ID   GCS21_MYCS2             Reviewed;         376 AA.
AC   A0QQQ2; I7FX34;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=MSMEG_0836, MSMEI_0817;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
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.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
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; CP000480; ABK73867.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP37297.1; -; Genomic_DNA.
DR   RefSeq; WP_003892265.1; NZ_SIJM01000010.1.
DR   RefSeq; YP_885240.1; NC_008596.1.
DR   AlphaFoldDB; A0QQQ2; -.
DR   SMR; A0QQQ2; -.
DR   STRING; 246196.MSMEI_0817; -.
DR   EnsemblBacteria; ABK73867; ABK73867; MSMEG_0836.
DR   EnsemblBacteria; AFP37297; AFP37297; MSMEI_0817.
DR   GeneID; 66739008; -.
DR   KEGG; msg:MSMEI_0817; -.
DR   KEGG; msm:MSMEG_0836; -.
DR   PATRIC; fig|246196.19.peg.829; -.
DR   eggNOG; COG2170; Bacteria.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; 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; Reference proteome.
FT   CHAIN           1..376
FT                   /note="Putative glutamate--cysteine ligase 2-1"
FT                   /id="PRO_0000323505"
SQ   SEQUENCE   376 AA;  41970 MW;  9AAEDD951D4A1F90 CRC64;
     MSSLPADSRI DFAGSPRPTV GVEWEFALVD AKTRELSNEA AAVIAEIGEN PHVHKELLRN
     TVEIVTGICE NSGEAMGDLC DTLSTVRRAV RGRGMELFCA GTHPFGKWSA AQLTDAPRYA
     ELIKRTQWWG RQMLIWGVHV HVGVSSAHKV MPIISSLLNQ YPHLLALSAS SPFWDGEDTG
     YASNRAMMFQ QLPTAGLPFQ FQTWHEFEGF VHDQKKTGII DHLSEIRWDI RPSPQLGTVE
     VRIFDGVSNV RELSALVALT HCLIVDLDRR LDAGEQLPVM PPWHVQENKW RAARYGLDAV
     IILDADSNER LVTEDLDDLL NHLEPVAASL HCADELAAVE DIYRLGGSYQ RQRRVAEEND
     GDLREVVDAL IGELEL