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Protein

Glutamate--cysteine ligase

Gene

gshA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 (gshA)
  2. Glutathione synthetase (gshB)
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

  • ATP binding Source: UniProtKB-KW
  • glutamate-cysteine ligase activity Source: EcoCyc
  • metal ion binding Source: EcoCyc

GO - Biological processi

  • cellular response to arsenic-containing substance Source: EcoCyc
  • cellular response to mercury ion Source: EcoCyc
  • glutathione biosynthetic process Source: EcoCyc
  • hyperosmotic response Source: EcoCyc

Keywordsi

Molecular functionLigase
Biological processGlutathione biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:GLUTCYSLIG-MONOMER.
MetaCyc:GLUTCYSLIG-MONOMER.
BRENDAi6.3.2.2. 2026.
SABIO-RKiP0A6W9.
UniPathwayiUPA00142; UER00209.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--cysteine ligase (EC:6.3.2.2)
Alternative name(s):
Gamma-ECS
Short name:
GCS
Gamma-glutamylcysteine synthetase
Gene namesi
Name:gshA
Synonyms:gsh-I
Ordered Locus Names:b2688, JW2663
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10418. gshA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Pathology & Biotechi

Chemistry databases

DrugBankiDB04464. N-Formylmethionine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001925241 – 518Glutamate--cysteine ligaseAdd BLAST518

Proteomic databases

PaxDbiP0A6W9.
PRIDEiP0A6W9.

Interactioni

Protein-protein interaction databases

BioGridi4262271. 8 interactors.
DIPiDIP-48212N.
IntActiP0A6W9. 5 interactors.
STRINGi316385.ECDH10B_2856.

Structurei

Secondary structure

1518
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 14Combined sources9
Helixi16 – 19Combined sources4
Beta strandi23 – 33Combined sources11
Beta strandi37 – 39Combined sources3
Helixi46 – 48Combined sources3
Turni51 – 53Combined sources3
Beta strandi55 – 59Combined sources5
Beta strandi65 – 69Combined sources5
Helixi76 – 91Combined sources16
Beta strandi102 – 104Combined sources3
Helixi111 – 113Combined sources3
Helixi123 – 139Combined sources17
Helixi141 – 144Combined sources4
Beta strandi148 – 154Combined sources7
Helixi157 – 164Combined sources8
Helixi169 – 190Combined sources22
Helixi193 – 198Combined sources6
Beta strandi201 – 204Combined sources4
Helixi206 – 208Combined sources3
Beta strandi224 – 227Combined sources4
Helixi234 – 236Combined sources3
Turni238 – 240Combined sources3
Helixi244 – 246Combined sources3
Helixi256 – 267Combined sources12
Helixi272 – 275Combined sources4
Beta strandi279 – 281Combined sources3
Beta strandi290 – 292Combined sources3
Helixi296 – 298Combined sources3
Beta strandi302 – 306Combined sources5
Helixi315 – 322Combined sources8
Beta strandi326 – 333Combined sources8
Helixi344 – 359Combined sources16
Helixi367 – 372Combined sources6
Helixi374 – 383Combined sources10
Helixi402 – 424Combined sources23
Helixi428 – 437Combined sources10
Turni438 – 441Combined sources4
Helixi443 – 445Combined sources3
Helixi447 – 457Combined sources11
Helixi464 – 476Combined sources13
Beta strandi481 – 483Combined sources3
Helixi485 – 505Combined sources21
Helixi510 – 514Combined sources5
Turni515 – 517Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V4GX-ray2.50A/B/C/D1-518[»]
1VA6X-ray2.10A/B1-518[»]
2D32X-ray2.40A/B/C/D1-518[»]
2D33X-ray2.60A/B/C/D1-518[»]
ProteinModelPortaliP0A6W9.
SMRiP0A6W9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6W9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105D9M. Bacteria.
COG2918. LUCA.
HOGENOMiHOG000266224.
InParanoidiP0A6W9.
KOiK01919.
PhylomeDBiP0A6W9.

Family and domain databases

HAMAPiMF_00578. Glu_cys_ligase. 1 hit.
InterProiView protein in InterPro
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR007370. Glu_cys_ligase.
IPR006334. Glut_cys_ligase.
PfamiView protein in Pfam
PF04262. Glu_cys_ligase. 1 hit.
SUPFAMiSSF55931. SSF55931. 1 hit.
TIGRFAMsiTIGR01434. glu_cys_ligase. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6W9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIPDVSQALA WLEKHPQALK GIQRGLERET LRVNADGTLA TTGHPEALGS
60 70 80 90 100
ALTHKWITTD FAEALLEFIT PVDGDIEHML TFMRDLHRYT ARNMGDERMW
110 120 130 140 150
PLSMPCYIAE GQDIELAQYG TSNTGRFKTL YREGLKNRYG ALMQTISGVH
160 170 180 190 200
YNFSLPMAFW QAKCGDISGA DAKEKISAGY FRVIRNYYRF GWVIPYLFGA
210 220 230 240 250
SPAICSSFLQ GKPTSLPFEK TECGMYYLPY ATSLRLSDLG YTNKSQSNLG
260 270 280 290 300
ITFNDLYEYV AGLKQAIKTP SEEYAKIGIE KDGKRLQINS NVLQIENELY
310 320 330 340 350
APIRPKRVTR SGESPSDALL RGGIEYIEVR SLDINPFSPI GVDEQQVRFL
360 370 380 390 400
DLFMVWCALA DAPEMSSSEL ACTRVNWNRV ILEGRKPGLT LGIGCETAQF
410 420 430 440 450
PLPQVGKDLF RDLKRVAQTL DSINGGEAYQ KVCDELVACF DNPDLTFSAR
460 470 480 490 500
ILRSMIDTGI GGTGKAFAEA YRNLLREEPL EILREEDFVA EREASERRQQ
510
EMEAADTEPF AVWLEKHA
Length:518
Mass (Da):58,269
Last modified:March 29, 2005 - v1
Checksum:i4E58C447B4D7FF16
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti100W → L in CAA27583 (PubMed:2872655).Curated1
Sequence conflicti494 – 495AS → GF in CAA27583 (PubMed:2872655).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03954 Genomic DNA. Translation: CAA27583.1.
U00096 Genomic DNA. Translation: AAC75735.1.
AP009048 Genomic DNA. Translation: BAA16555.1.
PIRiA65049. SYECEC.
RefSeqiNP_417173.1. NC_000913.3.
WP_000611804.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75735; AAC75735; b2688.
BAA16555; BAA16555; BAA16555.
GeneIDi944881.
KEGGiecj:JW2663.
eco:b2688.
PATRICifig|1411691.4.peg.4051.

Similar proteinsi

Entry informationi

Entry nameiGSH1_ECOLI
AccessioniPrimary (citable) accession number: P0A6W9
Secondary accession number(s): P06980, P78228
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: March 29, 2005
Last modified: October 25, 2017
This is version 104 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families