ID   GCS2_MYCSS              Reviewed;         376 AA.
AC   Q1BEJ0;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Mmcs_0573;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-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; CP000384; ABG06694.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1BEJ0; -.
DR   SMR; Q1BEJ0; -.
DR   KEGG; mmc:Mmcs_0573; -.
DR   HOGENOM; CLU_044848_1_0_11; -.
DR   OMA; LIFGLHV; -.
DR   BioCyc; MSP164756:G1G6O-585-MON; -.
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..376
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000291499"
SQ   SEQUENCE   376 AA;  42229 MW;  F78A43F52C4EB867 CRC64;
     MLSVPASSRI DFAGSPRPTV GVEWEFALVD AHTRDLSNEA ATVIAEIGET PHVHKELLRN
     TVEVVTGICE NTGEAMADLH DTLKVVRRIV RDRGMELFCA GTHPFANWST QQLTDAPRYA
     ELIKRTQWWG RQMLIWGVHV HVGISSAHKV MPIISSLLNQ YPHLLALSAS SPYWDGSDTG
     YASNRAMMFQ QLPTAGLPFQ FQSWPEFERF VHDQKKTGII DHMNEIRWDI RPSPHLGTVE
     IRVFDGVSNI AELGSLVALT HCLVVDLDRR LDAGEQLPVM PPWHVQENKW RAARYGLDAE
     IILDADSNER LVTEDLDDLL TRLQPVARSL DCADELAGVA EIYRHGASYQ RQRRVAEEHD
     GDLLAVVDAL VAELEL