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Database: UniProt
Entry: A0A0S9C5G3_9MICC
LinkDB: A0A0S9C5G3_9MICC
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ID   A0A0S9C5G3_9MICC        Unreviewed;       164 AA.
AC   A0A0S9C5G3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:KQN88842.1};
GN   ORFNames=ASE96_10375 {ECO:0000313|EMBL:KQN88842.1};
OS   Arthrobacter sp. Leaf69.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN88842.1, ECO:0000313|Proteomes:UP000051467};
RN   [1] {ECO:0000313|EMBL:KQN88842.1, ECO:0000313|Proteomes:UP000051467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf69 {ECO:0000313|EMBL:KQN88842.1,
RC   ECO:0000313|Proteomes:UP000051467};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN88842.1, ECO:0000313|Proteomes:UP000051467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf69 {ECO:0000313|EMBL:KQN88842.1,
RC   ECO:0000313|Proteomes:UP000051467};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQN88842.1}.
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DR   EMBL; LMLR01000011; KQN88842.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S9C5G3; -.
DR   STRING; 1736232.ASE96_10375; -.
DR   OrthoDB; 9812811at2; -.
DR   Proteomes; UP000051467; Unassembled WGS sequence.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd03018; PRX_AhpE_like; 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; PTHR43110; THIOL PEROXIDASE; 1.
DR   PANTHER; PTHR43110:SF1; THIOL 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          13..163
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        55
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   164 AA;  17840 MW;  6122A434C416B678 CRC64;
     MLGGQPVETR AVPALGEAAP DFELLNQFGE PVRLSELRGQ NVVVVFFPFA FSGICTGELC
     EIRDNLTLFE DADAVVLGIS VDSKFAQRAY AEKEGYAFDL LADFWPHGAV AEQYGVFDPA
     TGMAKRGTFI IDAAGIVRYL VVNPRGQARD FTEYRTALAG LGRN
//
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