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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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi178 – 1781C → S: Decreased activity. 1 Publication
Mutagenesisi220 – 2201R → K: Reduces activity with cysteine as substrate. 1 Publication
Mutagenesisi341 – 3411C → S: Decreased activity. 1 Publication
Mutagenesisi356 – 3561C → A: Decreased activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5555ChloroplastSequence analysisAdd
BLAST
Chaini56 – 514459Glutamate--cysteine ligase, chloroplasticPRO_0000013055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

1
514
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi83 – 919Combined sources
Helixi97 – 993Combined sources
Beta strandi102 – 11211Combined sources
Turni113 – 1153Combined sources
Helixi121 – 13515Combined sources
Beta strandi138 – 1425Combined sources
Beta strandi145 – 1517Combined sources
Beta strandi154 – 1585Combined sources
Beta strandi164 – 1674Combined sources
Beta strandi171 – 1733Combined sources
Helixi174 – 19522Combined sources
Beta strandi197 – 2004Combined sources
Helixi210 – 2123Combined sources
Helixi219 – 2279Combined sources
Helixi228 – 2303Combined sources
Helixi235 – 2417Combined sources
Beta strandi244 – 2496Combined sources
Helixi254 – 27522Combined sources
Helixi291 – 2955Combined sources
Helixi301 – 3033Combined sources
Helixi308 – 3114Combined sources
Helixi317 – 32610Combined sources
Beta strandi329 – 3346Combined sources
Beta strandi337 – 3448Combined sources
Helixi346 – 3505Combined sources
Helixi364 – 3718Combined sources
Beta strandi377 – 39014Combined sources
Helixi394 – 40815Combined sources
Helixi411 – 42010Combined sources
Turni421 – 4233Combined sources
Helixi426 – 43914Combined sources
Helixi440 – 4423Combined sources
Beta strandi443 – 4453Combined sources
Helixi450 – 46819Combined sources
Helixi473 – 4764Combined sources
Helixi477 – 4859Combined sources
Helixi489 – 49810Combined sources
Turni499 – 5035Combined sources
Helixi508 – 5114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GWCX-ray2.18A/B/C/D/E/F/G/H66-514[»]
2GWDX-ray2.09A66-514[»]
ProteinModelPortaliO23736.
SMRiO23736. Positions 76-514.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391K → R in CAA64808 (Ref. 2) Curated
Sequence conflicti215 – 2151T → I in CAA64808 (Ref. 2) Curated
Sequence conflicti257 – 2571M → T in CAA64808 (Ref. 2) Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2GWCX-ray2.18A/B/C/D/E/F/G/H66-514[»]
2GWDX-ray2.09A66-514[»]
ProteinModelPortaliO23736.
SMRiO23736. Positions 76-514.
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: December 9, 2015
This is version 85 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.