ID A0A1X2DCL2_9MYCO Unreviewed; 231 AA.
AC A0A1X2DCL2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00401};
DE EC=1.11.1.24 {ECO:0000256|HAMAP-Rule:MF_00401};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|HAMAP-Rule:MF_00401};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00401};
GN ORFNames=AWC22_11125 {ECO:0000313|EMBL:ORW85878.1};
OS Mycobacterium riyadhense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=486698 {ECO:0000313|EMBL:ORW85878.1, ECO:0000313|Proteomes:UP000193087};
RN [1] {ECO:0000313|EMBL:ORW85878.1, ECO:0000313|Proteomes:UP000193087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45176 {ECO:0000313|EMBL:ORW85878.1,
RC ECO:0000313|Proteomes:UP000193087};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00401}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00401};
CC -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
CC structure. {ECO:0000256|HAMAP-Rule:MF_00401}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00401}.
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. Although the primary
CC sequence of this enzyme is similar to those of the 1-Cys Prx6 enzymes,
CC its catalytic properties resemble those of the typical 2-Cys Prxs and
CC C(R) is provided by the other dimeric subunit to form an intersubunit
CC disulfide. The disulfide is subsequently reduced by thioredoxin.
CC {ECO:0000256|HAMAP-Rule:MF_00401}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00401}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORW85878.1}.
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DR EMBL; LQPQ01000027; ORW85878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2DCL2; -.
DR STRING; 486698.AWC22_11125; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000193087; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR HAMAP; MF_00401; Peroxiredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR022915; Peroxiredoxin_TDXH.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681:SF171; PEROXIREDOXIN-4; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 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 3: Inferred from homology;
KW Antioxidant {ECO:0000256|HAMAP-Rule:MF_00401};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00401};
KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00401};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00401}; Peroxidase {ECO:0000256|HAMAP-Rule:MF_00401};
KW Redox-active center {ECO:0000256|HAMAP-Rule:MF_00401}.
FT DOMAIN 2..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 44
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT ACT_SITE 44
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 44
FT /note="Interchain (with Cys-212); in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 206..212
FT /note="Alternate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
FT DISULFID 212
FT /note="Interchain (with Cys-44); in linked form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00401"
SQ SEQUENCE 231 AA; 25839 MW; 76235603257626B4 CRC64;
MPRIGETAPA FSALTTQGEI NFPRDYEGKW VILFSHPADF TPVCTTELMT FALMQQQFAA
YNTELVGLSV DGLYSHIAWL RTIKDKIAFR DLKNIEISYP VIEDVAMDVA KKYGMIMPGE
DSSKAVRAVF VVDHKGTIRA IIYYPLSLGR NFKELLRVVK ALQTADHFGV ATPADWRPGE
PVILPAPGSS GTAQERMETQ VGDAHCEDWF FCTKELTVDE VESAIRIRPH V
//