ID A0A1G2F2J2_9BACT Unreviewed; 187 AA.
AC A0A1G2F2J2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:OGZ32239.1};
GN ORFNames=A3H02_00860 {ECO:0000313|EMBL:OGZ32239.1};
OS Candidatus Niyogibacteria bacterium RIFCSPLOWO2_12_FULL_41_13.
OC Bacteria; Candidatus Niyogibacteria.
OX NCBI_TaxID=1801726 {ECO:0000313|EMBL:OGZ32239.1, ECO:0000313|Proteomes:UP000176787};
RN [1] {ECO:0000313|EMBL:OGZ32239.1, ECO:0000313|Proteomes:UP000176787}
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 -!- 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:OGZ32239.1}.
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DR EMBL; MHMS01000011; OGZ32239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2F2J2; -.
DR STRING; 1801726.A3H02_00860; -.
DR Proteomes; UP000176787; Unassembled WGS sequence.
DR GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
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: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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
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; 21171 MW; 10F524CFCAF56B76 CRC64;
MIKIGQKIQD FELEAYHNDE IKKIKLSQYK GKWLVLIFYP ADFTFVCPTE LEEAAQYYNE
FKKAGAEILS VSADTVFVHK AWHDVSPAIK KVKYPMLADP TGKLCQEFGT YIEEEGLSLR
GSFIIDPDGI LRAFEMNDNS IGRSAEELLR KLQAAKFVRE HKGQVCPASW TPGKKTLKPG
LKLVGKI
//
