Reviewed, UniProtKB/Swiss-Prot P19476 (CR29_ENTHI)

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	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 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 reduction Inferred 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

	Sequence		Length	Mass (Da)
	P19476-1 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: 3FFE70141692FF88	FASTA	233	26,253
	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

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

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	June 1, 1994
Last modified:	January 19, 2010
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)