ID   GCS2_LEGPH              Reviewed;         383 AA.
AC   Q5ZS01;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=lpg2719;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS   33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA   Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA   Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA   Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA   Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA   Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA   Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL   Science 305:1966-1968(2004).
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; AE017354; AAU28776.1; -; Genomic_DNA.
DR   RefSeq; WP_010948418.1; NC_002942.5.
DR   RefSeq; YP_096723.1; NC_002942.5.
DR   AlphaFoldDB; Q5ZS01; -.
DR   SMR; Q5ZS01; -.
DR   STRING; 272624.lpg2719; -.
DR   PaxDb; Q5ZS01; -.
DR   PRIDE; Q5ZS01; -.
DR   EnsemblBacteria; AAU28776; AAU28776; lpg2719.
DR   GeneID; 66491895; -.
DR   KEGG; lpn:lpg2719; -.
DR   PATRIC; fig|272624.6.peg.2905; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_1_6; -.
DR   OMA; HIHIGCP; -.
DR   Proteomes; UP000000609; 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; Reference proteome.
FT   CHAIN           1..383
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000218202"
SQ   SEQUENCE   383 AA;  44668 MW;  592FBB1A8A70994D CRC64;
     MRLLSFKKSK IVSIGTELEF QIIDCSSLSL VSRSKELMRA LKDMRYRDQI KPEITQSMIE
     INSSIHQSAK EMYDELLELQ KILVETAASI DIAFCGGGTH PFQQWTMQKI FPSKRFKKKF
     NQYRYLSKRA TVFGQHIHIG CPTGDDAIYL THALARYVPH FIAISASSPF YLGINTNYCS
     SRSTIFNAFP LSGVIPYLRN WQEFSDYYRK MYRWKIIENM KDFYWDIRPK PELGTIEIRV
     CDTPLTLRKS ILITAYIQAL ALYLLEEKSV QLSHDLYYVY NYNRFQASRH GLEGELTVTD
     KDRPIPIMDD ILETIKKIEQ YINGLGNSEY IEELYSDVIN KQNDSVLINK IYKQDGSFSK
     LVAAQCELWL SDSKDRKWMT QPS