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Protein

Glutamate--cysteine ligase, chloroplastic

Gene

GSH1

Organism
Brassica juncea (Indian mustard) (Sinapis juncea)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Participates in the detoxification process.2 Publications

Catalytic activityi

ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine.

Pathwayi: glutathione biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes glutathione from L-cysteine and L-glutamate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamate--cysteine ligase, chloroplastic (GSH1)
  2. Glutathione synthetase, chloroplastic (GSH2)
This subpathway is part of the pathway glutathione biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutathione from L-cysteine and L-glutamate, the pathway glutathione biosynthesis and in Sulfur metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Glutathione biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.2.2. 941.
UniPathwayiUPA00142; UER00209.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--cysteine ligase, chloroplastic (EC:6.3.2.2)
Alternative name(s):
Gamma-ECS
Short name:
GCS
Gamma-glutamylcysteine synthetase
Gene namesi
Name:GSH1
Synonyms:ECS1
OrganismiBrassica juncea (Indian mustard) (Sinapis juncea)
Taxonomic identifieri3707 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi178C → S: Decreased activity. 1 Publication1
Mutagenesisi220R → K: Reduces activity with cysteine as substrate. 1 Publication1
Mutagenesisi341C → S: Decreased activity. 1 Publication1
Mutagenesisi356C → A: Decreased activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 55ChloroplastSequence analysisAdd BLAST55
ChainiPRO_000001305556 – 514Glutamate--cysteine ligase, chloroplasticAdd BLAST459

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi178 ↔ 3981 Publication
Disulfide bondi341 ↔ 3561 Publication

Post-translational modificationi

The Cys-178-Cys-398 disulfide bridge is known to modulate the enzyme activity according to the redox status. The oxidized form constitutes the active enzyme.

Keywords - PTMi

Disulfide bond

Expressioni

Inductioni

Up-regulated by cadmium and cu2+.2 Publications

Interactioni

Subunit structurei

Homodimer or monomer when oxidized or reduced, respectively.1 Publication

Structurei

Secondary structure

1514
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi83 – 91Combined sources9
Helixi97 – 99Combined sources3
Beta strandi102 – 112Combined sources11
Turni113 – 115Combined sources3
Helixi121 – 135Combined sources15
Beta strandi138 – 142Combined sources5
Beta strandi145 – 151Combined sources7
Beta strandi154 – 158Combined sources5
Beta strandi164 – 167Combined sources4
Beta strandi171 – 173Combined sources3
Helixi174 – 195Combined sources22
Beta strandi197 – 200Combined sources4
Helixi210 – 212Combined sources3
Helixi219 – 227Combined sources9
Helixi228 – 230Combined sources3
Helixi235 – 241Combined sources7
Beta strandi244 – 249Combined sources6
Helixi254 – 275Combined sources22
Helixi291 – 295Combined sources5
Helixi301 – 303Combined sources3
Helixi308 – 311Combined sources4
Helixi317 – 326Combined sources10
Beta strandi329 – 334Combined sources6
Beta strandi337 – 344Combined sources8
Helixi346 – 350Combined sources5
Helixi364 – 371Combined sources8
Beta strandi377 – 390Combined sources14
Helixi394 – 408Combined sources15
Helixi411 – 420Combined sources10
Turni421 – 423Combined sources3
Helixi426 – 439Combined sources14
Helixi440 – 442Combined sources3
Beta strandi443 – 445Combined sources3
Helixi450 – 468Combined sources19
Helixi473 – 476Combined sources4
Helixi477 – 485Combined sources9
Helixi489 – 498Combined sources10
Turni499 – 503Combined sources5
Helixi508 – 511Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GWCX-ray2.18A/B/C/D/E/F/G/H66-514[»]
2GWDX-ray2.09A66-514[»]
ProteinModelPortaliO23736.
SMRiO23736.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO23736.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Family and domain databases

InterProiIPR006336. GCS2.
IPR011556. Glut_cys_lig_pln.
[Graphical view]
PfamiPF04107. GCS2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01436. glu_cys_lig_pln. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O23736-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLSQAGGA YTVPSGHVSS RTGTKTVSGC VNVLRMKETY VSSYSRTLST
60 70 80 90 100
KSMLKRSKRG HQLIVAASPP TEEAVVATEP LTREDLIAYL ASGCKSKEKW
110 120 130 140 150
RIGTEHEKFG FEVNTLRPMK YDQIAELLNS IAERFEWEKV MEGDKIIGLK
160 170 180 190 200
QGKQSISLEP GGQFELSGAP LETLHQTCAE VNSHLYQVKA VAEEMGIGFL
210 220 230 240 250
GMGFQPKWRR EDIPTMPKGR YDIMRNYMPK VGSLGLDMML RTCTVQVNLD
260 270 280 290 300
FSSEADMIRK FRAGLALQPI ATALFANSPF TEGKPNGFLS MRSHIWTDTD
310 320 330 340 350
KDRTGMLPFV FDDSFGFEQY VDYALDVPMY FAYRNGKYVD CTGMTFRQFL
360 370 380 390 400
AGKLPCLPGE LPTYNDWENH LTTIFPEVRL KRYMEMRGAD GGPWRRLCAL
410 420 430 440 450
PAFWVGLLYD EDVLQSVLDL TADWTPAERE MLRNKVPVTG LKTPFRDGLL
460 470 480 490 500
KHVAEDVLKL AKDGLERRGY KEVGFLNAVT EVVRTGVTPA ENLLEMYNGE
510
WGQSVDPVFQ ELLY
Length:514
Mass (Da):57,903
Last modified:January 1, 1998 - v1
Checksum:i07C71CB13E785FA8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti139K → R in CAA64808 (Ref. 2) Curated1
Sequence conflicti215T → I in CAA64808 (Ref. 2) Curated1
Sequence conflicti257M → T in CAA64808 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10848 mRNA. Translation: CAA71801.1.
AJ563921 mRNA. Translation: CAD91712.1.
X95563 mRNA. Translation: CAA64808.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10848 mRNA. Translation: CAA71801.1.
AJ563921 mRNA. Translation: CAD91712.1.
X95563 mRNA. Translation: CAA64808.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GWCX-ray2.18A/B/C/D/E/F/G/H66-514[»]
2GWDX-ray2.09A66-514[»]
ProteinModelPortaliO23736.
SMRiO23736.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00142; UER00209.
BRENDAi6.3.2.2. 941.

Miscellaneous databases

EvolutionaryTraceiO23736.

Family and domain databases

InterProiIPR006336. GCS2.
IPR011556. Glut_cys_lig_pln.
[Graphical view]
PfamiPF04107. GCS2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01436. glu_cys_lig_pln. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiGSH1_BRAJU
AccessioniPrimary (citable) accession number: O23736
Secondary accession number(s): Q43389, Q546C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.