GCS2_BURM1
ID GCS2_BURM1 Reviewed; 371 AA.
AC A9AJC7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=Bmul_0069, BMULJ_00001;
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT 17616.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249;
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) 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; CP000868; ABX13764.1; -; Genomic_DNA.
DR EMBL; AP009385; BAG41986.1; -; Genomic_DNA.
DR RefSeq; WP_006401501.1; NC_010804.1.
DR AlphaFoldDB; A9AJC7; -.
DR SMR; A9AJC7; -.
DR STRING; 395019.Bmul_0069; -.
DR EnsemblBacteria; BAG41986; BAG41986; BMULJ_00001.
DR KEGG; bmj:BMULJ_00001; -.
DR KEGG; bmu:Bmul_0069; -.
DR eggNOG; COG2170; Bacteria.
DR HOGENOM; CLU_044848_1_1_4; -.
DR OMA; LIFGLHV; -.
DR Proteomes; UP000008815; 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_1000148209"
SQ SEQUENCE 371 AA; 41812 MW; 9D857030CDE17765 CRC64;
MALETFVNSE PFTFGVELEI QVVNTHNYDL TKAASDLMRL IQGETFPGNI TPEITESMIE
LSTGICHTHE QALGELHAIR DVLVKAADQL NVGLAGGGTH AFQQWSDRQI YDAPRFQYLS
ELYGYLAKQF TVFGQHVHIG CPDPDSALFL LHSMSRFIPH FIALSASSPF VQNVDTGFHS
ARLNSVFAFP LSGRAPFALT WHDFEEYFTK MVNTGVVNSM KDFYWDIRPK PGYGTIEVRV
MDTPLSVDRA AAIACYIQTL ARYLLIDRPL TLTEDDYLVY TFNRFEACRF GLEGTCVNPQ
TGERRTIAED ILDTLDRIAP HAAELGSRAA LDEIGALAKA RVNDASWLRT VFKQEKSLNE
TVRQQCLRWR E