ID   AHPC_HELPY              Reviewed;         198 AA.
AC   P21762;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Alkyl hydroperoxide reductase C;
DE            EC=1.11.1.26 {ECO:0000250|UniProtKB:P0A251};
DE   AltName: Full=26 kDa antigen;
DE   AltName: Full=Peroxiredoxin;
DE   AltName: Full=Thioredoxin peroxidase;
GN   Name=ahpC; Synonyms=tsaA; OrderedLocusNames=HP_1563;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-46.
RX   PubMed=1987145; DOI=10.1128/jb.173.2.505-513.1991;
RA   O'Toole P.W., Logan S.M., Kostrzynska M., Wadstrom T., Trust T.J.;
RT   "Isolation and biochemical and molecular analyses of a species-specific
RT   protein antigen from the gastric pathogen Helicobacter pylori.";
RL   J. Bacteriol. 173:505-513(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides. {ECO:0000250|UniProtKB:P0A251}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+);
CC         Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.11.1.26;
CC         Evidence={ECO:0000250|UniProtKB:P0A251};
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
CC       assemble to form a ring-like decamer. {ECO:0000250|UniProtKB:P0A251}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AE08}.
CC   -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC       residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC       attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC       cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC       cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC       bridge. The disulfide is subsequently reduced by an appropriate
CC       electron donor to complete the catalytic cycle. In this typical 2-Cys
CC       peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC       intersubunit disulfide. The disulfide is subsequently reduced by
CC       thioredoxin. {ECO:0000250|UniProtKB:P56876}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; M55507; AAA18984.1; -; Unassigned_DNA.
DR   EMBL; AE000511; AAD08603.1; -; Genomic_DNA.
DR   PIR; C64715; C64715.
DR   RefSeq; NP_208354.1; NC_000915.1.
DR   RefSeq; WP_000961643.1; NC_018939.1.
DR   AlphaFoldDB; P21762; -.
DR   SMR; P21762; -.
DR   DIP; DIP-3646N; -.
DR   IntAct; P21762; 3.
DR   MINT; P21762; -.
DR   STRING; 85962.HP_1563; -.
DR   PaxDb; 85962-C694_08100; -.
DR   DNASU; 899728; -.
DR   EnsemblBacteria; AAD08603; AAD08603; HP_1563.
DR   GeneID; 66522755; -.
DR   KEGG; hpy:HP_1563; -.
DR   PATRIC; fig|85962.47.peg.1680; -.
DR   eggNOG; COG0450; Bacteria.
DR   InParanoid; P21762; -.
DR   OrthoDB; 9812811at2; -.
DR   PhylomeDB; P21762; -.
DR   BRENDA; 1.11.1.24; 2604.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   PANTHER; PTHR10681:SF128; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Antioxidant; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW   Oxidoreductase; Peroxidase; Redox-active center; Reference proteome.
FT   CHAIN           1..198
FT                   /note="Alkyl hydroperoxide reductase C"
FT                   /id="PRO_0000135144"
FT   DOMAIN          2..161
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        49
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P56876"
FT   DISULFID        49
FT                   /note="Interchain (with C-169)"
FT                   /evidence="ECO:0000250|UniProtKB:P56876"
FT   DISULFID        169
FT                   /note="Interchain (with C-49)"
FT                   /evidence="ECO:0000250|UniProtKB:P56876"
FT   CONFLICT        36
FT                   /note="A -> V (in Ref. 1; AAA18984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        64
FT                   /note="Q -> H (in Ref. 1; AAA18984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="T -> S (in Ref. 1; AAA18984)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   198 AA;  22236 MW;  599E2FF491CEA0BC CRC64;
     MLVTKLAPDF KAPAVLGNNE VDEHFELSKN LGKNGAILFF WPKDFTFVCP TEIIAFDKRV
     KDFQEKGFNV IGVSIDSEQV HFAWKNTPVE KGGIGQVTFP MVADITKSIS RDYDVLFEEA
     IALRGAFLID KNMKVRHAVI NDLPLGRNAD EMLRMVDALL HFEEHGEVCP AGWRKGDKGM
     KATHQGVAEY LKENSIKL
//