ID   GCS2_CUPNH              Reviewed;         371 AA.
AC   Q0K5N7;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=H16_A3627;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(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; AM260479; CAJ94684.1; -; Genomic_DNA.
DR   RefSeq; WP_010812176.1; NZ_CP039287.1.
DR   AlphaFoldDB; Q0K5N7; -.
DR   SMR; Q0K5N7; -.
DR   STRING; 381666.H16_A3627; -.
DR   EnsemblBacteria; CAJ94684; CAJ94684; H16_A3627.
DR   GeneID; 57645759; -.
DR   KEGG; reh:H16_A3627; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_1_4; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000008210; Chromosome 1.
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..371
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000291511"
SQ   SEQUENCE   371 AA;  41722 MW;  B80A195A64863D7E CRC64;
     MSLETFKHSE ALTFGVELEL QLVNRHDYDL APFAPDLLRA LKGAEHAGDI KPEISPSMIE
     ISTGICHTYQ QALEELTVMR DLMVAASRSL NLGIAGGGTH PFQQWADRTI SDSPRYQYIS
     ELYGYLAKQF TVFGQHVHIG CPSADESLFL LHAIGRYVPH FVALAASSPY VQGVDTGFAS
     ARLNSVAAFP MSGRAPFLLT WDAFTAYFEK MRNTGVIESM KDFYWDIRPK PEFGTIEVRV
     MDTPLTVQRA CDIAAYIQML ARYLLLSRPF MPQEDDYLVY TFNRFQACRF GLEGEYVHPN
     ELTRMPIADH ILSICDALVP HAEALGSLEA LANIRALAER RDGDAEWLRQ VDADARSQRE
     TVRKACDRWA A