ID   GCS2_PSEA7              Reviewed;         378 AA.
AC   A6V5Z4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Putative glutamate--cysteine ligase 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=PSPA7_3119;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC       glutamate--cysteine ligase activity. {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; CP000744; ABR85739.1; -; Genomic_DNA.
DR   RefSeq; WP_012075878.1; NC_009656.1.
DR   AlphaFoldDB; A6V5Z4; -.
DR   SMR; A6V5Z4; -.
DR   EnsemblBacteria; ABR85739; ABR85739; PSPA7_3119.
DR   KEGG; pap:PSPA7_3119; -.
DR   HOGENOM; CLU_044848_0_1_6; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000001582; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
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.
FT   CHAIN           1..378
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_1000069442"
SQ   SEQUENCE   378 AA;  42344 MW;  83AD9A4F8EF250EA CRC64;
     MIDSRADHGL RFGIEEEFFL LDATDLDIAR TAPSGFLEAC RAALGEHFAE EMFECQVEVA
     SPVFADLAQA ARFHGRARQR LAQLAAGFGL RALCVGTHPF ADWRRARSNP AAHFARLFED
     QGRVARRSLV CGLHVHVEIP ASHDRMVVLQ QVLPWLPLLL ALSASSPFRG GRRSGLASYR
     RALCGEWPRM NIPPALPDED AYRRHLALLR ESGCIREDGQ VWWMVRPSSH VPTLELRICD
     ACPRLADALC LAGLFRALVG QALLAGDAPA GPAARDACLE ENYWQAMRHG CAGRYLVDGR
     CVNARDWLER AWRQCHPQAR QGNEWAYGHA QRLLEENSAD RQLQRYQALR AEGRGRQAAL
     RRLVEELLEE NLQALPAI