ID A0A1Q7TKA2_9BACT Unreviewed; 171 AA.
AC A0A1Q7TKA2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 08-NOV-2023, entry version 32.
DE SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:OLD88896.1};
GN ORFNames=AUG81_05475 {ECO:0000313|EMBL:OLD88896.1};
OS Verrucomicrobia bacterium 13_1_20CM_4_54_11.
OC Bacteria; Verrucomicrobiota.
OX NCBI_TaxID=1805408 {ECO:0000313|EMBL:OLD88896.1, ECO:0000313|Proteomes:UP000185599};
RN [1] {ECO:0000313|EMBL:OLD88896.1, ECO:0000313|Proteomes:UP000185599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLD88896.1}.
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DR EMBL; MNIL01000063; OLD88896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7TKA2; -.
DR Proteomes; UP000185599; Unassembled WGS sequence.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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:SF121; ALKYL HYDROPEROXIDE REDUCTASE C; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 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}.
FT DOMAIN 12..162
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 54
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 171 AA; 18857 MW; C80347CF8D874F49 CRC64;
MIPQTNVYRS LLGAGRQAPE FTLQCTPDQT VSLNEFRGRP VVLAFYPADF SPVCGDQMAL
YNEMLNEFQE FEAELVGLSV DGAWCHAAFA KQNKLHFPLL ADFEPKGAVA RSYGVYDEKE
GTCERALFVI DRDGVIRWSY VSPIGVNPGA NGILSALEDL QTKSETTEAA K
//
