ID A0A1G2G913_9BACT Unreviewed; 173 AA.
AC A0A1G2G913;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Thioredoxin peroxidase {ECO:0000313|EMBL:OGZ46368.1};
GN ORFNames=A3J54_04220 {ECO:0000313|EMBL:OGZ46368.1};
OS Candidatus Ryanbacteria bacterium RIFCSPHIGHO2_02_FULL_45_13b.
OC Bacteria; Candidatus Ryanbacteria.
OX NCBI_TaxID=1802117 {ECO:0000313|EMBL:OGZ46368.1, ECO:0000313|Proteomes:UP000176576};
RN [1] {ECO:0000313|EMBL:OGZ46368.1, ECO:0000313|Proteomes:UP000176576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- 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:OGZ46368.1}.
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DR EMBL; MHNN01000010; OGZ46368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2G913; -.
DR STRING; 1802117.A3J54_04220; -.
DR Proteomes; UP000176576; Unassembled WGS sequence.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
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; 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; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000313|EMBL:OGZ46368.1}.
FT DOMAIN 4..157
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 49
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 173 AA; 19722 MW; A469C15D57EEF52B CRC64;
MVMIKIGEQA PDFKLKGYFG GKFKEYALKD YKNKWLVIFF YPLDFTFVCP TEIKEFSAKY
AQFKKLNAEV IGVSVDSEHS HKAWVEGPLG KINFPLLSDF HKRMSEAYDV LLEDKGIALR
GTFILDPYGK VRYVVISDND VGRSVDETLR VVAALQTGKL CPVEWKPGEK TLN
//