ID   GCS21_LEGPC             Reviewed;         383 AA.
AC   A5IAK4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=LPC_0414;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) 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; CP000675; ABQ54404.1; -; Genomic_DNA.
DR   RefSeq; WP_011947624.1; NC_009494.2.
DR   AlphaFoldDB; A5IAK4; -.
DR   SMR; A5IAK4; -.
DR   KEGG; lpc:LPC_0414; -.
DR   HOGENOM; CLU_044848_1_1_6; -.
DR   OMA; HIHIGCP; -.
DR   BioCyc; LPNE400673:LPC_RS14530-MON; -.
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 2-1"
FT                   /id="PRO_0000323504"
SQ   SEQUENCE   383 AA;  44733 MW;  6C71B749DE28B767 CRC64;
     MRLLSFKKSK IVSIGTELEF QIIDRSSLSL VSRSKELMRA LKDMRYRDQI KPEITQSMIE
     INSSIHQSAK EMYDELLELQ KILVETAASI DIAFCGGGTH PFQQWTMQKI FPSKRFKKKF
     NQYRYLSKRA TVFGQHIHIG CPTGDDAIYL THALARYVPH FIAISASSPF YLGINTNYCS
     SRSTIFNAFP LSGVIPYLRN WQEFSDYYRK MYRWKIIENM KDFYWDIRPK PELGTIEIRV
     CDTPLTLRKS ILITAYIQAL ALYLLKEKPV QLSHDLYYVY NYNRFQASRH GLEGELTVTD
     KDKPILIMDD ILETIKKIEQ YINGLGNSEY IEELYSDVIN KQNDSVLINK IYKQDGSFTK
     LVAAQCELWL SDSKDRKWMT QPS