ID A0A140NM76_PROSM Unreviewed; 200 AA.
AC A0A140NM76;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Alkyl hydroperoxide reductase C {ECO:0000256|ARBA:ARBA00017462};
DE EC=1.11.1.26 {ECO:0000256|ARBA:ARBA00013021};
DE AltName: Full=Peroxiredoxin {ECO:0000256|ARBA:ARBA00032077};
GN OrderedLocusNames=S70_06925 {ECO:0000313|EMBL:AFH93256.1};
OS Providencia stuartii (strain MRSN 2154).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1157951 {ECO:0000313|EMBL:AFH93256.1, ECO:0000313|Proteomes:UP000005012};
RN [1] {ECO:0000313|EMBL:AFH93256.1, ECO:0000313|Proteomes:UP000005012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154 {ECO:0000313|EMBL:AFH93256.1,
RC ECO:0000313|Proteomes:UP000005012};
RX PubMed=22740665; DOI=10.1128/JB.00615-12;
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete Genome Sequence of Providencia stuartii Clinical Isolate MRSN
RT 2154.";
RL J. Bacteriol. 194:3736-3737(2012).
RN [2] {ECO:0000313|Proteomes:UP000005012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSN 2154 {ECO:0000313|Proteomes:UP000005012};
RA Clifford R.J., Hang J., Riley M.C., Onmus-Leone F., Kuschner R.A.,
RA Lesho E.P., Waterman P.E.;
RT "Complete genome sequence of Providencia stuartii clinical isolate MRSN
RT 2154.";
RL Submitted (APR-2012) 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|ARBA:ARBA00037420}.
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:0000256|ARBA:ARBA00000318};
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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DR EMBL; CP003488; AFH93256.1; -; Genomic_DNA.
DR RefSeq; WP_004926964.1; NC_017731.1.
DR AlphaFoldDB; A0A140NM76; -.
DR GeneID; 79055105; -.
DR KEGG; psi:S70_06925; -.
DR PATRIC; fig|1157951.4.peg.1376; -.
DR HOGENOM; CLU_042529_21_1_6; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000005012; Chromosome.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; THIOREDOXIN PEROXIDASE; 1.
DR PANTHER; PTHR10681:SF128; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 2..163
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 50
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 200 AA; 22328 MW; F9ADD9CF75992A94 CRC64;
MVLVTRQAPD FTAAAVLGNG EIVDNFNLKN HLNGRPAVIF FWPMDFTFVC PSELIAFDHR
YEEFKKRGVE VIGVSFDSEF VHNAWRKTPV DNGGIGEVKY PMVADVKREI MKAYGIEHPE
AGVALRGSFL VDKNGVVRHQ VVNDLPLGRN IDEMLRMVDA LQFHEEHGDV CPAQWEKGKE
GMNASPKGVA DYLTKNATGL
//
