GSH1_ONCVO
ID GSH1_ONCVO Reviewed; 652 AA.
AC Q9NFN6; O44933;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Glutamate--cysteine ligase;
DE EC=6.3.2.2;
DE AltName: Full=Gamma-ECS;
DE Short=GCS;
DE AltName: Full=Gamma-glutamylcysteine synthetase;
GN Name=gcs-1;
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=11163433; DOI=10.1016/s0166-6851(00)00325-x;
RA Luersen K., Mueller S., Hussein A., Liebau E., Walter R.D.;
RT "The gamma-glutamylcysteine synthetase of Onchocerca volvulus.";
RL Mol. Biochem. Parasitol. 111:243-251(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 3 family.
CC {ECO:0000305}.
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DR EMBL; AF042168; AAB96970.1; -; mRNA.
DR EMBL; AJ276620; CAB82447.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9NFN6; -.
DR SMR; Q9NFN6; -.
DR STRING; 6282.Q9NFN6; -.
DR BindingDB; Q9NFN6; -.
DR ChEMBL; CHEMBL2366513; -.
DR PRIDE; Q9NFN6; -.
DR HOGENOM; CLU_010467_0_0_1; -.
DR BRENDA; 6.3.2.2; 4401.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000024404; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR004308; GCS.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11164; PTHR11164; 1.
DR Pfam; PF03074; GCS; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..652
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_0000192567"
FT CONFLICT 24
FT /note="Missing (in Ref. 1; CAB82447)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="T -> S (in Ref. 1; CAB82447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 652 AA; 74212 MW; F8BAFB591E76F03F CRC64;
MGLLTLGTPL PWNETVPYVD YIKEHGIAQF IALYHRLKGR EGDQLKWGDE IEYTIVKFDD
DAKRVRVSLR AEELLHQLQA GEELNALLGN ENCCLWRPEF ASYMIEGTPG APYGGLLACF
NVVESNMISR RAEVTRLLEN GESIMSISFP ALGTPDFTSP PYEPRPDDIN SFGCSLFFPD
EVIYGGHPRF RNLVRNIRQR RGEKVAINVP IYKDINTPSP YQEDFTKAKD GGQAARAAKS
DHIYMDHMGF GMGCCCLQVT FQAVNIDEAR WLYDQLTPIT PVLLALSAAT PVFRSRLADV
DSRWDVISAS VDDRTAEERG LVPLKNNKFV LEKSRYDTTD CYIYPCSESY NDIPLQYDDK
IYKQLIDGGI DDLLAQHIAH MFIRDPLQVF RERIEQDDTK STEHFETVQS SNWMNMRFKP
PPPDSEIGWR VEFRPSEVQL TDFENAAYCC FVVLLTRVMI SFRITLILPI SALTENMKRA
QRRNAVLEQK LLFRKGIATC NSPPCARGAG CTLESDDVVE MTVNEIINGN GNDFPGLIPL
MRQYLDSADV DVDSRCTVSQ YLSFIQKRAS GELQTLAAWM REFISEHPEY KHDSYVGDRI
IYDMLKEMDR ISKGEISCPK LLGDYCTKTD SRIPMAVRRA EEKLIVSTKK QS