ID E7NVQ8_TREPH Unreviewed; 190 AA.
AC E7NVQ8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Alkyl hydroperoxide reductase C {ECO:0000256|ARBA:ARBA00017462, ECO:0000256|RuleBase:RU366004};
DE EC=1.11.1.26 {ECO:0000256|ARBA:ARBA00013021, ECO:0000256|RuleBase:RU366004};
DE AltName: Full=Peroxiredoxin {ECO:0000256|ARBA:ARBA00032077, ECO:0000256|RuleBase:RU366004};
DE AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824, ECO:0000256|RuleBase:RU366004};
GN Name=ahpC {ECO:0000313|EMBL:EFW37339.1};
GN ORFNames=HMPREF9554_02171 {ECO:0000313|EMBL:EFW37339.1};
OS Treponema phagedenis F0421.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=754027 {ECO:0000313|EMBL:EFW37339.1, ECO:0000313|Proteomes:UP000004157};
RN [1] {ECO:0000313|EMBL:EFW37339.1, ECO:0000313|Proteomes:UP000004157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0421 {ECO:0000313|EMBL:EFW37339.1,
RC ECO:0000313|Proteomes:UP000004157};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2010) 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|RuleBase:RU366004}.
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 ECO:0000256|RuleBase:RU366004};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU366004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU366004}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796, ECO:0000256|RuleBase:RU366004}.
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:EFW37339.1}.
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DR EMBL; AEFH01000185; EFW37339.1; -; Genomic_DNA.
DR RefSeq; WP_002699590.1; NZ_GL638085.1.
DR AlphaFoldDB; E7NVQ8; -.
DR STRING; 162.TPHV1_190008; -.
DR GeneID; 57754277; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_21_3_12; -.
DR Proteomes; UP000004157; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR GO; GO:0006979; P:response to oxidative stress; IEA:UniProtKB-UniRule.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR017559; AhpC.
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 NCBIfam; TIGR03137; AhpC; 1.
DR PANTHER; PTHR10681:SF121; ALKYL HYDROPEROXIDE REDUCTASE C; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 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 Antioxidant {ECO:0000256|RuleBase:RU366004};
KW Cytoplasm {ECO:0000256|RuleBase:RU366004};
KW Disulfide bond {ECO:0000256|RuleBase:RU366004};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366004};
KW Peroxidase {ECO:0000256|RuleBase:RU366004, ECO:0000313|EMBL:EFW37339.1};
KW Redox-active center {ECO:0000256|RuleBase:RU366004}.
FT DOMAIN 5..160
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 190 AA; 21256 MW; B2F8BA3B5CD3B00A CRC64;
MENFNLIGRK IADFKLPAYH DGKFIEVSNE TIKGSWAVFM FYPADFTFVC PTELADLGHV
YPQFKEIGCK VFSVSTDSEF VHKAWADATD TIRNLPYPMI SDKTGKFADS FGILIHDAWQ
ALRGTFVIDP NGIIKAYEVH DLGIGRDADE LLRKVEAAQF VEKHGDQVCP AKWRPGSKTL
TPGIDLVGKL
//
