ID   GCS2_MYCA1              Reviewed;         379 AA.
AC   A0QLR0;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=MAV_4721;
OS   Mycobacterium avium (strain 104).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=243243;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-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; CP000479; ABK64676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0QLR0; -.
DR   SMR; A0QLR0; -.
DR   EnsemblBacteria; ABK64676; ABK64676; MAV_4721.
DR   KEGG; mav:MAV_4721; -.
DR   HOGENOM; CLU_044848_1_0_11; -.
DR   OMA; LIFGLHV; -.
DR   Proteomes; UP000001574; Chromosome.
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..379
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000291493"
SQ   SEQUENCE   379 AA;  42826 MW;  600F424CD227F178 CRC64;
     MSSVPARRGD AHIDFARSPR PTIGVEWEFA LVDAQTRDLS NEATAVIAEI GENPRVHKEL
     LRNTVEVVSG ICRTVPEAME DLRQTLGPAR RIVRDRGMEL FCAGAHPFAQ WTTQKLTDAP
     RYAELIKRTQ WWGRQMLIWG VHVHVGISSP NKVMPIMTSL LNYYPHLLAL SASSPWWTGV
     DTGYASNRAM MFQQLPTAGL PFQFQTWAEF EGFVYDQKKT GIIDHVDEVR WDIRPSPHLG
     TLEMRICDGV SNLHELAALV ALTHCLVVDL DRRLEADESL PTMPPWHHQE NKWRAARYGL
     DAVIILDADS NERLVTEDLD DVLNRLEPVA RKLQCADELA AVADIPRHGA SYQRQRRVAE
     EHDGDLRAVV DALVAELEI