ID   GCS2_PSEPK              Reviewed;         368 AA.
AC   Q88HV0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=PP_3253;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN68860.1; -; Genomic_DNA.
DR   RefSeq; NP_745396.1; NC_002947.4.
DR   RefSeq; WP_010954135.1; NC_002947.4.
DR   AlphaFoldDB; Q88HV0; -.
DR   SMR; Q88HV0; -.
DR   STRING; 160488.PP_3253; -.
DR   EnsemblBacteria; AAN68860; AAN68860; PP_3253.
DR   KEGG; ppu:PP_3253; -.
DR   PATRIC; fig|160488.4.peg.3456; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_1_6; -.
DR   OMA; LIFGLHV; -.
DR   PhylomeDB; Q88HV0; -.
DR   BioCyc; PPUT160488:G1G01-3479-MON; -.
DR   Proteomes; UP000000556; 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..368
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000218212"
SQ   SEQUENCE   368 AA;  41466 MW;  BF9CC3CFBBE8D240 CRC64;
     MIRPCTFGIE EEYLLVNLGS GQVPATPSPA VMGRCREALG RYFAQEMFRS QIELASPVFT
     NLYEAREFLQ RNRQRLRVAL AEEGMGPYAA ASHPCAAWLL QKPAAQGHYK QLFDDYRHVA
     RRSLLNGLHV HVGVPPACDR MQLINRLLPW LPLLLALSTS SPLWAGQPTG YLSYRRVICG
     EWPHMGLPEA LPDWAAYERY RALLQRTGAL AADGDLWWAL RPSRRYPTVE LRICDGCPNL
     EDVLCIAALF RHLVEHSIAY RHDPLPCSRE LRWIAQENYW RAMRHGRHAQ FIGCHEQQPV
     TAQGWLAQLQ AQIPIDSADA ERACQHALHV LRHGTHADQQ LRCLAQARAD GLGKGQALRA
     VVAAGTCI