ID I3WFG9_BIFBI Unreviewed; 187 AA.
AC I3WFG9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, 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:AFL03632.1};
GN ORFNames=BBB_0035 {ECO:0000313|EMBL:AFL03632.1};
OS Bifidobacterium bifidum BGN4.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=484020 {ECO:0000313|EMBL:AFL03632.1, ECO:0000313|Proteomes:UP000006173};
RN [1] {ECO:0000313|EMBL:AFL03632.1, ECO:0000313|Proteomes:UP000006173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGN4 {ECO:0000313|EMBL:AFL03632.1,
RC ECO:0000313|Proteomes:UP000006173};
RX PubMed=22887663; DOI=10.1128/JB.00988-12;
RA Yu D.S., Jeong H., Lee D.H., Kwon S.K., Song J.Y., Kim B.K., Park M.S.,
RA Ji G.E., Oh T.K., Kim J.F.;
RT "Complete Genome Sequence of the Probiotic Bacterium Bifidobacterium
RT bifidum Strain BGN4.";
RL J. Bacteriol. 194:4757-4758(2012).
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}.
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DR EMBL; CP001361; AFL03632.1; -; Genomic_DNA.
DR RefSeq; WP_003817384.1; NC_017999.1.
DR AlphaFoldDB; I3WFG9; -.
DR GeneID; 56628272; -.
DR KEGG; bbf:BBB_0035; -.
DR PATRIC; fig|484020.3.peg.33; -.
DR HOGENOM; CLU_042529_21_3_11; -.
DR Proteomes; UP000006173; Chromosome.
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:AFL03632.1};
KW Redox-active center {ECO:0000256|RuleBase:RU366004};
KW Reference proteome {ECO:0000313|Proteomes:UP000006173}.
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; 21152 MW; 54A67E2C4C7E7F98 CRC64;
MTLLQHELTD FTVQAFQNNE FHEVTKADVL GHWSVFFFYP ADFTFVCPTE LEDLAAKYED
FKKIGCEIYS VSCDTHFVHK AWHDANEKIA KIQYPMLADP TALLAKDLDT YNEADGVAER
GDFIVNPEGK VVAYEVISSN VGRNADELLR RVQASQFVYE HGDQVCPAKW TPGEETIEPS
LDLVGLL
//
