ID A0A0D6EU66_9PROT Unreviewed; 188 AA.
AC A0A0D6EU66;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:CEZ19040.1};
GN ORFNames=BN1208_0145 {ECO:0000313|EMBL:CEZ19040.1}, FIT69_00660
GN {ECO:0000313|EMBL:QDD01119.1};
OS Candidatus Methylopumilus planktonicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylopumilus.
OX NCBI_TaxID=1581557 {ECO:0000313|EMBL:CEZ19040.1, ECO:0000313|Proteomes:UP000064007};
RN [1] {ECO:0000313|Proteomes:UP000064007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000064007};
RA Salcher M.M.;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CEZ19040.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MMS-10A-171 {ECO:0000313|EMBL:CEZ19040.1};
RA Salcher M Michaela;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QDD01119.1, ECO:0000313|Proteomes:UP000314748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-VB-116 {ECO:0000313|EMBL:QDD01119.1,
RC ECO:0000313|Proteomes:UP000314748};
RA Salcher M., Schaefle D., Kaspar M., Neuenschwander S.M., Ghai R.;
RT "Evolution in action: Habitat-transition from sediment to pelagial leads to
RT genome-streamlining in Methylophilaceae.";
RL ISME J. 0:0-0(2019).
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; LN827929; CEZ19040.1; -; Genomic_DNA.
DR EMBL; CP040978; QDD01119.1; -; Genomic_DNA.
DR RefSeq; WP_046486793.1; NZ_LN827929.1.
DR AlphaFoldDB; A0A0D6EU66; -.
DR STRING; 1581557.BN1208_0145; -.
DR KEGG; mbat:BN1208_0145; -.
DR HOGENOM; CLU_042529_21_3_4; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000064007; Chromosome 1.
DR Proteomes; UP000314748; 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:CEZ19040.1};
KW Redox-active center {ECO:0000256|RuleBase:RU366004};
KW Reference proteome {ECO:0000313|Proteomes:UP000064007}.
FT DOMAIN 3..158
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 48
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 188 AA; 20763 MW; 0062D12C0673EEE8 CRC64;
MSSLVNTEVK PFKATAFHNG KFVDVTEANL KGKWSVVIFM PAAFTFNCPT EVEDAADHYA
EFQKVGAEVY IVTTDTHFSH KVWHETSPAV GKSKFPLVGD PTHQLTRAFE VHIDEEGLAL
RGTFIINPKG EIKTMEVHDN AIARDVKETL RKLKAAQYVA NNPGQVCPAK WQEGAKTIAP
SLDLVGKI
//