ID K0UAP9_MYCVA Unreviewed; 155 AA.
AC K0UAP9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824};
GN ORFNames=MVAC_28978 {ECO:0000313|EMBL:EJZ04412.1};
OS Mycolicibacterium vaccae ATCC 25954.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1194972 {ECO:0000313|EMBL:EJZ04412.1, ECO:0000313|Proteomes:UP000006072};
RN [1] {ECO:0000313|EMBL:EJZ04412.1, ECO:0000313|Proteomes:UP000006072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25954 {ECO:0000313|EMBL:EJZ04412.1,
RC ECO:0000313|Proteomes:UP000006072};
RX PubMed=23105074; DOI=10.1128/JB.01462-12;
RA Ho Y.S., Adroub S.A., Abadi M., Al Alwan B., Alkhateeb R., Gao G.,
RA Ragab A., Ali S., van Soolingen D., Bitter W., Pain A., Abdallah A.M.;
RT "Complete Genome Sequence of Mycobacterium vaccae Type Strain ATCC 25954.";
RL J. Bacteriol. 194:6339-6340(2012).
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 and as sensor of hydrogen peroxide-mediated
CC signaling events. {ECO:0000256|ARBA:ARBA00003330}.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00000280};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC {ECO:0000256|ARBA:ARBA00038489}.
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:EJZ04412.1}.
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DR EMBL; ALQA01000120; EJZ04412.1; -; Genomic_DNA.
DR RefSeq; WP_003932102.1; NZ_JH814695.1.
DR AlphaFoldDB; K0UAP9; -.
DR PATRIC; fig|1194972.3.peg.5741; -.
DR eggNOG; COG1225; Bacteria.
DR HOGENOM; CLU_042529_14_2_11; -.
DR Proteomes; UP000006072; Unassembled WGS sequence.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd03017; PRX_BCP; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42801:SF8; PEROXIREDOXIN RV1608C-RELATED; 1.
DR PANTHER; PTHR42801; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 4..155
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 47
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 155 AA; 16852 MW; CA0D8A33C5A50923 CRC64;
MNPLKPGDRV ADFELKDQTG TSRTLTGLLA DGPVVLFFYP AAMTPGCTKE ACHFRDLAAE
FAAVGANRVG ISADPVDKQA AFAEQQKFDY PLLSDTEGVV ATQFGVKRGL LGKLMPVKRT
TFVIDTDRTV LDVIASEFSM DTHADKALET LRRRA
//
