ID   GCS21_LEGPA             Reviewed;         373 AA.
AC   Q5X7D7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=lpp0668;
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; CAH11816.1; -; Genomic_DNA.
DR   RefSeq; WP_011213216.1; NC_006368.1.
DR   AlphaFoldDB; Q5X7D7; -.
DR   SMR; Q5X7D7; -.
DR   KEGG; lpp:lpp0668; -.
DR   LegioList; lpp0668; -.
DR   HOGENOM; CLU_044848_1_1_6; -.
DR   OMA; LIFGLHV; -.
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..373
FT                   /note="Putative glutamate--cysteine ligase 2-1"
FT                   /id="PRO_0000218200"
SQ   SEQUENCE   373 AA;  42871 MW;  D7DD617A75E220D6 CRC64;
     MPLQPFKTSN LLTMGVELEL QLISLSNFDL TAASPDILEL LGRSSFPGSF TPEITESMLE
     IATDVHEEYD QLLKQLFHIR DTLVTVGDRL NIGICGGGTH PFQMWSNQRI FNKTRFIEVS
     ELYGYLTKQF TIFGQHIHIG CEDGNQALFL LHSLNRYIPH FIALSASSPF VQSKDTLYNS
     ARLNSVFAFP LSGRAPFVLN WDEFSLGYFE KMEHTGIVKS MKDFYWDLRP KPEFGTIEMR
     VCDSPLTVER AAALACYMQA LCSYLLENKE PLPHEDDYLV YNYNRFQACR FGLDGTLVHP
     KTYEQILLRE DILTTLRRLK PYANQLNSTM ALEHIYEITH KGSDASFLRE KYAEHRTLES
     VVNESLKQFR SSK