ID W2UQS7_9FLAO Unreviewed; 212 AA.
AC W2UQS7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:ETN95826.1};
DE EC=1.11.1.15 {ECO:0000313|EMBL:ETN95826.1};
GN ORFNames=P278_15480 {ECO:0000313|EMBL:ETN95826.1};
OS Zhouia amylolytica AD3.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zhouia.
OX NCBI_TaxID=1286632 {ECO:0000313|EMBL:ETN95826.1, ECO:0000313|Proteomes:UP000018850};
RN [1] {ECO:0000313|Proteomes:UP000018850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD3 {ECO:0000313|Proteomes:UP000018850};
RA Jin H., Jeon C.O.;
RT "Draft genome sequence from a member of Zhouia, isolated tidal flat.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ETN95826.1, ECO:0000313|Proteomes:UP000018850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD3 {ECO:0000313|EMBL:ETN95826.1,
RC ECO:0000313|Proteomes:UP000018850};
RX PubMed=27151796;
RA Jia B., Jin H.M., Lee H.J., Jeon C.O.;
RT "Draft Genome Sequence of Zhouia amylolytica AD3, Isolated from Tidal Flat
RT Sediment.";
RL Genome Announc. 4:0-0(2016).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. {ECO:0000256|ARBA:ARBA00037420}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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:ETN95826.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYXY01000019; ETN95826.1; -; Genomic_DNA.
DR RefSeq; WP_038264500.1; NZ_AYXY01000019.1.
DR AlphaFoldDB; W2UQS7; -.
DR STRING; 376730.SAMN04487906_0802; -.
DR PATRIC; fig|1286632.3.peg.1536; -.
DR eggNOG; COG0450; Bacteria.
DR Proteomes; UP000018850; Unassembled WGS sequence.
DR GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:RHEA.
DR CDD; cd03015; PRX_Typ2cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR PANTHER; PTHR10681:SF128; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL; 1.
DR Pfam; PF10417; 1-cysPrx_C; 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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ETN95826.1}; Peroxidase {ECO:0000313|EMBL:ETN95826.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018850}.
FT DOMAIN 2..179
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 212 AA; 24007 MW; 2EE70C82F7F7AA8C CRC64;
MAFVGKKFPN IAVNAMNEMG DTFKLNVLEE AKKNNKKVLL FWYPKDFTFV CPTELHAFQE
ALSEFEKRDT IVIGASCDTA EVHFAWLNTE KDNGGIEGVT YPLLADSNRN LANVLGILDL
TNETFDEETN TYLYEGDNVT YRATYLIDEE GTVFHESINH MPLGRNVNEY LRLIDAYTHV
QKNGEVCPAN WEEGKTAMTA DRKGVADYLS LN
//
