PRX5_SYNY3
ID PRX5_SYNY3 Reviewed; 189 AA.
AC P73728;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Peroxiredoxin sll1621;
DE Short=Prx;
DE EC=1.11.1.27 {ECO:0000250|UniProtKB:P44758};
DE AltName: Full=Glutathione-dependent peroxiredoxin {ECO:0000305};
GN OrderedLocusNames=sll1621;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-10.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
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:0000250|UniProtKB:P44758}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione
CC disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58297; EC=1.11.1.27;
CC Evidence={ECO:0000250|UniProtKB:P44758};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:A9PCL4}.
CC -!- INTERACTION:
CC P73728; P73728: sll1621; NbExp=2; IntAct=EBI-862771, EBI-862771;
CC P73728; P52232: slr0233; NbExp=2; IntAct=EBI-862771, EBI-863606;
CC P73728; P73263: slr1139; NbExp=4; IntAct=EBI-862771, EBI-862065;
CC P73728; P52231: trxA; NbExp=3; IntAct=EBI-862771, EBI-862916;
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this 1-Cys
CC peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC with a cysteine from another protein or with a small thiol molecule.
CC {ECO:0000250|UniProtKB:A9PCL4}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000305}.
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DR EMBL; BA000022; BAA17776.1; -; Genomic_DNA.
DR PIR; S74815; S74815.
DR AlphaFoldDB; P73728; -.
DR SMR; P73728; -.
DR IntAct; P73728; 9.
DR STRING; 1148.1652858; -.
DR PaxDb; P73728; -.
DR EnsemblBacteria; BAA17776; BAA17776; BAA17776.
DR KEGG; syn:sll1621; -.
DR eggNOG; COG0678; Bacteria.
DR InParanoid; P73728; -.
DR OMA; GYINHPK; -.
DR PhylomeDB; P73728; -.
DR BRENDA; 1.11.1.24; 6192.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR CDD; cd03013; PRX5_like; 1.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PTHR10430; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Antioxidant; Direct protein sequencing; Oxidoreductase; Peroxidase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..189
FT /note="Peroxiredoxin sll1621"
FT /id="PRO_0000056615"
FT DOMAIN 2..177
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 55
FT /note="Cysteine sulfenic acid (-SOH) intermediate (for
FT peroxiredoxin activity)"
FT /evidence="ECO:0000250|UniProtKB:P44758"
SQ SEQUENCE 189 AA; 21167 MW; 82F8BB502DD9A6B5 CRC64;
MTPERVPSVV FKTRVRDESV PGPNPYRWED KTTEQIFGGK KVVLFSLPGA FTPTCSSNHL
PRYEQLFEEF QALGVDDIIC LSVNDAFVMF QWGKQIGADK VKLLPDGNGE FTRKMGMLVE
KSNLGFGMRS WRYSMFVNDG KIEKMFIEPE FGDNCPVDPF ECSDADTMLA YLKGAEAPGV
SEPVKAFVG
