AHPC_HELPJ
ID AHPC_HELPJ Reviewed; 198 AA.
AC P56876;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 122.
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=jhp_1471;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=915;
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 [3]
RP REDUCTION BY THIOREDOXIN.
RX PubMed=11222594; DOI=10.1128/jb.183.6.1961-1973.2001;
RA Baker L.M., Raudonikiene A., Hoffman P.S., Poole L.B.;
RT "Essential thioredoxin-dependent peroxiredoxin system from Helicobacter
RT pylori: genetic and kinetic characterization.";
RL J. Bacteriol. 183:1961-1973(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS), SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=16213196; DOI=10.1016/j.bbapap.2005.09.001;
RA Papinutto E., Windle H.J., Cendron L., Battistutta R., Kelleher D.,
RA Zanotti G.;
RT "Crystal structure of alkyl hydroperoxide-reductase (AhpC) from
RT Helicobacter pylori.";
RL Biochim. Biophys. Acta 1753:240-246(2005).
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 (PubMed:16213196).
CC {ECO:0000269|PubMed:16213196}.
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 (PubMed:16213196). The disulfide is subsequently
CC reduced by thioredoxin (PubMed:11222594). {ECO:0000269|PubMed:11222594,
CC ECO:0000269|PubMed:16213196}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE001439; AAD07055.1; -; Genomic_DNA.
DR PIR; H71801; H71801.
DR RefSeq; WP_000961648.1; NZ_CP011330.1.
DR PDB; 1ZOF; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J=1-198.
DR PDBsum; 1ZOF; -.
DR AlphaFoldDB; P56876; -.
DR SMR; P56876; -.
DR IntAct; P56876; 2.
DR STRING; 85963.jhp_1471; -.
DR EnsemblBacteria; AAD07055; AAD07055; jhp_1471.
DR KEGG; hpj:jhp_1471; -.
DR PATRIC; fig|85963.30.peg.1071; -.
DR eggNOG; COG0450; Bacteria.
DR OMA; WWPKDFT; -.
DR EvolutionaryTrace; P56876; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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 3D-structure; Antioxidant; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Oxidoreductase; Peroxidase; Redox-active center.
FT CHAIN 1..198
FT /note="Alkyl hydroperoxide reductase C"
FT /id="PRO_0000135145"
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:0000305|PubMed:16213196"
FT DISULFID 49
FT /note="Interchain (with C-169)"
FT /evidence="ECO:0000269|PubMed:16213196,
FT ECO:0007744|PDB:1ZOF"
FT DISULFID 169
FT /note="Interchain (with C-49)"
FT /evidence="ECO:0000269|PubMed:16213196,
FT ECO:0007744|PDB:1ZOF"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:1ZOF"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1ZOF"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1ZOF"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:1ZOF"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:1ZOF"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:1ZOF"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:1ZOF"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:1ZOF"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1ZOF"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1ZOF"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:1ZOF"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1ZOF"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1ZOF"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1ZOF"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:1ZOF"
FT HELIX 148..163
FT /evidence="ECO:0007829|PDB:1ZOF"
SQ SEQUENCE 198 AA; 22259 MW; 3E6C18E6F06D52F0 CRC64;
MLVTKLAPDF KAPAVLGNNE VDEHFELSKN LGKNGVILFF WPKDFTFVCP TEIIAFDKRV
KDFHEKGFNV IGVSIDSEQV HFAWKNTPVE KGGIGQVSFP MVADITKSIS RDYDVLFEEA
IALRGAFLID KNMKVRHAVI NDLPLGRNAD EMLRMVDALL HFEEHGEVCP AGWRKGDKGM
KATHQGVAEY LKENSIKL
