Q20117

PR
Gene name
gcs-1 (F37B12.2)
Protein name
Glutamate--cysteine ligase
Names
Gamma-ECS, GCS, Gamma-glutamylcysteine synthetase
Species
Caenorhabditis elegans
KEGG Pathway
cel:CELE_F37B12.2
EC number
6.3.2.2: Acid--amino-acid ligases (peptide synthases)
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

45-114 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q20117

Entry ID Method Resolution Chain Position Source
AF-Q20117-F1 Predicted AlphaFoldDB

No variants for Q20117

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q20117

No associated diseases with Q20117

No regional properties for Q20117

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q20117

Functions

Description
EC Number 6.3.2.2 Acid--amino-acid ligases (peptide synthases)
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
glutamate-cysteine ligase complex An enzyme complex that catalyzes the ligation of glutamate to cysteine, forming glutamylcysteine.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
glutamate-cysteine ligase activity Catalysis of the reaction: L-cysteine + L-glutamate + ATP = L-gamma-glutamyl-L-cysteine + ADP + 2 H(+) + phosphate.

5 GO annotations of biological process

Name Definition
glutathione biosynthetic process The chemical reactions and pathways resulting in the formation of glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins.
response to arsenic-containing substance Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an arsenic stimulus from compounds containing arsenic, including arsenates, arsenites, and arsenides.
response to heat Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism.
response to reactive oxygen species Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals.
response to superoxide Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a superoxide stimulus. Superoxide is the anion, oxygen-, formed by addition of one electron to dioxygen (O2) or any compound containing the superoxide anion.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9W3K5 Gclc Glutamate--cysteine ligase Drosophila melanogaster (Fruit fly) PR
P19468 Gclc Glutamate--cysteine ligase catalytic subunit Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MGLLTKGSPL TWAETVPHID YIKKHGIAQF INLYHRLKSR HGDQLKWGDE IEYTIVKFDD
70 80 90 100 110 120
ANKKVRVSCK AEELLNKLQA EEQVNAMLGT ANRFLWRPEF GSYMIEGTPG MPYGGLIACF
130 140 150 160 170 180
NIVEANMKLR RQVVKKLLKK DETCLSISFP SLGVPGFTFP EVAADRKNDD AANSVFWPEQ
190 200 210 220 230 240
AVFLGHPRFK NLTKNIKGRR GSKVAINVPI FKDTNTPSPF VEDLSALGGP DDTRDAKPDH
250 260 270 280 290 300
IYMDHMGFGM GCCCLQVTFQ AVNVDEARWL YDQLTPITPI LLALSAATPI FRGKLSNVDS
310 320 330 340 350 360
RWDIISASVD DRTPEERGLE PLKNSKWVID KSRYDSTDCY IYPCSVGYND IPLQYDETIY
370 380 390 400 410 420
KQLIDGNIDE PLAKHIAHMF IRDPHQVFRE RIEQDDEKSS EHFETIQSSN WMNMRFKPPP
430 440 450 460 470 480
PDAPEIGWRV EFRPTEVQLT DFENAAYCCF VVLLTRMMIS FRLTYLMPIS MVTENMKRAQ
490 500 510 520 530 540
QKDAVLNQKF LFRKGLAECK SAPENLKGSE KCGPPSQDIE EMSIDEIING KKNGFPGLIS
550 560 570 580 590 600
LIRQFLDSAD VDVDTRCTIS QYLNFISKRA TGEINTLAHW TRGFVQSHPA YKHDSDVNDN
610 620 630 640 650
IVYDLLKKMD AISNGEDHCE KLLGCYRSKT DHAISAAVRK AEEHMIVSSQ KRAH