Skip Header

Contribute Send feedback
Read comments (?) or add your own

P19476 (CR29_ENTHI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative peroxiredoxin

EC=1.11.1.15
Alternative name(s):
29 kDa cysteine-rich surface antigen
Thioredoxin peroxidase
OrganismEntamoeba histolytica
Taxonomic identifier5759 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaArchamoebaeEntamoebidaeEntamoeba

Protein attributes

Sequence length233 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Membrane; Peripheral membrane protein.

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 componentMembrane
   DomainRedox-active center
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMDisulfide bond
Gene Ontology (GO)
   Cellular componentmembrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionperoxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

peroxiredoxin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 233233Putative peroxiredoxin
PRO_0000135100

Regions

Domain41 – 200160Thioredoxin

Sites

Active site871Cysteine sulfenic acid (-SOH) intermediate By similarity

Amino acid modifications

Disulfide bond87Interchain (with C-208); in linked form By similarity
Disulfide bond208Interchain (with C-87); in linked form By similarity

Experimental info

Sequence conflict701R → K in AAA29095. Ref.3
Sequence conflict1051N → D in AAA29110. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P19476 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 3FFE70141692FF88

FASTA23326,253
        10         20         30         40         50         60 
MSCNQQKECC KKECQEKECC KECCCPRIKA FKKFINTFEK AQIGKEAPEF KAPAYCPCGS 

        70         80         90        100        110        120 
IKEIDINEYR GKYVVLLFYP LDWTFVCPTE MIGYSELAGQ LKEINCEVIG VSVDSVYCHQ 

       130        140        150        160        170        180 
AWCEADKSKG GVGKLTFPLV SDIKRCISIK YGMLNVEAGI ARRGYVIIDD KGKVRYIQMN 

       190        200        210        220        230 
DDGIGRSTEE TIRIVKAIQF SDEHGAVCPL NWKPGKDTIE PTPDGIKKYL TAH 

« Hide

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.
+Additional computationally mapped references.

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.
PIRS67947.

3D structure databases

ProteinModelPortalP19476.
SMRP19476. Positions 40-233.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
Gene3DG3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCR29_ENTHI
AccessionPrimary (citable) accession number: P19476
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: June 1, 1994
Last modified: October 19, 2011
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families