ID   GCS2_HALWD              Reviewed;         363 AA.
AC   Q18H65;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS {ECO:0000255|HAMAP-Rule:MF_01609};
GN   Name=gshA {ECO:0000255|HAMAP-Rule:MF_01609}; OrderedLocusNames=HQ_2566A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
CC   -!- FUNCTION: Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC),
CC       the main low-molecular-weight thiol compound instead of glutathione in
CC       halophilic archaea. {ECO:0000255|HAMAP-Rule:MF_01609}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01609};
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC       YbdK subfamily. {ECO:0000255|HAMAP-Rule:MF_01609}.
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DR   EMBL; AM180088; CAJ52678.1; -; Genomic_DNA.
DR   RefSeq; WP_011571796.1; NC_008212.1.
DR   AlphaFoldDB; Q18H65; -.
DR   SMR; Q18H65; -.
DR   STRING; 362976.HQ_2566A; -.
DR   EnsemblBacteria; CAJ52678; CAJ52678; HQ_2566A.
DR   GeneID; 4194020; -.
DR   KEGG; hwa:HQ_2566A; -.
DR   eggNOG; arCOG02722; Archaea.
DR   HOGENOM; CLU_044848_1_0_2; -.
DR   OMA; LIFGLHV; -.
DR   Proteomes; UP000001975; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR   InterPro; IPR006336; GCS2.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR011793; YbdK.
DR   Pfam; PF04107; GCS2; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR02050; gshA_cyan_rel; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..363
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000255818"
SQ   SEQUENCE   363 AA;  40593 MW;  6C3D0D48C4203699 CRC64;
     MDVGSADAFD RMGTLGVEEE FFVVDDSGQP TAGIQELIYD YNHPPAGVLA DRLDHELFQF
     VIETQTPLLE DVSAVSESVQ AVRDALVTHA ADHGYRIAAA GLHPTAKWRE RNHVEKPRYQ
     SQLDRIQYPQ HRNTTAGLHV HVGVDDPDAA TWIANELRWY LPPLLALSAN SPYWNGFDTG
     LASARAKIFE ALPNTGMPTR FEDFEAYYQL EKRMVETGSI KDRGELWYDV RPHTGHGTVE
     VRTPDAQADP SVTVAIVEYI HALVMDFAAR YADGESGTKV RREILDANKW HAMRYGRDAE
     FIIPGSMETV TLSEFVDRET NRLGVDGLTT LLAREGGAKK QRRLHASDNI DTLLESLCLD
     TDT