ID   GCS2_PARXL              Reviewed;         371 AA.
AC   Q13SL4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Bxeno_A4387; ORFNames=Bxe_A0002;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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; CP000270; ABE32925.1; -; Genomic_DNA.
DR   RefSeq; WP_011490322.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q13SL4; -.
DR   SMR; Q13SL4; -.
DR   STRING; 266265.Bxe_A0002; -.
DR   EnsemblBacteria; ABE32925; ABE32925; Bxe_A0002.
DR   KEGG; bxb:DR64_2182; -.
DR   KEGG; bxe:Bxe_A0002; -.
DR   PATRIC; fig|266265.5.peg.4610; -.
DR   eggNOG; COG2170; Bacteria.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000001817; 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_0000255797"
SQ   SEQUENCE   371 AA;  41503 MW;  3E66A657BC48A0D5 CRC64;
     MSLEPFIDSK PFTFGVELEM QIVNTHDYDL TKAGSDLLRL IKDEKIPGNI TPEITESMIE
     LSTGICTTHE QAVADLRKIR DTLVSAADHL NVGLCGGGTH AFQQWSERQI VDTPRFQYLS
     ELYGYLAKQF TVFGQHVHIG CPDPNSALYL LHSMSRFIPH FIALSASSPF VQGVDTGFHS
     ARLNSVFAFP LSGRAPFVLT WDSFEEYFSK MVHTGVVNSM KDFYWDIRPK PGFGTIEVRV
     MDTPLSVDRA AAIACYIQTL ARHLLLDKPI SPKEDDYLVY TFNRFEACRF GLAGTCINPQ
     TGERKTISED ILETLDRIAP HAEALGSGNA LAEIGAIARS QVNDATWLRG VVEREKSLHE
     AVRQQCLEWR A