ID   GSH1_PHOPR              Reviewed;         524 AA.
AC   Q6LMV1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=PBPRA3047;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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; CR378673; CAG21375.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6LMV1; -.
DR   SMR; Q6LMV1; -.
DR   STRING; 298386.PBPRA3047; -.
DR   PRIDE; Q6LMV1; -.
DR   EnsemblBacteria; CAG21375; CAG21375; PBPRA3047.
DR   KEGG; ppr:PBPRA3047; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000000593; Chromosome 1.
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;
KW   Reference proteome.
FT   CHAIN           1..524
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_0000192531"
SQ   SEQUENCE   524 AA;  59265 MW;  FBA773AACA6D9245 CRC64;
     MAFMDFSQRL QQISANSDAL TQLGRGLERE ALRITSEGNL SEQPHPVGLG SALTNKWVTT
     DYAESLLEFI TPVSQDVDHL LTQLSDIHQF TYRQMGDERL WPMSMPCFVG KENDITLAQY
     GSSNTGRMKT LYREGLKHRY GSVMQVISGV HFNFSFPESF WQELFGDQSE QDRQDSISDA
     YFGLIRNYYR FGWLIPYLFG ASPALCGSFL NKHNSSVDFK QLGCGTYYLP NATALRLSDL
     GYTSNAQSSL KIGFNSLDQY LDGLNQAIRT PSDDYADIGV KVEGEYRQLN SNVLQIENEL
     YAPIRPKRVA KDGEKPSEAL GRAGVEYIEV RSLDVNPFSP IGITEDQVRF LDLFLTWAVL
     TPSDDMDDSE LACWRDNWNR VVLDGRNPDL MLKIGCNGER LSLQDWGVRV FKELQDVAVV
     MDKAAGNNKY QETCERLKGW VLNPDLTLSA QLLEKVKQNE GIGSVGHQLA AEHSQTLAER
     SYGFYSQPEF DVEAKISVEK QQKIEQGDTV SFEQFLDDYF ADLK