ID A0A1G5SDW5_9PROT Unreviewed; 200 AA.
AC A0A1G5SDW5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Name=tsaA {ECO:0000313|EMBL:SCZ85332.1};
GN ORFNames=NSMM_370111 {ECO:0000313|EMBL:SCZ85332.1};
OS Nitrosomonas mobilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=51642 {ECO:0000313|EMBL:SCZ85332.1, ECO:0000313|Proteomes:UP000198729};
RN [1] {ECO:0000313|EMBL:SCZ85332.1, ECO:0000313|Proteomes:UP000198729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1 {ECO:0000313|EMBL:SCZ85332.1};
RA de Groot N.N.;
RL Submitted (OCT-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|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; FMWO01000044; SCZ85332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5SDW5; -.
DR STRING; 51642.NSMM_370111; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000198729; Unassembled WGS sequence.
DR GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:RHEA.
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,
KW ECO:0000313|EMBL:SCZ85332.1}; Peroxidase {ECO:0000313|EMBL:SCZ85332.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198729}.
FT DOMAIN 3..163
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 200 AA; 22315 MW; B5D506812243A4A0 CRC64;
MSILVTHPAP DFTKPAVLPD GSFDENFNFH THIRDKYAVL FFYPLDFTFV CPSEIIAHSH
RAKDFQRRNV EVIGVSVDSH FTHYAWRNTP ITQGGIGPIN IALVSDLGGE VMNAYGVSHP
DHVALRGSFL IDRKGIVRHQ VVNDLPLGRD VDEMLRMVDA LQFFEERGEL CPAGWKSGEA
GMKASPEGVA EYLSQHADKL
//
