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Database: UniProt
Entry: A0A0P4R489_9ACTN
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ID   A0A0P4R489_9ACTN        Unreviewed;       220 AA.
AC   A0A0P4R489;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE            EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
DE   AltName: Full=Thioredoxin peroxidase {ECO:0000256|ARBA:ARBA00032824};
GN   ORFNames=TPA0598_02_02760 {ECO:0000313|EMBL:GAO07038.1};
OS   Streptomyces lydicamycinicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1546107 {ECO:0000313|EMBL:GAO07038.1, ECO:0000313|Proteomes:UP000048965};
RN   [1] {ECO:0000313|Proteomes:UP000048965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110027 {ECO:0000313|Proteomes:UP000048965};
RA   Komaki H., Ichikawa N., Katano-Makiyama Y., Hosoyama A., Hashimoto M.,
RA   Uohara A., Kitahashi Y., Ohji S., Kimura A., Yamazoe A., Igarashi Y.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Streptomyces sp. NBRC 110027.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAO07038.1, ECO:0000313|Proteomes:UP000048965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110027 {ECO:0000313|EMBL:GAO07038.1,
RC   ECO:0000313|Proteomes:UP000048965};
RX   PubMed=26380643; DOI=10.1186/s40793-015-0046-5;
RA   Komaki H., Ichikawa N., Hosoyama A., Fujita N., Igarashi Y.;
RT   "Draft genome sequence of marine-derived Streptomyces sp. TP-A0598, a
RT   producer of anti-MRSA antibiotic lydicamycins.";
RL   Stand. Genomic Sci. 10:58-58(2015).
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 and as sensor of hydrogen peroxide-mediated
CC       signaling events. {ECO:0000256|ARBA:ARBA00003330}.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000280};
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. BCP/PrxQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00038489}.
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:GAO07038.1}.
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DR   EMBL; BBNO01000002; GAO07038.1; -; Genomic_DNA.
DR   RefSeq; WP_042150668.1; NZ_BBNO01000002.1.
DR   AlphaFoldDB; A0A0P4R489; -.
DR   OrthoDB; 9809746at2; -.
DR   Proteomes; UP000048965; Unassembled WGS sequence.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02970; PRX_like2; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42801:SF7; SLL1159 PROTEIN; 1.
DR   PANTHER; PTHR42801; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000048965}.
FT   DOMAIN          45..218
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   220 AA;  23842 MW;  BFE528617F7772F2 CRC64;
     MSYADGLTAF LREHYPHIQI PDAERAVMDR AGRELAASGL AERALRTGDT APGFSLPTST
     GRTVTLDGLL SAGPVVLTFY RGAWCPFCNF ALRLLQQHHA DITARGAQLV AISPQIPDES
     LTLAEKHALA FDVLSDLGCD TAKQFGLSFD LPDDLAVVYE SFGFDLQRVN GGHPRTLPVP
     ATYVIDQDGT IRWSFVDTDY TARAEPSDIL AALDARPTAH
//
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