Q93113 (GST1D_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase 1, isoform D
EC=2.5.1.18
EC=4.5.1.1

Alternative name(s):
AgGst1-alpha
Aggst1-1
Aggst1-6
Aggst2-1
DDT-dehydrochlorinase
GST class-theta

Gene names

Name:	GstD1
Synonyms:	GST1a
ORF Names:	AGAP004164

Organism

Anopheles gambiae (African malaria mosquito) [Reference proteome]

Taxonomic identifier

7165 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicimorpha › Culicoidea › Culicidae › Anophelinae › Anopheles › Cellia › Pyretophorus › gambiae species complex

Protein attributes

Sequence length	209 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. Has DDT dehydrochlorinase activity. Ref.1 Ref.4
Catalytic activity	RX + glutathione = HX + R-S-glutathione. Ref.4 1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride. Ref.4
Enzyme regulation	Inhibited by S-hexylglutathione. Ref.5
Subunit structure	Homodimer. Ref.5
Developmental stage	Expressed in larvae. Ref.1
Sequence similarities	Belongs to the GST superfamily. Theta family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Molecular function	Lyase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	DDT-dehydrochlorinase activity Inferred from electronic annotation. Source: EC glutathione transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform D (identifier: Q93113-1)

Also known as: 1-1; 1-6; 2-1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform A (identifier: O77462-1)

Also known as: 1-3;

The sequence of this isoform can be found in the external entry O77462.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform B (identifier: O77473-1)

Also known as: 1-4;

The sequence of this isoform can be found in the external entry O77473.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Isoform C (identifier: Q93112-1)

Also known as: 1-5;

The sequence of this isoform can be found in the external entry Q93112.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 209

209

Glutathione S-transferase 1, isoform D

PRO_0000185962

Regions

Domain

1 – 80

80

GST N-terminal

Domain

86 – 207

122

GST C-terminal

Region

50 – 52

3

Glutathione binding

Region

64 – 66

3

Glutathione binding

Sites

Binding site

9

1

Glutathione

Experimental info

Sequence conflict

24

1

V → A in CAA96105. Ref.1

Secondary structure

1

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209

Helix Strand Turn

Details...

Beta strand

2 – 5

4

Helix

10 – 21

12

Beta strand

27 – 30

4

Helix

33 – 35

3

Helix

37 – 39

3

Helix

41 – 46

6

Beta strand

52 – 57

6

Beta strand

60 – 64

5

Helix

65 – 76

12

Helix

87 – 102

16

Helix

104 – 118

15

Helix

124 – 140

17

Turn

141 – 143

3

Beta strand

149 – 151

3

Helix

154 – 169

16

Helix

177 – 189

13

Helix

193 – 207

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform D (1-1) (1-6) (2-1) [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 3B262EEE21FAA9D0	FASTA	209	23,445
	10 20 30 40 50 60 MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TDLMKGEHMK PEFLKLNPQH CIPTLVDNGF 70 80 90 100 110 120 ALWESRAIQI YLAEKYGKDD KLYPKDPQKR AVVNQRLYFD MGTLYQRFAD YHYPQIFAKQ 130 140 150 160 170 180 PANPENEKKM KDAVGFLNTF LEGQEYAAGN DLTIADLSLA ATIATYEVAG FDFAPYPNVA 190 200 AWFARCKANA PGYALNQAGA DEFKAKFLS
	Isoform A (1-3) [UniParc]. See O77462.		–	–
	Isoform B (1-4) [UniParc]. See O77473.		–	–
	Isoform C (1-5) [UniParc]. See Q93112.		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and localization of a glutathione S-transferase class I gene from Anopheles gambiae." Ranson H., Cornel A.J., Fournier D., Vaughan A., Collins F.H., Hemingway J. J. Biol. Chem. 272:5464-5468(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE. Strain: G3 and Zands. Tissue: Larva.
[2]	"The role of alternative mRNA splicing in generating heterogeneity within the Anopheles gambiae class I glutathione S-transferase family." Ranson H., Collins F.H., Hemingway J. Proc. Natl. Acad. Sci. U.S.A. 95:14284-14289(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING. Strain: ZAN/U.
[3]	"The genome sequence of the malaria mosquito Anopheles gambiae." Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L. Science 298:129-149(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST.
[4]	"Cloning and characterization of two glutathione S-transferases from a DDT-resistant strain of Anopheles gambiae." Ranson H., Prapanthadara L., Hemingway J. Biochem. J. 324:97-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY. Strain: Zands.
[5]	"Structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae." Chen L., Hall P.R., Zhou X.E., Ranson H., Hemingway J., Meehan E.J. Acta Crystallogr. D 59:2211-2217(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH S-HEXYLGLUTATHIONE INHIBITOR, ENZYME REGULATION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z71481 mRNA. Translation: CAA96105.1.
Z81292 mRNA. Translation: CAB03593.1.
AF071160 Genomic DNA. Translation: AAC79995.1.
AAAB01008880 Genomic DNA. Translation: EAA44713.3.

RefSeq

XP_313050.3. XM_313050.4.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PN9	X-ray	2.00	A/B	1-209	[»]

ProteinModelPortal

Q93113.

SMR

Q93113. Positions 1-209.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

AGAP004164-RB; AGAP004164-PB; AGAP004164.

GeneID

1273988.

KEGG

aga:AgaP_AGAP004164.

VectorBase

AGAP004163. Anopheles gambiae.

Organism-specific databases

CTD

1273988.

Phylogenomic databases

HOGENOM

HOG000125741.

KO

K00799.

OMA

LEGQEYA.

Gene expression databases

ArrayExpress

Q93113.

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

EvolutionaryTrace

Q93113.

Entry information

Entry name

GST1D_ANOGA

Accession

Primary (citable) accession number: Q93113
Secondary accession number(s): Q7PH24, Q94998

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	April 3, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)