ID A0A1J5FI10_9BACT Unreviewed; 188 AA.
AC A0A1J5FI10;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:OIP60001.1};
GN ORFNames=AUK19_01035 {ECO:0000313|EMBL:OIP60001.1};
OS Candidatus Moranbacteria bacterium CG2_30_45_14.
OC Bacteria; Candidatus Moranbacteria.
OX NCBI_TaxID=1805255 {ECO:0000313|EMBL:OIP60001.1, ECO:0000313|Proteomes:UP000183500};
RN [1] {ECO:0000313|EMBL:OIP60001.1, ECO:0000313|Proteomes:UP000183500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_45_14 {ECO:0000313|EMBL:OIP60001.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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:OIP60001.1}.
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DR EMBL; MNYT01000013; OIP60001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5FI10; -.
DR STRING; 1805255.AUK19_01035; -.
DR Proteomes; UP000183500; 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 1..158
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 45
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 188 AA; 21345 MW; 45B837FD831A060A CRC64;
MIGKTIPNLE FDYYQKENFH KAHFSDYRGK WAIVFFYPAD FTFVCPTELE EMQKNYQKFQ
ELGAEVLSVS TDTKFTHKAW HDHSPAIKQL EYPMIADPSG DIAETFGVLI HEGDDRGLAL
RGTFIIDPDG VLQAYEVHSN NVGRSADELL RKLEAAIFVR EHHGEVCPAS WKKGSKTLKP
GIDLVGKI
//
