ID   GCS2_MYCTA              Reviewed;         376 AA.
AC   A5TZF9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=MRA_0438;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ72159.1; -; Genomic_DNA.
DR   RefSeq; WP_003900145.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5TZF9; -.
DR   SMR; A5TZF9; -.
DR   STRING; 419947.MRA_0438; -.
DR   EnsemblBacteria; ABQ72159; ABQ72159; MRA_0438.
DR   KEGG; mra:MRA_0438; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_11; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000001988; 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..376
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_1000069441"
SQ   SEQUENCE   376 AA;  42295 MW;  4DF1093357169E40 CRC64;
     MPARRSAARI DFAGSPRPTL GVEWEFALVD SQTRDLSNEA TAVIAEIGEN PRVHKELLRN
     TVEIVSGICE CTAEAMQDLR DTLGPARQIV RDRGMELFCA GTHPFARWSA QKLTDAPRYA
     ELIKRTQWWG RQMLIWGVHV HVGIRSAHKV MPIMTSLLNY YPHLLALSAS SPWWGGEDTG
     YASNRAMMFQ QLPTAGLPFH FQRWAEFEGF VYDQKKTGII DHMDEIRWDI RPSPHLGTLE
     VRICDGVSNL RELGALVALT HCLIVDLDRR LDAGETLPTM PPWHVQENKW RAARYGLDAV
     IILDADSNER LVTDDLADVL TRLEPVAKSL NCADELAAVS DIYRDGASYQ RQLRVAQQHD
     GDLRAVVDAL VAELVI