ID A0A418XNU5_9PSED Unreviewed; 200 AA.
AC A0A418XNU5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, 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 ORFNames=D3879_13215 {ECO:0000313|EMBL:RJG14125.1};
OS Pseudomonas cavernicola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2320866 {ECO:0000313|EMBL:RJG14125.1, ECO:0000313|Proteomes:UP000284021};
RN [1] {ECO:0000313|EMBL:RJG14125.1, ECO:0000313|Proteomes:UP000284021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1S02-6 {ECO:0000313|EMBL:RJG14125.1,
RC ECO:0000313|Proteomes:UP000284021};
RA Zhu H.;
RL Submitted (SEP-2018) 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}.
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:RJG14125.1}.
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DR EMBL; QYUR01000002; RJG14125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418XNU5; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000284021; 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:RJG14125.1}; Peroxidase {ECO:0000313|EMBL:RJG14125.1}.
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; 21728 MW; B840D96E051AEF37 CRC64;
MSVLVGKQAP DFNVAAVLGN GEIVDSFSLS SAIKGKYGLV FFYPLDFTFV CPSELIALDH
RIPEFKARNV EVIGVSIDSH FTHNAWRNTP VDKGGIGQVK YTLAADVKHE IAKAYDVESA
DGVAFRGAFL IDLNGVVRSQ IVNDLPLGRN MDELLRLVDA LQFTEEHGEV CPANWKKGDK
GMTATPEGVA SYLAENASKL
//