P30113 (GST28_SCHBO) Reviewed, UniProtKB/Swiss-Prot

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): Sb28GST
Organism	Schistosoma bovis (Blood fluke)
Taxonomic identifier	6184 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Platyhelminthes › Trematoda › Digenea › Strigeidida › Schistosomatoidea › Schistosomatidae › Schistosoma

Protein attributes

Sequence length	211 AA.
Sequence status	Complete.
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. Ref.2
Sequence similarities	Belongs to the GST superfamily. Mu family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.
Sequence caution	The sequence AAA29892.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Molecular function	Transferase
Technical term	3D-structure
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

Chain

1 – 211

211

Glutathione S-transferase class-mu 28 kDa isozyme

PRO_0000185812

Regions

Domain

4 – 86

83

GST N-terminal

Domain

88 – 211

124

GST C-terminal

Region

41 – 45

5

Glutathione binding

Region

70 – 71

2

Glutathione binding

Sites

Binding site

10

1

Glutathione

Binding site

16

1

Glutathione

Binding site

53

1

Glutathione; via amide nitrogen and carbonyl oxygen

Experimental info

Mutagenesis

10

1

Y → F: Loss of enzyme activity. Ref.2

Mutagenesis

21

1

R → L: Reduces catalytic activity 12-fold. Ref.2

Mutagenesis

21

1

R → Q: Reduces catalytic activity 120-fold. Ref.2

Secondary structure

1

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211

Helix Strand Turn

Details...

Beta strand

5 – 11

7

Turn

13 – 17

5

Helix

18 – 26

9

Beta strand

32 – 35

4

Turn

38 – 40

3

Helix

41 – 44

4

Helix

45 – 47

3

Beta strand

53 – 59

7

Beta strand

65 – 70

6

Helix

71 – 81

11

Helix

89 – 110

22

Turn

111 – 114

4

Helix

117 – 129

13

Helix

131 – 144

14

Beta strand

147 – 155

9

Helix

158 – 173

16

Turn

175 – 180

6

Helix

183 – 195

13

Helix

197 – 202

6

Sequences

	Sequence		Length	Mass (Da)
	P30113 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: 9B9F1358710D3C76	FASTA	211	23,898
	10 20 30 40 50 60 MTGDHIKVIY FNGRGRAESI RMTLVAAGVN YEDERISFQD WPKIKPTIPG GRLPAVKITD 70 80 90 100 110 120 NHGHVKWMVE SLAIARYMAK KHHMMGGTEE EYYNVEKLIG QAEDLEHEYY KTLMKPEEEK 130 140 150 160 170 180 QKIIKEILNG KVPVLLDIIC ESLKASTGKL AVGDKVTLAD LVLIAVIDHV TDLDKEFLTG 190 200 210 KYPEIHKHRE NLLASSPRLA KYLSDRAATP F

References

[1]

"Inter-species variation of schistosome 28-kDa glutathione S-transferases." Trottein F., Goding G., Sellin B., Gorillot I., Samaio M., Lecocq J.-P., Capron A. Mol. Biochem. Parasitol. 54:63-72(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

[2]

"Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography." Baiocco P., Gourlay L.J., Angelucci F., Fontaine J., Herve M., Miele A.E., Trottein F., Brunori M., Bellelli A. J. Mol. Biol. 360:678-689(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT, MUTAGENESIS OF TYR-10 AND ARG-21.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M87799 Genomic DNA. Translation: AAA29892.1. Different initiation.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C80	X-ray	2.30	A/B	1-211	[»]
2C8U	X-ray	2.00	A/B	1-211	[»]
2CA8	X-ray	2.49	A	1-211	[»]
2CAI	X-ray	2.26	A/B	1-211	[»]
2CAQ	X-ray	2.00	A	1-211	[»]
2F8F	X-ray	2.10	A/B	1-211	[»]

ProteinModelPortal

P30113.

SMR

P30113. Positions 4-211.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

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.
[Graphical view]

Pfam

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

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

DrugBank

DB00143. Glutathione.

EvolutionaryTrace

P30113.

Entry information

Entry name

GST28_SCHBO

Accession

Primary (citable) accession number: P30113

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	June 1, 1994
Last modified:	April 3, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)