ID   GCS2_HALSA              Reviewed;         360 AA.
AC   Q9HPZ9;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=VNG_1397C;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004437; AAG19718.1; -; Genomic_DNA.
DR   PIR; B84294; B84294.
DR   RefSeq; WP_010903015.1; NC_002607.1.
DR   AlphaFoldDB; Q9HPZ9; -.
DR   SMR; Q9HPZ9; -.
DR   STRING; 64091.VNG_1397C; -.
DR   PaxDb; Q9HPZ9; -.
DR   EnsemblBacteria; AAG19718; AAG19718; VNG_1397C.
DR   GeneID; 5953901; -.
DR   KEGG; hal:VNG_1397C; -.
DR   PATRIC; fig|64091.14.peg.1067; -.
DR   HOGENOM; CLU_044848_1_0_2; -.
DR   InParanoid; Q9HPZ9; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 39298at2157; -.
DR   PhylomeDB; Q9HPZ9; -.
DR   Proteomes; UP000000554; 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:0016879; F:ligase activity, forming carbon-nitrogen bonds; IBA:GO_Central.
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..360
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000218224"
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