ID A0A0Q7B058_9BURK Unreviewed; 248 AA.
AC A0A0Q7B058;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Glutathione peroxidase {ECO:0000313|EMBL:KQW40657.1};
GN ORFNames=ASC76_04395 {ECO:0000313|EMBL:KQW40657.1};
OS Rhizobacter sp. Root404.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW40657.1, ECO:0000313|Proteomes:UP000051611};
RN [1] {ECO:0000313|EMBL:KQW40657.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW40657.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW40657.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW40657.1,
RC ECO:0000313|Proteomes:UP000051611};
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:KQW40657.1}.
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DR EMBL; LMDS01000001; KQW40657.1; -; Genomic_DNA.
DR RefSeq; WP_056462858.1; NZ_LMDS01000001.1.
DR AlphaFoldDB; A0A0Q7B058; -.
DR STRING; 1736528.ASC76_04395; -.
DR OrthoDB; 9800621at2; -.
DR Proteomes; UP000051611; Unassembled WGS sequence.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF08534; Redoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:KQW40657.1};
KW Peroxidase {ECO:0000313|EMBL:KQW40657.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051611}.
FT DOMAIN 5..169
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 248 AA; 27556 MW; 7DAA4B2D539B19A1 CRC64;
MPEATREGQP VPQVKFRYRQ NNEWKEITSD QLFKGRTVAV FSLPGAFTPT CSSTHLPRFN
ELASTFKDNG VDQVICIAVN DPFVMEEWAK SQESDNVFML PDGNGTFTEQ MGMLVDKSDL
NFGKRSWRYS MLVRDGIVEK MFVEPDEPGD PFKVSDADTL LHYVNGNARE PDQIALLTRE
GCAFCAKAKK DLAEAGITYA EVPLPHHIRT RALGAIAKAK TVPQLFVNGE LIGGSDAVEA
WVKRRAAA
//
