ID   GCS2_HALVD              Reviewed;         347 AA.
AC   D4GZN2;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 61.
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=HVO_1668;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [2]
RP   FUNCTION.
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=19525351; DOI=10.1128/jb.00297-09;
RA   Malki L., Yanku M., Borovok I., Cohen G., Mevarech M., Aharonowitz Y.;
RT   "Identification and characterization of gshA, a gene encoding the
RT   glutamate-cysteine ligase in the halophilic archaeon Haloferax volcanii.";
RL   J. Bacteriol. 191:5196-5204(2009).
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       ECO:0000269|PubMed:19525351}.
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; CP001956; ADE04411.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4GZN2; -.
DR   SMR; D4GZN2; -.
DR   STRING; 309800.C498_03695; -.
DR   PRIDE; D4GZN2; -.
DR   EnsemblBacteria; ADE04411; ADE04411; HVO_1668.
DR   KEGG; hvo:HVO_1668; -.
DR   eggNOG; arCOG02722; Archaea.
DR   HOGENOM; CLU_044848_1_0_2; -.
DR   OMA; LIFGLHV; -.
DR   BRENDA; 6.3.2.2; 2561.
DR   Proteomes; UP000008243; 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..347
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000428862"
SQ   SEQUENCE   347 AA;  38714 MW;  03BA025CC38B89CC CRC64;
     MGTLGVEEEF YIVDADGRPT SGIDDLVYGP EPPEPLAGRL DHELFQFTIE TQTPLIEDPD
     EAGAAVSTVR EALVDHAAAH GYRIAAAGLH PAAKWRELDH ATKPRYQAQL DRIQYPQHRN
     TTAGLHVHVG VDDADKAVWV ANELRWYLAP LLALSANSPF WNGFDTGLAS ARAKVFENLP
     NTGMPTAFDD FEEFQRFERR MVEYGSIDDR GELWYDVRPH TGHGTVEIRT PDAQTDPERV
     TDFVEYVHAL VLDLADRYEA GESGTSVRRE LLDENKWRAT RYGRDTDFIA PDSEGVVSLV
     SFVETESDRL GVDGLRSLLD AESGTAVQRR IHEESGLDGL CEHLTLD