Reviewed, UniProtKB/Swiss-Prot P09792 (GST28_SCHMA)

Names and origin

Protein names	Recommended name:     Glutathione S-transferase class-mu 28 kDa isozyme       Short name=GST 28     EC=2.5.1.18 Alternative name(s):     Sm28GST     Sm28 antigen     Protective 28 kDa antigen     Smp28
Organism	Schistosoma mansoni (Blood fluke)
Taxonomic identifier	6183 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Platyhelminthes › Trematoda › Digenea › Strigeidida › Schistosomatoidea › Schistosomatidae › Schistosoma

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Homodimer.
Miscellaneous	There are at least three isoenzymes of GST in S.mansoni.
Sequence similarities	Belongs to the GST superfamily. Mu family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Molecular function	Transferase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	glutathione transferase 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

Initiator methionine

1

1

Removed

Chain

2 – 211

210

Glutathione S-transferase class-mu 28 kDa isozyme

PRO_0000185815

Regions

Domain

4 – 86

83

GST N-terminal

Domain

88 – 211

124

GST C-terminal

Sites

Active site

10

1

By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.4

Secondary structure

1

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211

Helix Strand Turn

Details...

Beta strand

5 – 14

10

Helix

15 – 17

3

Helix

18 – 27

10

Beta strand

32 – 36

5

Turn

38 – 40

3

Helix

41 – 44

4

Helix

45 – 47

3

Beta strand

55 – 59

5

Beta strand

61 – 63

3

Beta strand

65 – 69

5

Helix

71 – 81

11

Helix

89 – 110

22

Turn

111 – 114

4

Helix

119 – 129

11

Helix

131 – 144

14

Beta strand

147 – 152

6

Helix

158 – 173

16

Turn

175 – 180

6

Helix

183 – 195

13

Helix

197 – 205

9

Sequences

	Sequence		Length	Mass (Da)
	P09792-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: F988AAF041D767E3	FASTA	211	23,820
	10 20 30 40 50 60 MAGEHIKVIY FDGRGRAESI RMTLVAAGVD YEDERISFQD WPKIKPTIPG GRLPAVKVTD 70 80 90 100 110 120 DHGHVKWMLE SLAIARYMAK KHHMMGETDE EYYSVEKLIG QAEDVEHEYH KTLMKPQEEK 130 140 150 160 170 180 EKITKEILNG KVPVLLNMIC ESLKGSTGKL AVGDKVTLAD LVLIAVIDHV TDLDKGFLTG 190 200 210 KYPEIHKHRE NLLASSPRLA KYLSNRPATP F

References

[1]	"Molecular cloning of a protective antigen of schistosomes." Balloul J.-M., Sondermeyer P., Dreyer D., Capron M., Grzych J.M., Pierce R.J., Carvallo D., Lecocq J.-P., Capron A. Nature 326:149-153(1987) [PubMed: 2434863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Cloning and characterisation of the gene encoding the 28-kDa glutathione S-transferase of Schistosoma mansoni." McNair A.T., Dissous C., Duvaux-Miret O., Capron A. Gene 124:245-249(1993) [PubMed: 8444348] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Schistosoma mansoni: characterization of sequence variants of the 28-kDa glutathione S-transferase." Pierce R.J., Khalife J., Williams D.L., Kanno R., Trottein F., Lepresle T., Sabatier J., Achstetter T., Capron A. Exp. Parasitol. 79:81-84(1994) [PubMed: 7519566] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Puerto Rican.
[4]	"Analysis of the primary structure and post-translational modifications of the Schistosoma mansoni antigen Smp28 by electrospray mass spectrometry." Bouchon B., Jaquinod M., Klarskov K., Trottein F., Klein M., van Dorsselaer A., Bischoff R., Roitsch C. J. Chromatogr. B 662:279-290(1994) [PubMed: 7719482] [Abstract] Cited for: ACETYLATION AT ALA-2, MASS SPECTROMETRY.
[5]	"Crystallization and preliminary X-ray diffraction studies of a protective cloned 28 kDa glutathione S-transferase from Schistosoma mansoni." Trottein F., Vaney M.C., Bachet B., Pierce R.J., Colloc'h N., Lecocq J.-P., Capron A., Mornon J.-P. J. Mol. Biol. 224:515-518(1992) [PubMed: 1560466] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05148 mRNA. Translation: CAA28796.1.
M98271 Genomic DNA. Translation: AAA29891.1.
S71584 mRNA. Translation: AAC60508.1.

PIR

JU0137.

RefSeq

XP_002576704.1.

UniGene

Sma.6813

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U3I	X-ray	1.89	A	1-211	[»]

ModBase

Search...

Genome annotation databases

GeneID

8342765.

KEGG

smm:Smp_054160.

Organism-specific databases

CTD

8342765.

Enzyme and pathway databases

BRENDA

2.5.1.18. 1460.

Family and domain databases

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GST28_SCHMA

Accession

Primary (citable) accession number: P09792

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	February 9, 2010
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)