Glutathione synthetase, chloroplastic precursor - Arabidopsis thaliana (Mouse-ear cress)

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P46416 (GSHB_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutathione synthetase, chloroplastic
Short name=GSH synthetase
Short name=GSH-S
Short name=Glutathione synthase
EC=6.3.2.3

Gene names

Name:	GSH2
Synonyms:	GSHII
Ordered Locus Names:	At5g27380
ORF Names:	F21A20_90

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	539 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 2/2.
Subunit structure	Homodimer By similarity.
Subcellular location	Plastid › chloroplast.
Sequence similarities	Belongs to the eukaryotic GSH synthase family.
Sequence caution	The sequence AAA64781.1 differs from that shown. Reason: Erroneous initiation. The sequence AAA99146.1 differs from that shown. Reason: Frameshift at positions 40 and 44. The sequence AAL11580.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA58318.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Glutathione biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to jasmonic acid stimulus Inferred from expression pattern PubMed 16262714. Source: TAIR
Cellular_component	chloroplast Inferred from direct assay PubMed 15610346. Source: TAIR cytosol Inferred from direct assay PubMed 15610346 PubMed 21166475. Source: TAIR
Molecular_function	ATP binding Inferred from sequence or structural similarity. Source: UniProtKB glutathione binding Inferred from sequence or structural similarity. Source: UniProtKB glutathione synthase activity Inferred from direct assay PubMed 15302873. Source: TAIR magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 61

Chloroplast Potential

Chain

62 – 539

478

Glutathione synthetase, chloroplastic

PRO_0000013058

Regions

Nucleotide binding

428 – 437

ATP By similarity

Nucleotide binding

464 – 467

ATP By similarity

Region

213 – 216

Substrate binding By similarity

Region

281 – 283

Substrate binding By similarity

Region

335 – 338

Substrate binding By similarity

Region

526 – 527

Substrate binding By similarity

Sites

Metal binding

209

Magnesium By similarity

Metal binding

211

Magnesium By similarity

Metal binding

432

Magnesium By similarity

Binding site

193

Substrate By similarity

Binding site

209

ATP By similarity

Binding site

287

Substrate By similarity

Binding site

374

ATP By similarity

Binding site

439

ATP By similarity

Binding site

490

ATP By similarity

Binding site

515

Substrate By similarity

Binding site

517

ATP By similarity

Binding site

523

ATP; via carbonyl oxygen By similarity

Experimental info

Sequence conflict

N → S in CAB51026. Ref.2

Sequence conflict

N → S in CAB51027. Ref.2

Sequence conflict

S → P in CAB51026. Ref.2

Sequence conflict

S → P in CAB51027. Ref.2

Sequence conflict

30 – 34

SSSLK → ELRQG in CAA90515. Ref.5

Sequence conflict

S → P Ref.2

Sequence conflict

S → P Ref.6

Sequence conflict

V → G in CAA58318. Ref.6

Sequence conflict

101

S → T Ref.2

Sequence conflict

101

S → T Ref.6

Sequence conflict

124

A → G Ref.2

Sequence conflict

124

A → G Ref.6

Sequence conflict

135

N → D Ref.2

Sequence conflict

135

N → D Ref.6

Sequence conflict

151

G → S in CAB51027. Ref.2

Sequence conflict

199

D → G in CAB51027. Ref.2

Sequence conflict

219

G → A in CAA58318. Ref.6

Sequence conflict

438

I → T in CAB51027. Ref.2

Sequence conflict

488

I → M in CAB51027. Ref.2

Sequence conflict

503

E → K Ref.2

Sequence conflict

503

E → K Ref.6

Sequence conflict

539

I → N Ref.2

Sequence conflict

539

I → N Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P46416 [UniParc].

Last modified April 30, 2003. Version 3.
Checksum: 2BFBF9A1D53E4A96
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FASTA

539

60,271

        10         20         30         40         50         60 
MGSGCSSLSY SSSSTCNATV FSISSSPSSS SSLKLNPSSF LFQNPKTLRN QSPLRCGRSF 

        70         80         90        100        110        120 
KMESQKPIFD LEKLDDEFVQ KLVYDALVWS SLHGLVVGDK SYQKSGNVPG VGLMHAPIAL 

       130        140        150        160        170        180 
LPTAFPEAYW KQACNVTPLF NELIDRVSLD GKFLQDSLSR TKKVDVFTSR LLDIHSKMLE 

       190        200        210        220        230        240 
RNKKEDIRLG LHRFDYMLDE ETNSLLQIEM NTISCSFPGL SRLVSQLHQS LLRSYGDQIG 

       250        260        270        280        290        300 
IDSERVPINT STIQFADALA KAWLEYSNPR AVVMVIVQPE ERNMYDQHLL SSILREKHNI 

       310        320        330        340        350        360 
VVIRKTLAEV EKEGSVQEDE TLIVGGQAVA VVYFRSGYTP NDHPSESEWN ARLLIEESSA 

       370        380        390        400        410        420 
VKCPSIAYHL TGSKKIQQEL AKPGVLERFL DNKEDIAKLR KCFAGLWSLD DSEIVKQAIE 

       430        440        450        460        470        480 
KPGLFVMKPQ REGGGNNIYG DDVRENLLRL QKEGEEGNAA YILMQRIFPK VSNMFLVREG 

       490        500        510        520        530 
VYHKHQAISE LGVYGAYLRS KDEVIVNEQS GYLMRTKIAS SDEGGVAAGF GVLDSIYLI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the cDNA and genomic clones for glutathione synthetase from Arabidopsis thaliana and complementation of a gsh2 mutant in fission yeast." Wang C.L., Oliver D.J. Plant Mol. Biol. 31:1093-1104(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: cv. RLD.
[2]	"Isolation of cDNA and genomic clones of glutathione synthetase containing plastidic targeting sequences from Arabidopsis thaliana." Skipsey M., Andrews C.J., Townson J.K., Jepson I., Edwards R. Plant Gene Register PGR99-137 Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. Fransz P.F. Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Characterisation of an Arabidopsis thaliana cDNA encoding glutathione synthetase." Rawlins M.R., Leaver C.J., May M.J. FEBS Lett. 376:81-86(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-539. Strain: cv. C24.
[6]	"Cloning of Arabidopsis thaliana glutathione synthetase (GSH2) by functional complementation of a yeast gsh2 mutant." Ullmann P., Gondet L., Potier S., Bach T.J. Eur. J. Biochem. 236:662-669(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-539. Strain: cv. Landsberg erecta.
[7]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-539. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U22359 mRNA. Translation: AAA64781.1. Different initiation. U53856 Genomic DNA. Translation: AAA99146.1. Frameshift. AJ243812 Genomic DNA. Translation: CAB51026.1. AJ243813 mRNA. Translation: CAB51027.1. AC007123 Genomic DNA. No translation available. CP002688 Genomic DNA. Translation: AED93678.1. Z50153 mRNA. Translation: CAA90515.1. X83411 mRNA. Translation: CAA58318.1. Different initiation. AF424586 mRNA. Translation: AAL11580.1. Different initiation. BT000624 mRNA. Translation: AAN18190.1.
IPI	IPI00545571.
PIR	S62654. S68223. T52565.
RefSeq	NP_568495.2. NM_122620.3.
UniGene	At.21515. At.55036.
3D structure databases
ProteinModelPortal	P46416.
SMR	P46416. Positions 67-538.
ModBase	Search...
Proteomic databases
PaxDb	P46416.
PRIDE	P46416.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G27380.1; AT5G27380.1; AT5G27380.
GeneID	832797.
KEGG	ath:AT5G27380.
Organism-specific databases
TAIR	At5g27380.
Phylogenomic databases
eggNOG	NOG329040.
HOGENOM	HOG000172641.
InParanoid	P46416.
KO	K01920.
OMA	EQSGYLM.
PhylomeDB	P46416.
ProtClustDB	PLN02977.
Enzyme and pathway databases
UniPathway	UPA00142; UER00210.
Gene expression databases
ArrayExpress	P46416.
Genevestigator	P46416.
GermOnline	AT5G27380. Arabidopsis thaliana.
Family and domain databases
Gene3D	1.10.1080.10. 1 hit. 3.30.1490.50. 1 hit. 3.30.1490.80. 1 hit. 3.40.50.1760. 1 hit.
InterPro	IPR004887. Glutathione_synth_subst-bd_euk. IPR014042. Glutathione_synthase_a-hlx_euk. IPR014709. Glutathione_synthase_dom. IPR005615. Glutathione_synthase_euk. IPR014049. Glutathione_synthase_N_euk. IPR016185. PreATP-grasp_dom. [Graphical view]
PANTHER	PTHR11130. PTHR11130. 1 hit.
Pfam	PF03917. GSH_synth_ATP. 1 hit. PF03199. GSH_synthase. 1 hit. [Graphical view]
PIRSF	PIRSF001558. GSHase. 1 hit.
SUPFAM	SSF52440. PreATP-grasp-like. 1 hit.
TIGRFAMs	TIGR01986. glut_syn_euk. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GSHB_ARATH

Accession

Primary (citable) accession number: P46416
Secondary accession number(s): Q8H171, Q9SMW4, Q9SMW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	April 30, 2003
Last modified:	May 1, 2013
This is version 113 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents