ID   GCS2_NATPD              Reviewed;         362 AA.
AC   Q3IQ21;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=NP_3372A;
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC   2260 / Gabara;
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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; CR936257; CAI49777.1; -; Genomic_DNA.
DR   RefSeq; WP_011323397.1; NC_007426.1.
DR   AlphaFoldDB; Q3IQ21; -.
DR   SMR; Q3IQ21; -.
DR   STRING; 348780.NP_3372A; -.
DR   EnsemblBacteria; CAI49777; CAI49777; NP_3372A.
DR   GeneID; 3701754; -.
DR   KEGG; nph:NP_3372A; -.
DR   eggNOG; arCOG02722; Archaea.
DR   HOGENOM; CLU_044848_1_0_2; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 39298at2157; -.
DR   Proteomes; UP000002698; 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..362
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000255819"
SQ   SEQUENCE   362 AA;  40568 MW;  84FFE129509D7FC8 CRC64;
     MDLGSREAFD RTGTLGIEEE FFVVDEYGRP TAGTDELVYE NEPPEPLKDR LDHELFKCVI
     ETQTPTIGSL SAADDALAEV RKALVSHAET HGFGIAAAGL HPAAKWRELD HAEKPRYRAQ
     LDRIQYPQHR NTTAGLHIHV GVDDADKAVW VANELRWYMP VMLALSANSP YWNGFDTGLQ
     SARAKIFEAL PNTGMPTAFE DFESFQSFER TMVETGSIND RGELWYDVRP HSEHGTVEVR
     TPDGQADPDH VLAFVEYTQA LVEDLSARYE DGESGANHRR ELLDENKWRA LRHGHDAELL
     DRSLEESVPL GELVESECQR LGVSGIRDVY EAESGAEKQR RLLESEGMDA LCGSLSVEWD
     SS