ID A0A0Q4NF85_9GAMM Unreviewed; 181 AA.
AC A0A0Q4NF85;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Thioredoxin/glutathione peroxidase BtuE {ECO:0000256|HAMAP-Rule:MF_02061};
DE EC=1.11.1.24 {ECO:0000256|HAMAP-Rule:MF_02061};
DE EC=1.11.1.9 {ECO:0000256|HAMAP-Rule:MF_02061};
GN Name=btuE {ECO:0000256|HAMAP-Rule:MF_02061,
GN ECO:0000313|EMBL:KQN61882.1};
GN ORFNames=ASF13_22105 {ECO:0000313|EMBL:KQN61882.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN61882.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN61882.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN61882.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN61882.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN61882.1,
RC ECO:0000313|Proteomes:UP000050856};
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 -!- FUNCTION: Non-specific peroxidase that can use thioredoxin or
CC glutathione as a reducing agent. {ECO:0000256|HAMAP-Rule:MF_02061}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_02061};
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. BtuE
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_02061}.
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:KQN61882.1}.
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DR EMBL; LMLK01000007; KQN61882.1; -; Genomic_DNA.
DR RefSeq; WP_056234655.1; NZ_LMLK01000007.1.
DR AlphaFoldDB; A0A0Q4NF85; -.
DR STRING; 1736225.ASF13_22105; -.
DR Proteomes; UP000050856; Unassembled WGS sequence.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR HAMAP; MF_02061; Thiored_glutath_peroxid; 1.
DR InterPro; IPR033674; BtuE.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF40; THIOREDOXIN_GLUTATHIONE PEROXIDASE BTUE; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02061};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|HAMAP-
KW Rule:MF_02061}; Reference proteome {ECO:0000313|Proteomes:UP000050856}.
FT ACT_SITE 35
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02061,
FT ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 181 AA; 19827 MW; 2964AD9DD7E2F9D0 CRC64;
MTIYDTQLTT LDGEATTLAQ WQGEVLLVVN VASKCGLTPQ YEQLEALHKA WHAQGFSVLG
FPCNAFLGQE PGSDEEIKTF CSTTYGVTFP MFSKIEVNGE QRHPLYAQLV AAQQQALAPE
GSGFLERMTS KGRAPEAPGD ILWNFEKFLI GRDGKVLARF SPDMTPDDAQ IVTAVQQALA
E
//
