ID A0A0Q4V5N0_9MICO Unreviewed; 157 AA.
AC A0A0Q4V5N0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:KQO65006.1};
GN ORFNames=ASF23_02320 {ECO:0000313|EMBL:KQO65006.1};
OS Curtobacterium sp. Leaf261.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO65006.1, ECO:0000313|Proteomes:UP000050821};
RN [1] {ECO:0000313|EMBL:KQO65006.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO65006.1,
RC ECO:0000313|Proteomes:UP000050821};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO65006.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO65006.1,
RC ECO:0000313|Proteomes:UP000050821};
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:KQO65006.1}.
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DR EMBL; LMMJ01000001; KQO65006.1; -; Genomic_DNA.
DR RefSeq; WP_055948293.1; NZ_LMMJ01000001.1.
DR AlphaFoldDB; A0A0Q4V5N0; -.
DR STRING; 1736311.ASF23_02320; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000050821; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050821}.
FT DOMAIN 3..154
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 46
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 157 AA; 17398 MW; 190FB5978AC88012 CRC64;
MALEIGSLAP DFDLPNQFGE HVVLSDFRGV RPVALVFFPL AFSSTCTSEL CTLRDNIEMF
ADHRVELIGI SVDSKATLRS FAEVNGYDFT LLADFWPHGA VSKEYGVFLE KKGFANRATF
VIDVDGRIRA SVITEPGLAR DVTEYREALD RIAPAHV
//
