Glutathione S-transferase class-mu 26 kDa isozyme

Functionⁱ

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.

Miscellaneous

There are at least two isoenzymes of GST in S.japonicum.

Catalytic activityⁱ

RX + glutathione = HX + R-S-glutathione.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	111	SubstrateCurated		1

GO - Molecular functionⁱ

glutathione transferase activity Source: UniProtKB-EC

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase

Molecular function

Transferase

Enzyme and pathway databases

BRENDAⁱ	2.5.1.18 5607

BRENDAⁱ

2.5.1.18 5607

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Glutathione S-transferase class-mu 26 kDa isozyme (EC:2.5.1.18) Short name: GST 26 Alternative name(s): Sj26 antigen SjGST
Organismⁱ	Schistosoma japonicum (Blood fluke)
Taxonomic identifierⁱ	6182 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Platyhelminthes › Trematoda › Digenea › Strigeidida › Schistosomatoidea › Schistosomatidae › Schistosoma

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000185805	2 – 218	Glutathione S-transferase class-mu 26 kDa isozymeAdd BLAST		217

Proteomic databases

PRIDEⁱ	P08515

PRIDEⁱ

P08515

Interactionⁱ

Subunit structureⁱ

Homodimer.1 Publication

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	4 – 6	Combined sources	3
Beta strandⁱ	9 – 11	Combined sources	3
Helixⁱ	12 – 14	Combined sources	3
Helixⁱ	15 – 21	Combined sources	7
Beta strandⁱ	29 – 31	Combined sources	3
Helixⁱ	35 – 37	Combined sources	3
Helixⁱ	38 – 42	Combined sources	5
Turnⁱ	43 – 46	Combined sources	4
Beta strandⁱ	55 – 59	Combined sources	5
Beta strandⁱ	64 – 67	Combined sources	4
Helixⁱ	68 – 72	Combined sources	5
Helixⁱ	77 – 79	Combined sources	3
Helixⁱ	86 – 107	Combined sources	22
Turnⁱ	108 – 111	Combined sources	4
Helixⁱ	115 – 136	Combined sources	22
Turnⁱ	137 – 139	Combined sources	3
Beta strandⁱ	145 – 147	Combined sources	3
Helixⁱ	150 – 162	Combined sources	13
Turnⁱ	163 – 165	Combined sources	3
Turnⁱ	167 – 172	Combined sources	6
Helixⁱ	174 – 184	Combined sources	11
Helixⁱ	187 – 193	Combined sources	7
Beta strandⁱ	195 – 197	Combined sources	3
Beta strandⁱ	203 – 207	Combined sources	5
Beta strandⁱ	209 – 211	Combined sources	3
Beta strandⁱ	213 – 215	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P08515
SMRⁱ	P08515
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P08515

EvolutionaryTraceⁱ

P08515

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	2 – 83	GST N-terminalAdd BLAST		82
Domainⁱ	85 – 203	GST C-terminalAdd BLAST		119

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	7 – 8	Glutathione binding1 Publication1 Publication	2
Regionⁱ	41 – 45	Glutathione binding1 Publication1 Publication	5
Regionⁱ	54 – 55	Glutathione binding1 Publication1 Publication	2
Regionⁱ	67 – 68	Glutathione binding1 Publication1 Publication	2

Sequence similaritiesⁱ

Belongs to the GST superfamily. Mu family.Curated

Family and domain databases

InterProⁱ	View protein in InterPro IPR010987 Glutathione-S-Trfase_C-like IPR036282 Glutathione-S-Trfase_C_sf IPR004045 Glutathione_S-Trfase_N IPR004046 GST_C IPR036249 Thioredoxin-like_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF14497 GST_C_3, 1 hit PF02798 GST_N, 1 hit
SUPFAMⁱ	SSF47616 SSF47616, 1 hit SSF52833 SSF52833, 1 hit
PROSITEⁱ	View protein in PROSITE PS50405 GST_CTER, 1 hit PS50404 GST_NTER, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P08515-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL 
        60         70         80         90        100
EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL 
       110        120        130        140        150
DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH 
       160        170        180        190        200
PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA 
       210 
WPLQGWQATF GGGDHPPK

Length:218

Mass (Da):25,499

Last modified:January 23, 2007 - v3

Checksum:ⁱ5E2AC418BD0EF13F

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M14654 mRNA Translation: AAB59203.1
PIRⁱ	A61514

Protein	Similar proteins		Species	Score	Length	Source
P08515	Clone ZZD245 mRNA sequence		SCHJA		218	UniRef100_P08515
Chain A, The 2.4 Angstrom Structure Of The Fasciola Hepatica Mu Class Gst (Fragment)		methanotrophic bacterial endosymbiont of Bathymodiolus sp.		210
UPI00001108C8		RAT		254

Protein	Similar proteins		Species	Score	Length	Source
P08515	Clone ZZD245 mRNA sequence		SCHJA		218	UniRef90_P08515
Chain A, The 2.4 Angstrom Structure Of The Fasciola Hepatica Mu Class Gst (Fragment)		methanotrophic bacterial endosymbiont of Bathymodiolus sp.		210
UPI00001108C8		RAT		254
Glutathione S-transferase M1		SCHJA		218
UPI00004CF2F0		SCHJA		218
+2

Protein	Similar proteins		Species	Score	Length	Source
P08515	Clone ZZD245 mRNA sequence		SCHJA		218	UniRef50_P08515
Chain A, The 2.4 Angstrom Structure Of The Fasciola Hepatica Mu Class Gst (Fragment)		methanotrophic bacterial endosymbiont of Bathymodiolus sp.		210
Glutathione S-transferase, N-terminal domain		CHLTH		239
Glutathione S-transferase domain A (Fragment)		bacterium AMS-A3		58
UPI00001108C8		RAT		254
+12

Entry informationⁱ

Entry nameⁱ	GST26_SCHJA
Accessionⁱ	P08515Primary (citable) accession number: P08515
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
	Last sequence update:	January 23, 2007
	Last modified:	October 25, 2017
	This is version 121 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing

UniProtKB - P08515 (GST26_SCHJA)

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Functionⁱ

Miscellaneous

Catalytic activityⁱ

Sites

GO - Molecular functionⁱ

Keywordsⁱ

Enzyme and pathway databases

Names & Taxonomyⁱ

PTM / Processingⁱ

Molecule processing

Proteomic databases

Interactionⁱ

Subunit structureⁱ

Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

Family & Domainsⁱ

Domains and Repeats

Region

Sequence similaritiesⁱ

Family and domain databases

Sequenceⁱ

Sequence databases

Similar proteinsⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ

UniProt is an ELIXIR core data resource

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P08515 (GST26_SCHJA)

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Glutathione S-transferase class-mu 26 kDa isozyme

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Sequence databases

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Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ