ID E5WR80_9BACI Unreviewed; 187 AA.
AC E5WR80;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
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 ORFNames=HMPREF1013_04970 {ECO:0000313|EMBL:EFV74712.1};
OS Bacillus sp. 2_A_57_CT2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV74712.1, ECO:0000313|Proteomes:UP000003283};
RN [1] {ECO:0000313|EMBL:EFV74712.1, ECO:0000313|Proteomes:UP000003283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV74712.1,
RC ECO:0000313|Proteomes:UP000003283};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL Submitted (DEC-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:EFV74712.1}.
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DR EMBL; ACWD01000072; EFV74712.1; -; Genomic_DNA.
DR RefSeq; WP_009335870.1; NZ_GL635759.1.
DR AlphaFoldDB; E5WR80; -.
DR GeneID; 67522272; -.
DR eggNOG; COG0450; Bacteria.
DR HOGENOM; CLU_042529_21_3_9; -.
DR Proteomes; UP000003283; 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|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU366004};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366004}; Peroxidase {ECO:0000256|RuleBase:RU366004};
KW Redox-active center {ECO:0000256|RuleBase:RU366004};
KW Reference proteome {ECO:0000313|Proteomes:UP000003283}.
FT DOMAIN 2..157
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 47
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 187 AA; 20794 MW; 7D6895DF26EE6504 CRC64;
MALIGSEVLP FAAKAYHNGD FIDVTEENFK GKWSVVCFYP ADFTFVCPTE LEDLQNEYAT
LKDMGAEVYS VSTDTHFTHK AWHDNSETIN KIEYVMIGDP NQRISRNFEV LNEEDGLAER
GTFIIDPDGI IQTVEINAGG IGRDASQVVS KLKAAQYVRN NPGEVCPAKW KEGSETLKPS
LDLVGKI
//
