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Database: UniProt
Entry: A0A1X2DCL2_9MYCO
LinkDB: A0A1X2DCL2_9MYCO
Original site: A0A1X2DCL2_9MYCO 
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
//
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