ID A0A0J6BLZ2_9SYNE Unreviewed; 196 AA.
AC A0A0J6BLZ2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=thioredoxin-dependent peroxiredoxin {ECO:0000256|ARBA:ARBA00013017};
DE EC=1.11.1.24 {ECO:0000256|ARBA:ARBA00013017};
GN ORFNames=SYNGFB01_01730 {ECO:0000313|EMBL:KMM17787.1};
OS Synechococcus sp. GFB01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1662190 {ECO:0000313|EMBL:KMM17787.1, ECO:0000313|Proteomes:UP000035901};
RN [1] {ECO:0000313|EMBL:KMM17787.1, ECO:0000313|Proteomes:UP000035901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GFB01 {ECO:0000313|EMBL:KMM17787.1,
RC ECO:0000313|Proteomes:UP000035901};
RA Guimaraes P.I., Leao T.F., de Melo A.G., Ramos R.T., Silva A., Fiore M.F.,
RA Schneider M.P.;
RT "Draft genome of the picocyanobacterium Synechococcus sp. strain GFB01
RT isolated from a freshwater lagoon of the Brazilian Amazon.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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. 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:KMM17787.1}.
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DR EMBL; LFEK01000009; KMM17787.1; -; Genomic_DNA.
DR RefSeq; WP_048016664.1; NZ_LFEK01000009.1.
DR AlphaFoldDB; A0A0J6BLZ2; -.
DR STRING; 1662190.SYNGFB01_01730; -.
DR PATRIC; fig|1662190.3.peg.2914; -.
DR OrthoDB; 9801080at2; -.
DR Proteomes; UP000035901; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
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:SF168; 2-CYS PEROXIREDOXIN BAS1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000035901}.
FT DOMAIN 3..161
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 48
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 196 AA; 21890 MW; 7A5AD6D638A5025E CRC64;
MSRLVGLQAP DFTATAVVDQ EFKTVSLSHY RGKYVVLFFY PLDFTFVCPT EITAFSDRYA
DFTSRNTEVL GVSVDSEFSH LAWVQTDRKN GGLGECRYPL VADLKKDIAR AYNVLDEDAG
VALRGLFIID PDGVIMHSTI NNLPVGRSVD ETLRVLQAFQ YVQSHPDEVC PANWQPGDKT
MNPDPVKSKD FFAAVN
//
