ID   GCS23_MYCS2             Reviewed;         365 AA.
AC   A0R3T8; I7GEI1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=MSMEG_5590, MSMEI_5440;
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; ABK73440.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP41881.1; -; Genomic_DNA.
DR   RefSeq; WP_011730643.1; NZ_SIJM01000034.1.
DR   RefSeq; YP_889826.1; NC_008596.1.
DR   AlphaFoldDB; A0R3T8; -.
DR   SMR; A0R3T8; -.
DR   STRING; 246196.MSMEI_5440; -.
DR   EnsemblBacteria; ABK73440; ABK73440; MSMEG_5590.
DR   EnsemblBacteria; AFP41881; AFP41881; MSMEI_5440.
DR   GeneID; 66736888; -.
DR   KEGG; msg:MSMEI_5440; -.
DR   KEGG; msm:MSMEG_5590; -.
DR   PATRIC; fig|246196.19.peg.5451; -.
DR   eggNOG; COG2170; Bacteria.
DR   OMA; HIHIGCP; -.
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..365
FT                   /note="Putative glutamate--cysteine ligase 2-3"
FT                   /id="PRO_0000323507"
SQ   SEQUENCE   365 AA;  39966 MW;  4E4A3BF4FE9C4B97 CRC64;
     MSNNPTFGVE EEFLLVDPRT GEPIARNKAV AETAAAKGVD LQLELTSCQV ETATEVMDNS
     DDLRKALLRL RRVATDAAET NGARLLAAGL PPTVPHKFPI TPTPRYRRIG HRFGMIAHEQ
     GICGCHVHVE VPSRDAAIRV SNRLRPWLHL LLALTANSAI YRGSDSGYAT FRSVLWARWP
     SAGPPPFFDS EAQYDATVAM LEDAGAALDD GMIYWDVRPS NKFPTVEVRV SDVPATVAET
     VLFATLVRAA VMTATEAEKN GEPVVPLTDY VLKAAYWKSA RDGLDGRTID LAESHAVAPT
     VELLTNFVEH LRPALEQLGE YDTVRGELAR VIETGNGAMR QRRAFERRRE AADVIDELAA
     ATIAE