ID   GCS2_BURCM              Reviewed;         371 AA.
AC   Q0BJQ3;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Bamb_0059;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000440; ABI85620.1; -; Genomic_DNA.
DR   RefSeq; WP_006751345.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BJQ3; -.
DR   SMR; Q0BJQ3; -.
DR   STRING; 339670.Bamb_0059; -.
DR   EnsemblBacteria; ABI85620; ABI85620; Bamb_0059.
DR   GeneID; 44690745; -.
DR   GeneID; 60995395; -.
DR   KEGG; bam:Bamb_0059; -.
DR   PATRIC; fig|339670.21.peg.1575; -.
DR   eggNOG; COG2170; Bacteria.
DR   OMA; LIFGLHV; -.
DR   Proteomes; UP000000662; 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.
FT   CHAIN           1..371
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000291488"
SQ   SEQUENCE   371 AA;  41767 MW;  CBCFC606E3AE47CD CRC64;
     MALETFVNSE PFTFGVELEI QVVNTHNYDL TKAASDLMRL IQGETFPGNI TPEITESMIE
     LSTGICHSHE QAVSELHAIR DVLVKAADQL NVGLCGGGTH AFQQWSDRQI YDAPRFQYIS
     ELYGYLAKQF TVFGQHVHIG CPDPDSALFL LHSMSRFIPH FIALSASSPF VQNVDTGFHS
     ARLNSVFAFP LSGRAPFVLT WDSFEEYFTK MVNTGVVNSM KDFYWDIRPK PGYGTIEVRV
     MDTPLSVDRA AAIACYIQTL ARYLLTDRPL KLSEDDYLVY TFNRFEACRF GLEGTCVNPQ
     TGERRTIAED ILDTLDRIAP HAAALGSRAA LDEIGALAKA RVNDASWLRT VFKQEKSLNE
     TVRQQCLRWR E