ID   GSH1_SODGM              Reviewed;         520 AA.
AC   Q2NVK9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00578};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00578};
DE   AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00578};
DE            Short=GCS {ECO:0000255|HAMAP-Rule:MF_00578};
DE   AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00578};
GN   Name=gshA {ECO:0000255|HAMAP-Rule:MF_00578}; OrderedLocusNames=SG0541;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
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_00578};
CC   -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC       L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC       Rule:MF_00578}.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family.
CC       Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00578}.
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DR   EMBL; AP008232; BAE73816.1; -; Genomic_DNA.
DR   RefSeq; WP_011410514.1; NZ_LN854557.1.
DR   AlphaFoldDB; Q2NVK9; -.
DR   SMR; Q2NVK9; -.
DR   STRING; 343509.SG0541; -.
DR   EnsemblBacteria; BAE73816; BAE73816; SG0541.
DR   KEGG; sgl:SG0541; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   OrthoDB; 967793at2; -.
DR   BioCyc; SGLO343509:SGP1_RS04790-MON; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000001932; 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:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00578; Glu_cys_ligase; 1.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR007370; Glu_cys_ligase.
DR   InterPro; IPR006334; Glut_cys_ligase.
DR   PANTHER; PTHR38761; PTHR38761; 1.
DR   Pfam; PF04262; Glu_cys_ligase; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding.
FT   CHAIN           1..520
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000025191"
SQ   SEQUENCE   520 AA;  58853 MW;  455D5E3C0D5167D6 CRC64;
     MIPDVSTALS WLEANPQALK GIRRGVEREG LRINANGSLA QTPHPESLGS ALTHKWITTD
     FAEALLEFIT PVDDDIDHML TLLRDIHRYV ARRLGDERLW PMSMPCFIDS AQPIELAQYG
     SSNIGRMKTL YRKGLKNRYS ALMQVIAGVH YNFSLPLAFW QAYAGIRDEA SGKEAISAGY
     LRLIRNYYRF GWIILYLFGA SPGICPSFLN GRKTDLLFEQ APSGLIYLPY ATSLRLSDLG
     YTNKSQSQLN ITFNHLDEYV RGLKQAIKTP SADYQRMGLQ RGGHYLQLNT NVLQIENELY
     APIRPKRVTR DDESPSDALM RGGIEYVEVR SLDINPFSPV GVDEEQARFL DLFLIWCTLA
     EAPEMSAEEL RCTRTNWNRV ILEGRKPGLM LGIDCGSTEQ PLTILGKSLF SDLRRVAETL
     DSNNGDTHYQ LVCDKLVAGF DNPELTLSAR FMDQLIEHGI GGLGLILAND YRQTLRDEPL
     QVLNEAQLDE ERLRSWQRQR SLEVADHLSF DEFLASQNGR