ID   GCS2_CUPPJ              Reviewed;         371 AA.
AC   Q46VZ0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Reut_A3336;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ62694.1; -; Genomic_DNA.
DR   RefSeq; WP_011299463.1; NC_007347.1.
DR   AlphaFoldDB; Q46VZ0; -.
DR   SMR; Q46VZ0; -.
DR   STRING; 264198.Reut_A3336; -.
DR   EnsemblBacteria; AAZ62694; AAZ62694; Reut_A3336.
DR   KEGG; reu:Reut_A3336; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_1_4; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
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..371
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000255806"
SQ   SEQUENCE   371 AA;  41804 MW;  9F7CC425E26608B4 CRC64;
     MSLEPFKHSE ALTFGVELEL QLVNRHDYDL APFAPDLLRA LKGAQHAGDI KPEISPSMIE
     ISTGICHTYQ QALDELTTMR DLMQAASRSL NIGISGGGTH PFQQWADRII SDSPRYQYIS
     ELYGYLAKQF TVFGQHVHIG CPSADESLFL LHAIGRYVPH FVALAASSPY VQGVDTGFAS
     ARLNSVAAFP MSGRAPFLLT WDAFTAYFEK MRNTGVIESM KDFYWDIRPK PEFGTIEVRV
     MDTPLTVERA CDIAAYIQML ARYLLLSRPF MPQEDDYLVY TFNRFQACRF GLEGEYVHPN
     ELTRRPIAEH ILSICDALVP HAEALGSMQA LANIRALAEN RNGDAEWLRQ VDADARTQRE
     TVRQACERWA A