(data stored in SCRATCH zone)

SWISSPROT: C3MHK5_SINFN

ID   C3MHK5_SINFN            Unreviewed;       161 AA.
AC   C3MHK5;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   RecName: Full=Peroxiredoxin {ECO:0000256|RuleBase:RU366011};
DE            EC=1.11.1.15 {ECO:0000256|RuleBase:RU366011};
GN   OrderedLocusNames=NGR_c05370 {ECO:0000313|EMBL:ACP24333.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24333.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24333.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
CC       of hydrogen peroxide and organic hydroperoxides to water and
CC       alcohols, respectively. Plays a role in cell protection against
CC       oxidative stress by detoxifying peroxides.
CC       {ECO:0000256|RuleBase:RU366011}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide
CC         + an alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593,
CC         Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
CC         EC=1.11.1.15; Evidence={ECO:0000256|RuleBase:RU366011};
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC       {ECO:0000256|RuleBase:RU366011}.
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DR   EMBL; CP001389; ACP24333.1; -; Genomic_DNA.
DR   RefSeq; WP_012707118.1; NC_012587.1.
DR   RefSeq; YP_002825086.1; NC_012587.1.
DR   STRING; 394.NGR_c05370; -.
DR   EnsemblBacteria; ACP24333; ACP24333; NGR_c05370.
DR   GeneID; 7791763; -.
DR   KEGG; rhi:NGR_c05370; -.
DR   PATRIC; fig|394.7.peg.3350; -.
DR   eggNOG; ENOG4105EHV; Bacteria.
DR   eggNOG; COG0678; LUCA.
DR   HOGENOM; HOG000255884; -.
DR   OMA; QRYAMVV; -.
DR   OrthoDB; 892697at2; -.
DR   BioCyc; SFRE394:GBYN-536-MONOMER; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
DR   PRODOM; C3MHK5.
DR   SWISS-2DPAGE; C3MHK5.
KW   Antioxidant {ECO:0000256|RuleBase:RU366011};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU366011};
KW   Peroxidase {ECO:0000256|RuleBase:RU366011};
KW   Redox-active center {ECO:0000256|RuleBase:RU366011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN        3    161       Thioredoxin. {ECO:0000259|PROSITE:
FT                                PS51352}.
SQ   SEQUENCE   161 AA;  16915 MW;  68D675D698AB2540 CRC64;
     MTIAVGDKLP NATFKEKTAD GPVEVTTDQL FKGKRVVLFA VPGAFTPTCS LNHLPGYLEN
     RDAILARGVD DIAVVAVNDL HVMGAWATSS GGMGKIHFLS DWNAAFTKAL GLDIDLSAGT
     LGIRSKRYSM LVEDGVVKAL NVEDAPGQAT VSGAAAMLEQ L
//

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