AHPC_HELPY
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 25-MAY-2022, entry version 139.
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; Proteobacteria; 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.C694_08100; -.
DR PaxDb; P21762; -.
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 OMA; WWPKDFT; -.
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:alkylhydroperoxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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 Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 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
