ID   GCS2_HALS3              Reviewed;         360 AA.
AC   B0R5I4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=OE_2998R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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; AM774415; CAP14001.1; -; Genomic_DNA.
DR   RefSeq; WP_010903015.1; NC_010364.1.
DR   AlphaFoldDB; B0R5I4; -.
DR   SMR; B0R5I4; -.
DR   EnsemblBacteria; CAP14001; CAP14001; OE_2998R.
DR   GeneID; 5953901; -.
DR   KEGG; hsl:OE_2998R; -.
DR   HOGENOM; CLU_044848_1_0_2; -.
DR   OMA; LIFGLHV; -.
DR   PhylomeDB; B0R5I4; -.
DR   Proteomes; UP000001321; 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.
FT   CHAIN           1..360
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000148221"
SQ   SEQUENCE   360 AA;  40019 MW;  9958A3A833F8561D CRC64;
     MDVGSPEAFS ESGTLGVEEE FFVVDEHGVP TAGSDELVYE GEPPEPIAGR LDHELFKFVV
     ETQTPTLNGV AEAPAAIREV RAALVAYASE HGLRIAGAGL HPGARWREHE HAEKPRYRSQ
     LDRIQYPQHR NTTAGLHIHV GVDDPDKAVW VSNRMRWHMP VLLALSANSP YWNGFDTGLA
     SARAKIFEGL PNTGLPTAFE SYAAFQAFER RMVEHGGIED RGELWYDVRP HSGHGTVEVR
     APDAQADPAV VDAFVEYAHA LVTEYAQRYD DHPDPFSVTG LRRELLDANK WRAMRDGHDA
     SFVARETQGA VDLGTVVDRE CDRLGVSGIR DVYDDVSGAQ QQRRILDTHG EKRLYNHLSL