ID   GCS2_PSEAB              Reviewed;         404 AA.
AC   Q02LX5;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=PA14_36370;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ11359.1; -; Genomic_DNA.
DR   RefSeq; WP_009315730.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02LX5; -.
DR   SMR; Q02LX5; -.
DR   PRIDE; Q02LX5; -.
DR   EnsemblBacteria; ABJ11359; ABJ11359; PA14_36370.
DR   KEGG; pau:PA14_36370; -.
DR   HOGENOM; CLU_044848_0_1_6; -.
DR   OMA; LIFGLHV; -.
DR   BioCyc; PAER208963:G1G74-3056-MON; -.
DR   Proteomes; UP000000653; 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..404
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000291508"
FT   REGION          377..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   404 AA;  44829 MW;  5860AF0B0F7B14B3 CRC64;
     MTHDLAASGL RFGIEEEFFL LDASDLDIVR SAPAGFVAAC RDTLGEHFAE EMFECQVEVA
     SPVFSTLAEA ARFHGQARQR LAHLAMDFGL RSLCVGTHPF ADWRRARSNP AAHFARLFED
     QGRVARRSLV CGLHVHVEIP PSHDRMAVLQ RVLPWLPLLL ALSASSPFRG GRRSGLASYR
     RALCGEWPRM NIPPALPDED AYRRHLALLR EAGCIREDGQ VWWMIRPSSH VPTLELRICD
     ACPRLADALS LAGLFRALVG EALGAGPRTL PVARDACLEE NYWQALRYGC AGRYLVGGRA
     VGAGDWLEMA WRQCRPQARQ GNEWAYEHAR GLLGETSASR QLRRYQTLRA AGQERHVALR
     RLVEELLEEN LQPALAGPAG KRAHEGGRSF RPAAGAPMSI RGQE