ID   GCS2_HALMA              Reviewed;         359 AA.
AC   Q5V3Q5;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=rrnAC0866;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV45847.1; -; Genomic_DNA.
DR   RefSeq; WP_011223286.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V3Q5; -.
DR   SMR; Q5V3Q5; -.
DR   STRING; 272569.rrnAC0866; -.
DR   EnsemblBacteria; AAV45847; AAV45847; rrnAC0866.
DR   GeneID; 40151891; -.
DR   KEGG; hma:rrnAC0866; -.
DR   PATRIC; fig|272569.17.peg.1605; -.
DR   eggNOG; arCOG02722; Archaea.
DR   HOGENOM; CLU_044848_1_0_2; -.
DR   OMA; LIFGLHV; -.
DR   Proteomes; UP000001169; Chromosome I.
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..359
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000218223"
SQ   SEQUENCE   359 AA;  40676 MW;  7AFF31D83F250385 CRC64;
     MDATGSAEHF TRMGTLGIEE EFYVVDEFGR PTSGTDELVY ETEPPAVLDG RLDHELFKCV
     IETQTPRIDD PANAGDHLRS VRDALVDHAE ANGFGIAAAG LHPLAKWREL EHAEKPRYKS
     QLDRIQYPQH RNTTAGLHVH VGVDDADKAV WVANELRWHL PLMLALSANS PYWNGFDTGL
     QSARGKIFEA LPNTGMPTTF DDYDAFETYE QRMLETGSID DRGELWFDVR PHSGHGTVEV
     RAPDGQADPD RVLAFVEYVH ELVVDLAERY EDGESGRRLR REFLDENKWR AIRHGQSAEL
     LSRDLSTTRS VEELVEIESD RLGVDGLWEL YHRESGAERQ RRLRSEEGVM ALADSLRLS