR PRIDE; P19480; -.
DR EnsemblBacteria; AAL19560; AAL19560; STM0609.
DR GeneID; 1252129; -.
DR KEGG; stm:STM0609; -.
DR PATRIC; fig|99287.12.peg.641; -.
DR HOGENOM; CLU_031864_0_0_6; -.
DR OMA; VTVFEFM; -.
DR PhylomeDB; P19480; -.
DR BioCyc; SENT99287:STM0609-MON; -.
DR EvolutionaryTrace; P19480; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW NAD; NADP; Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..521
FT /note="Alkyl hydroperoxide reductase subunit F"
FT /id="PRO_0000166777"
FT DOMAIN 109..208
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 214..229
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 357..371
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 478..488
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT DISULFID 345..348
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 9
FT /note="Q -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="E -> DR (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:1HYU"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:1HYU"
FT TURN 332..341
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 365..377
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 394..400
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 411..419
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 421..431
FT /evidence="ECO:0007829|PDB:1HYU"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:1HYU"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:1HYU"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:1HYU"
FT HELIX 497..518
FT /evidence="ECO:0007829|PDB:1HYU"
SQ SEQUENCE 521 AA; 55950 MW; 813DEA1398DAE26F CRC64;
MLDTNMKTQL RAYLEKLTKP VELIATLDDS AKSAEIKELL AEIAELSDKV TFKEDNTLPV
RKPSFLITNP GSQQGPRFAG SPLGHEFTSL VLALLWTGGH PSKEAQSLLE QIRDIDGDFE
FETYYSLSCH NCPDVVQALN LMAVLNPRIK HTAIDGGTFQ NEITERNVMG VPAVFVNGKE
FGQGRMTLTE IVAKVDTGAE KRAAEALNKR DAYDVLIVGS GPAGAAAAVY SARKGIRTGL
MGERFGGQVL DTVDIENYIS VPKTEGQKLA GALKAHVSDY DVDVIDSQSA SKLVPAATEG
GLHQIETASG AVLKARSIII ATGAKWRNMN VPGEDQYRTK GVTYCPHCDG PLFKGKRVAV
IGGGNSGVEA AIDLAGIVEH VTLLEFAPEM KADQVLQDKV RSLKNVDIIL NAQTTEVKGD
GSKVVGLEYR DRVSGDIHSV ALAGIFVQIG LLPNTHWLEG ALERNRMGEI IIDAKCETSV
KGVFAAGDCT TVPYKQIIIA TGEGAKASLS AFDYLIRTKI A
