ID A0A062Y3G5_9BACT Unreviewed; 195 AA.
AC A0A062Y3G5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:KDA54936.1};
GN ORFNames=EG19_03800 {ECO:0000313|EMBL:KDA54936.1}, ENQ31_06685
GN {ECO:0000313|EMBL:HET47835.1};
OS Thermoanaerobaculum aquaticum.
OC Bacteria; Acidobacteriota; Thermoanaerobaculia; Thermoanaerobaculales;
OC Thermoanaerobaculaceae; Thermoanaerobaculum.
OX NCBI_TaxID=1312852 {ECO:0000313|EMBL:KDA54936.1, ECO:0000313|Proteomes:UP000027284};
RN [1] {ECO:0000313|EMBL:KDA54936.1, ECO:0000313|Proteomes:UP000027284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP-01 {ECO:0000313|EMBL:KDA54936.1,
RC ECO:0000313|Proteomes:UP000027284};
RA Stamps B.W., Losey N.A., Lawson P.A., Stevenson B.S.;
RT "The Genome Sequence of Thermoanaerobaculum aquaticum MP-01, The First
RT Cultivated Group 23 Acidobacterium.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:HET47835.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SpSt-299 {ECO:0000313|EMBL:HET47835.1};
RX PubMed=31911466;
RA Zhou Z., Liu Y., Xu W., Pan J., Luo Z.H., Li M.;
RT "Genome- and Community-Level Interaction Insights into Carbon Utilization
RT and Element Cycling Functions of Hydrothermarchaeota in Hydrothermal
RT Sediment.";
RL mSystems 5:e00795-e00719(2020).
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}.
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:KDA54936.1}.
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DR EMBL; DSMR01000486; HET47835.1; -; Genomic_DNA.
DR EMBL; JMFG01000002; KDA54936.1; -; Genomic_DNA.
DR RefSeq; WP_038046310.1; NZ_JMFG01000002.1.
DR AlphaFoldDB; A0A062Y3G5; -.
DR STRING; 1312852.EG19_03800; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000027284; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000027284}.
FT DOMAIN 2..161
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 195 AA; 21600 MW; 76DEE13611C7F837 CRC64;
MSLVGKPAPL FTLEGYHNGE FVSVSLEKLR GKWVYLLFYP LDFTFVCPTE VLAFSRDAHE
FAARNCQIFG VSVDSKYTHK AWVDAPRERG GLGGSLNYPL LADLTKEVSR AYGVLDEQAG
VALRGLFLIN PEGVIVHETT NFLPVGRSSR EALRTLKAFQ YVSQHTNEVC PADWDEGKDT
MVATPEGAAQ YLATH
//
