ID A7H055_CAMC5 Unreviewed; 199 AA.
AC A7H055;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Alkyl hydroperoxide reductase protein, peroxidase component {ECO:0000313|EMBL:EAU01022.1};
DE EC=1.8.1.- {ECO:0000313|EMBL:EAU01022.1};
GN Name=ahpC {ECO:0000313|EMBL:EAU01022.1};
GN ORFNames=CCV52592_1698 {ECO:0000313|EMBL:EAU01022.1};
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105 {ECO:0000313|EMBL:EAU01022.1, ECO:0000313|Proteomes:UP000006380};
RN [1] {ECO:0000313|Proteomes:UP000006380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92 {ECO:0000313|Proteomes:UP000006380};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-2007) 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 -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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DR EMBL; CP000767; EAU01022.1; -; Genomic_DNA.
DR RefSeq; WP_011992648.1; NC_009715.2.
DR AlphaFoldDB; A7H055; -.
DR STRING; 360105.CCV52592_1698; -.
DR KEGG; ccv:CCV52592_1698; -.
DR HOGENOM; CLU_042529_21_1_7; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000006380; Chromosome.
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:EAU01022.1}; Peroxidase {ECO:0000313|EMBL:EAU01022.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006380}.
FT DOMAIN 1..162
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 49
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 199 AA; 22110 MW; A2FADD3150E49583 CRC64;
MLVTKKAPDF TAAAVLGNNQ IVNDFNLYKN IGEKGTVVFF YPMDFTFVCP SEIIAFDKRY
DEFKARGIEV IGVSCDNQFS HFAWKETPVN KGGIGKVRFP IVADMTKSIA RGFDVLLEDA
GVALRGSFLL DKDGTVRHAV INDLPLGRNI DEMIRMVDTM LFTNEHGEVC PAGWHKGDEG
MKPSTEGVAD YLSHNENKL
//
