ID   GCS22_LEGPA             Reviewed;         383 AA.
AC   Q5X1G7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=lpp2776;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(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; CR628336; CAH13929.1; -; Genomic_DNA.
DR   RefSeq; WP_015961775.1; NC_006368.1.
DR   AlphaFoldDB; Q5X1G7; -.
DR   SMR; Q5X1G7; -.
DR   KEGG; lpp:lpp2776; -.
DR   LegioList; lpp2776; -.
DR   HOGENOM; CLU_044848_1_1_6; -.
DR   OMA; HIHIGCP; -.
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..383
FT                   /note="Putative glutamate--cysteine ligase 2-2"
FT                   /id="PRO_0000218201"
SQ   SEQUENCE   383 AA;  44589 MW;  D2EC94CDAF80845F CRC64;
     MRLLSFKKSK IVSIGTELEF QIIDCSSLSL VSRSKELMRA LKDMRYRDQI KPEITQSMIE
     INSSIHQSAK EMYDELLELQ KILVETAASI DIAFCGGGTH PFQQWTMQKI FPSKRFKKKF
     NQYRYLSKRA TVFGQHIHIG CPTGDDAIYL THALARYVPH FIAISASSPF YLGINTNYCS
     SRSTIFNAFP LSGVIPYLRS WQEFSDYYRK MYRWKIIENM KDFYWDIRPK PELGTIEIRV
     CDTPLTLRKS ILITAYIQAL ALYLLEERPV QLSHDLYYVY NYNRFQASRH GLEGELTVTD
     KDRPIPIMDD ILETIKKIEQ YINGLGNGEY IEELCSDVIN KQNDSVLINK IYKQDGSFSK
     LVAAQCELWL SDSKDRKWMT QPS