AHPC_MYCS2
ID AHPC_MYCS2 Reviewed; 195 AA.
AC A0R1V9; I7FIL4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Alkyl hydroperoxide reductase C;
DE EC=1.11.1.28;
DE AltName: Full=Peroxiredoxin;
DE AltName: Full=Thioredoxin peroxidase;
GN OrderedLocusNames=MSMEG_4891, MSMEI_4766;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP PUPYLATION AT LYS-41, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20094657; DOI=10.1039/b916104j;
RA Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA Barry C.E. III, Bark S., Dorrestein P.C.;
RT "Expansion of the mycobacterial 'PUPylome'.";
RL Mol. Biosyst. 6:376-385(2010).
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. Together with AhpD, DlaT and Lpd, constitutes
CC an NADH-dependent peroxidase active against hydrogen and alkyl
CC peroxides as well as serving as a peroxynitrite reductase, thus
CC protecting the bacterium against reactive nitrogen intermediates and
CC oxidative stress generated by the host immune system. Does not however
CC seem to play a role in detoxification of isoniazid.
CC {ECO:0000250|UniProtKB:P9WQB7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[lipoyl-carrier protein] + a
CC hydroperoxide = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + an
CC alcohol + H2O; Xref=Rhea:RHEA:62636, Rhea:RHEA-COMP:10502, Rhea:RHEA-
CC COMP:16355, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.11.1.28;
CC Evidence={ECO:0000250|UniProtKB:P9WQB7};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 6 homodimers
CC assemble to form a ring-like dodecamer. Identified in a complex with
CC AhpD, DlaT and Lpd. {ECO:0000250|UniProtKB:P9WQB7}.
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 can subsequently be reduced
CC through a mixed disulfide with the C-terminal cysteine of AhpD,
CC resolved by its second cysteine or by thioredoxin (TrxC).
CC {ECO:0000250|UniProtKB:P9WQB7}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000480; ABK73669.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41215.1; -; Genomic_DNA.
DR RefSeq; WP_011730169.1; NZ_SIJM01000024.1.
DR RefSeq; YP_889147.1; NC_008596.1.
DR AlphaFoldDB; A0R1V9; -.
DR SMR; A0R1V9; -.
DR STRING; 246196.MSMEI_4766; -.
DR PRIDE; A0R1V9; -.
DR EnsemblBacteria; ABK73669; ABK73669; MSMEG_4891.
DR EnsemblBacteria; AFP41215; AFP41215; MSMEI_4766.
DR GeneID; 66736196; -.
DR KEGG; msg:MSMEI_4766; -.
DR KEGG; msm:MSMEG_4891; -.
DR PATRIC; fig|246196.56.peg.4874; -.
DR eggNOG; COG0450; Bacteria.
DR OMA; FWYPKDF; -.
DR OrthoDB; 892697at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
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; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF121; PTHR10681:SF121; 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; Disulfide bond; Isopeptide bond; Oxidoreductase;
KW Peroxidase; Redox-active center; Reference proteome; Stress response;
KW Ubl conjugation.
FT CHAIN 1..195
FT /note="Alkyl hydroperoxide reductase C"
FT /id="PRO_0000396111"
FT DOMAIN 4..170
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 61
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P9WQB7"
FT DISULFID 61
FT /note="Interchain (with C-133 in AhpD); transient"
FT /evidence="ECO:0000250|UniProtKB:P9WQB7"
FT DISULFID 61
FT /note="Interchain (with C-174); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P9WQB7"
FT DISULFID 174
FT /note="Interchain (with C-61); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P9WQB7"
FT CROSSLNK 41
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20094657"
SQ SEQUENCE 195 AA; 21626 MW; 556A5C17A5DA937F CRC64;
MALLTIGDQF PEYDLTAVVG GDLSKVDAKQ PDDYFTRVTS KDYEGKWRII FFWPKDFTFV
CPTEIAAFGK LNEDFEDRDA KVLGVSVDNE FVHFQWRAQH EDLKTLPFPM VSDLKRELTA
ACGVLNADGV ADRATFIVDP NNEVQFVSVT AGSVGRNVDE VLRVLDALQS DELCACNWKK
GDPTINAGEL LAGAV
