Reviewed,
UniProtKB/Swiss-Prot P19476 (CR29_ENTHI)
Last modified
January 19, 2010.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative peroxiredoxin EC=1.11.1.15 Alternative name(s): Thioredoxin peroxidase 29 kDa cysteine-rich surface antigen |
| Organism | Entamoeba histolytica |
| Taxonomic identifier | 5759 [NCBI] |
| Taxonomic lineage | Eukaryota › Amoebozoa › Archamoebae › Entamoebidae › Entamoeba |
Protein attributes
| Sequence length | 233 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Reduces peroxides. May play an important role in eliminating peroxides generated during metabolism By similarity. |
| Catalytic activity | 2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH. |
| Subunit structure | Homodimer; disulfide-linked, upon oxidation. Ref.4 |
| Subcellular location | |
| Post-translational modification | The Cys-87-SH group is the primary site of oxidation by H2O2, and the oxidized Cys-87 (probably Cys-SOH) rapidly reacts with Cys-208-SH of the other subunit to form an intermolecular disulfide. This disulfide might subsequently be reduced by thioredoxin By similarity. |
| Sequence similarities | Belongs to the ahpC/TSA family. Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Domain | Redox-active center |
| Molecular function | Antioxidant Oxidoreductase Peroxidase |
| PTM | Disulfide bond |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | peroxiredoxin activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 233 | 233 | Putative peroxiredoxin | PRO_0000135100 | |||||
Regions | |||||||||
| Domain | 41 – 200 | 160 | Thioredoxin | ||||||
Sites | |||||||||
| Active site | 87 | 1 | Cysteine sulfenic acid (-SOH) intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Disulfide bond | 87 | Interchain (with C-208); in linked form By similarity | |||||||
| Disulfide bond | 208 | Interchain (with C-87); in linked form By similarity | |||||||
Experimental info | |||||||||
| Sequence conflict | 70 | 1 | R → K in AAA29095. Ref.3 | ||||||
| Sequence conflict | 105 | 1 | N → D in AAA29110. Ref.2 | ||||||
Sequences
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References
| [1] | "Analysis of the genomic sequence encoding the 29-kDa cysteine-rich protein of Entamoeba histolytica." Bruchhaus I., Tannich E. Trop. Med. Parasitol. 44:116-118(1993) [PubMed: 8367659] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Molecular and cellular characterization of the 29-kilodalton peripheral membrane protein of Entamoeba histolytica: differentiation between pathogenic and nonpathogenic isolates." Reed S.L., Flores B.M., Batzer M.A., Stein M.A., Stroeher V.L., Carlton J.E., Diedrich D.L., Torian B.E. Infect. Immun. 60:542-549(1992) [PubMed: 1730488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-233. |
| [3] | "cDNA sequence analysis of a 29-kDa cysteine-rich surface antigen of pathogenic Entamoeba histolytica." Torian B.E., Flores B.M., Stroeher V.L., Hagen F.S., Stamm W.E. Proc. Natl. Acad. Sci. U.S.A. 87:6358-6362(1990) [PubMed: 2201027] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-233. Strain: H-302:NIH. |
| [4] | "Structural analysis and demonstration of the 29 kDa antigen of pathogenic Entamoeba histolytica as the major accessible free thiol-containing surface protein." Flores B.M., Batzer M.A., Stein M.A., Petersen C., Diedrich D.L., Torian B.E. Mol. Microbiol. 7:755-763(1993) [PubMed: 7682280] [Abstract] Cited for: SUBUNIT. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X70996 Genomic DNA. Translation: CAA50324.1. M75858 mRNA. Translation: AAA29110.1. Sequence problems. M35635 mRNA. Translation: AAA29095.1. |
| PIR | S67947. |
3D structure databases | |
| SMR | P19476. Positions 40-233. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.11.1.15. 323. |
Family and domain databases | |
| InterPro | IPR000866. Alkyl_hydroperoxide_Rdtase. IPR019479. Peroxiredoxin_C. IPR017936. Thioredoxin-like. IPR012336. Thioredoxin-like_fold. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| Pfam | PF10417. 1-cysPrx_C. 1 hit. PF00578. AhpC-TSA. 1 hit. [Graphical view] |
| PROSITE | PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CR29_ENTHI | ||||||||
| Accession | Primary (citable) accession number: P19476 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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