AHPC_SALTY
ID AHPC_SALTY Reviewed; 187 AA.
AC P0A251; P19479;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Alkyl hydroperoxide reductase C {ECO:0000303|PubMed:2191951};
DE EC=1.11.1.26 {ECO:0000269|PubMed:2643600};
DE AltName: Full=Alkyl hydroperoxide reductase protein C22 {ECO:0000303|PubMed:2643600};
DE AltName: Full=Peroxiredoxin;
DE AltName: Full=Thioredoxin peroxidase;
GN Name=ahpC {ECO:0000303|PubMed:2191951}; OrderedLocusNames=STM0608;
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].
RC STRAIN=TN1379;
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 SEQUENCE REVISION TO C-TERMINUS, AND FUNCTION.
RX PubMed=8041738; DOI=10.1073/pnas.91.15.7017;
RA Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G.;
RT "Cloning and sequencing of thiol-specific antioxidant from mammalian brain:
RT alkyl hydroperoxide reductase and thiol-specific antioxidant define a large
RT family of antioxidant enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7017-7021(1994).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=2693740; DOI=10.1016/0022-2836(89)90104-6;
RA Tartaglia L.A., Storz G., Ames B.N.;
RT "Identification and molecular analysis of oxyR-regulated promoters
RT important for the bacterial adaptation to oxidative stress.";
RL J. Mol. Biol. 210:709-719(1989).
RN [5]
RP PROTEIN SEQUENCE OF 2-33, AND SUBUNIT.
RX PubMed=8555198; DOI=10.1021/bi951887s;
RA Poole L.B., Ellis H.R.;
RT "Flavin-dependent alkyl hydroperoxide reductase from Salmonella
RT typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF
RT and AhpC proteins.";
RL Biochemistry 35:56-64(1996).
RN [6]
RP PROTEIN SEQUENCE OF 2-25, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
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).
RN [7]
RP REDUCTION BY AHPF.
RX PubMed=7592740; DOI=10.1074/jbc.270.43.25645;
RA Niimura Y., Poole L.B., Massey V.;
RT "Amphibacillus xylanus NADH oxidase and Salmonella typhimurium alkyl-
RT hydroperoxide reductase flavoprotein components show extremely high
RT scavenging activity for both alkyl hydroperoxide and hydrogen peroxide in
RT the presence of S. typhimurium alkyl-hydroperoxide reductase 22-kDa protein
RT component.";
RL J. Biol. Chem. 270:25645-25650(1995).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT.
RX PubMed=11969410; DOI=10.1021/bi012173m;
RA Wood Z.A., Poole L.B., Hantgan R.R., Karplus P.A.;
RT "Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine
RT peroxiredoxins.";
RL Biochemistry 41:5493-5504(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF MUTANT SER-47.
RX PubMed=12714747; DOI=10.1126/science.1080405;
RA Wood Z.A., Poole L.B., Karplus P.A.;
RT "Peroxiredoxin evolution and the regulation of hydrogen peroxide
RT signaling.";
RL Science 300:650-653(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), DISULFIDE BONDS, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=16060667; DOI=10.1021/bi050448i;
RA Parsonage D., Youngblood D.S., Sarma G.N., Wood Z.A., Karplus P.A.,
RA Poole L.B.;
RT "Analysis of the link between enzymatic activity and oligomeric state in
RT AhpC, a bacterial peroxiredoxin.";
RL Biochemistry 44:10583-10592(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS), AND ACTIVE SITE.
RX PubMed=18986167; DOI=10.1021/bi801718d;
RA Nelson K.J., Parsonage D., Hall A., Karplus P.A., Poole L.B.;
RT "Cysteine pK(a) values for the bacterial peroxiredoxin AhpC.";
RL Biochemistry 47:12860-12868(2008).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS).
RX PubMed=24175952; DOI=10.1021/bi4011573;
RA Perkins A., Nelson K.J., Williams J.R., Parsonage D., Poole L.B.,
RA Karplus P.A.;
RT "The sensitive balance between the fully folded and locally unfolded
RT conformations of a model peroxiredoxin.";
RL Biochemistry 52:8708-8721(2013).
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:0000269|PubMed:2643600,
CC ECO:0000269|PubMed:8041738}.
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:0000269|PubMed:2643600};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 uM for H(2)O(2) {ECO:0000269|PubMed:16060667};
CC Note=kcat is 55.1 sec(-1) with H(2)O(2) as substrate.
CC {ECO:0000269|PubMed:16060667};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (PubMed:2643600,
CC PubMed:8555198). 5 homodimers assemble to form a ring-like decamer
CC (PubMed:11969410). {ECO:0000269|PubMed:11969410,
CC ECO:0000269|PubMed:2643600, ECO:0000269|PubMed:8555198}.
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 AhpF.
CC {ECO:0000269|PubMed:7592740, ECO:0000305|PubMed:2643600}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J05478; AAA16431.1; -; Unassigned_DNA.
DR EMBL; AE006468; AAL19559.1; -; Genomic_DNA.
DR PIR; A35441; A35441.
DR RefSeq; NP_459600.1; NC_003197.2.
DR RefSeq; WP_000052802.1; NC_003197.2.
DR PDB; 1N8J; X-ray; 2.17 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=2-187.
DR PDB; 1YEP; X-ray; 2.50 A; A/B/C/D/E=2-187.
DR PDB; 1YEX; X-ray; 2.30 A; A/B/C/D/E=2-187.
DR PDB; 1YF0; X-ray; 2.50 A; A/B/C/D/E=2-187.
DR PDB; 1YF1; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J=2-187.
DR PDB; 3EMP; X-ray; 4.00 A; A/B/C/D/E=2-187.
DR PDB; 4MA9; X-ray; 1.82 A; A/B/C/D/E=2-187.
DR PDB; 4MAB; X-ray; 1.90 A; A/B/C/D/E=2-187.
DR PDB; 4XRA; X-ray; 1.75 A; A/B/C/D/E=2-187.
DR PDB; 4XRD; X-ray; 2.30 A; A/B/C/D/E=2-187.
DR PDB; 4XS1; X-ray; 2.10 A; A/B/C/D/E=2-187.
DR PDB; 4XS4; X-ray; 2.65 A; A/B/C/D/E=2-187.
DR PDB; 4XS6; X-ray; 3.35 A; A/B/C/D/E=2-187.
DR PDB; 4XTS; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=2-187.
DR PDB; 5UKA; X-ray; 1.90 A; A/B/C/D/E=2-187.
DR PDBsum; 1N8J; -.
DR PDBsum; 1YEP; -.
DR PDBsum; 1YEX; -.
DR PDBsum; 1YF0; -.
DR PDBsum; 1YF1; -.
DR PDBsum; 3EMP; -.
DR PDBsum; 4MA9; -.
DR PDBsum; 4MAB; -.
DR PDBsum; 4XRA; -.
DR PDBsum; 4XRD; -.
DR PDBsum; 4XS1; -.
DR PDBsum; 4XS4; -.
DR PDBsum; 4XS6; -.
DR PDBsum; 4XTS; -.
DR PDBsum; 5UKA; -.
DR AlphaFoldDB; P0A251; -.
DR SMR; P0A251; -.
DR STRING; 99287.STM0608; -.
DR PeroxiBase; 4829; SetypAhpC.
DR PaxDb; P0A251; -.
DR EnsemblBacteria; AAL19559; AAL19559; STM0608.
DR GeneID; 1252128; -.
DR GeneID; 66755075; -.
DR KEGG; stm:STM0608; -.
DR PATRIC; fig|99287.12.peg.640; -.
DR HOGENOM; CLU_042529_21_3_6; -.
DR OMA; FWYPKDF; -.
DR PhylomeDB; P0A251; -.
DR BioCyc; SENT99287:STM0608-MON; -.
DR BRENDA; 1.11.1.24; 5542.
DR BRENDA; 1.11.1.26; 5542.
DR EvolutionaryTrace; P0A251; -.
DR Proteomes; UP000001014; 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 GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR InterPro; IPR017559; AhpC.
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:SF121; PTHR10681:SF121; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR03137; AhpC; 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;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2643600,
FT ECO:0000269|PubMed:8555198"
FT CHAIN 2..187
FT /note="Alkyl hydroperoxide reductase C"
FT /id="PRO_0000135120"
FT DOMAIN 2..157
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 47
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000305|PubMed:18986167"
FT DISULFID 47
FT /note="Interchain (with C-166); in linked form"
FT /evidence="ECO:0000269|PubMed:16060667,
FT ECO:0007744|PDB:1YEP, ECO:0007744|PDB:1YEX,
FT ECO:0007744|PDB:1YF0, ECO:0007744|PDB:1YF1"
FT DISULFID 166
FT /note="Interchain (with C-47); in linked form"
FT /evidence="ECO:0000269|PubMed:16060667,
FT ECO:0007744|PDB:1YEP, ECO:0007744|PDB:1YEX,
FT ECO:0007744|PDB:1YF0, ECO:0007744|PDB:1YF1"
FT CONFLICT 2
FT /note="S -> G (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 5
FT /note="N -> D (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="Q -> N (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="K -> H (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="E -> H (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="E -> S (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:4XRA"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:4XRA"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:4XRA"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4XRA"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4MA9"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:4XRA"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:4XRA"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:4XRA"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:4XRA"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4XRA"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:4XRA"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:4XRA"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:4XRA"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:4XS6"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4XRA"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:4XRA"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:5UKA"
FT HELIX 145..160
FT /evidence="ECO:0007829|PDB:4XRA"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4XS1"
FT TURN 182..186
FT /evidence="ECO:0007829|PDB:4XRA"
SQ SEQUENCE 187 AA; 20747 MW; 83B251C74DE9860D CRC64;
MSLINTKIKP FKNQAFKNGE FIEVTEKDTE GRWSVFFFYP ADFTFVCPTE LGDVADHYEE
LQKLGVDVYS VSTDTHFTHK AWHSSSETIA KIKYAMIGDP TGALTRNFDN MREDEGLADR
ATFVVDPQGI IQAIEVTAEG IGRDASDLLR KIKAAQYVAA HPGEVCPAKW KEGEATLAPS
LDLVGKI
