ID   GCS2_PSEE4              Reviewed;         380 AA.
AC   Q1I926;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=PSEEN3084;
OS   Pseudomonas entomophila (strain L48).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=384676;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L48;
RX   PubMed=16699499; DOI=10.1038/nbt1212;
RA   Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA   Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA   Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT   "Complete genome sequence of the entomopathogenic and metabolically
RT   versatile soil bacterium Pseudomonas entomophila.";
RL   Nat. Biotechnol. 24:673-679(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; CT573326; CAK15852.1; -; Genomic_DNA.
DR   RefSeq; WP_011534240.1; NC_008027.1.
DR   AlphaFoldDB; Q1I926; -.
DR   SMR; Q1I926; -.
DR   STRING; 384676.PSEEN3084; -.
DR   PRIDE; Q1I926; -.
DR   EnsemblBacteria; CAK15852; CAK15852; PSEEN3084.
DR   KEGG; pen:PSEEN3084; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_1_6; -.
DR   OMA; HIHIGCP; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000000658; 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..380
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000291509"
SQ   SEQUENCE   380 AA;  42924 MW;  23D4CDFF55B63817 CRC64;
     MARPWTFGIE EEYLLADTTS GQVLASPSPA VTRRCREMLG ATFAEEMFLS QIEVVSPVFD
     SLHQARSFLG ENRQRLGEAL GDFGVGLYGA ASHPCAQWLR QHPRGTAHFR QLFDDYRLVA
     RRSLVNGLHV HVGVPAGTDR MQLINRVLYW LPLFLVLSTS SPLWGGQDTG YMSYRRVICG
     EWPHMGLPEP LADWHAYQRY RGLLQRTGAL AEDGDFWWAI RPSRRFPTVE LRICDGCPRL
     EDGLAIAGLY RHLVQHALAR HDGMAVSREI RWITQENYWR AARYGRRGTF IGAVDQQPVS
     AEGWLAQLQS WLPADSAEAE RSFMQARRIL REGTSADRQR EAYALARENG LAGREALRAV
     ARQVMAEHFP GAGLPQGEIE