(data stored in ACNUC7421 zone)

SWISSPROT: C4KL40_SULIK

ID   C4KL40_SULIK            Unreviewed;       215 AA.
AC   C4KL40;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 52.
DE   RecName: Full=Peroxiredoxin {ECO:0000256|HAMAP-Rule:MF_00401};
DE            EC=1.11.1.15 {ECO:0000256|HAMAP-Rule:MF_00401};
GN   OrderedLocusNames=M164_0375 {ECO:0000313|EMBL:ACR41005.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR41005.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR41005.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Protects cells against oxidative stress. Can reduce
CC       hydrogen peroxide and/or alkyl hydroperoxides using dithiothreitol
CC       as an electron donor (in vitro). {ECO:0000256|HAMAP-
CC       Rule:MF_00401}.
CC   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC       {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring
CC       structure. {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00401}.
CC   -!- SIMILARITY: Belongs to the AhpC/TSA family. TDXH subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00401}.
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DR   EMBL; CP001402; ACR41005.1; -; Genomic_DNA.
DR   RefSeq; WP_012710510.1; NC_012726.1.
DR   ProteinModelPortal; C4KL40; -.
DR   EnsemblBacteria; ACR41005; ACR41005; M164_0375.
DR   GeneID; 8760198; -.
DR   KEGG; sid:M164_0375; -.
DR   HOGENOM; HOG000022346; -.
DR   KO; K03386; -.
DR   OMA; CPANWEE; -.
DR   OrthoDB; POG093Z0BGG; -.
DR   BioCyc; SISL426118:GI01-377-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   HAMAP; MF_00401; Peroxiredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR022915; Peroxiredoxin_TDXH.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KL40.
DR   SWISS-2DPAGE; C4KL40.
KW   Antioxidant {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00401};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00401}.
FT   DOMAIN        7    162       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
FT   ACT_SITE     49     49       Cysteine sulfenic acid (-SOH)
FT                                intermediate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00401}.
FT   BINDING     125    125       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00401}.
SQ   SEQUENCE   215 AA;  24645 MW;  D772DF75629045B5 CRC64;
     MSEGRIPLIG EKFPEMEVIT THGKIKLPDD YKGRWFVLFS HPGDFTPVCT TEFYSFSKKY
     EEFKKLNTEL IGLSVDSNIS HIEWVMWIEK NLKVEVPFPI IADPMGNVAK RLGMIHAESS
     TATVRAVFII DDKGTVRLIL YYPMEIGRNI DEILRAIRAL QLVDKAGVVT PANWPNNELI
     GDKVINPAPR TIKDAKMRLG QPFDWWFTYK EVKTT
//

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