ID   GCS22_MYCSK             Reviewed;         364 AA.
AC   A1ULE3;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=Mkms_4460;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
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   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-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; CP000518; ABL93651.1; -; Genomic_DNA.
DR   RefSeq; WP_011768368.1; NC_008705.1.
DR   AlphaFoldDB; A1ULE3; -.
DR   SMR; A1ULE3; -.
DR   STRING; 189918.Mkms_4460; -.
DR   EnsemblBacteria; ABL93651; ABL93651; Mkms_4460.
DR   KEGG; mkm:Mkms_4460; -.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   OMA; HIHIGCP; -.
DR   OrthoDB; 991285at2; -.
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..364
FT                   /note="Putative glutamate--cysteine ligase 2-2"
FT                   /id="PRO_0000291498"
SQ   SEQUENCE   364 AA;  39449 MW;  CA93FF4A4262138E CRC64;
     MAAHPTVGVE EEFLLVDPDS GAPIARNRDV ARHAADRGVD LQLELTSCQV ETATGVASSM
     ADVREQLTHL RSTVARAADD SGARLLAVAV PPTVPHEFPV TDNPRYHRIA ERFGMLAREQ
     GICGAHVHVA VPTREVAIRV SNRLRPWLPV LLALTANSAI YRNADSGYAS WRRMLWARWP
     SAGPPPHFDS ADEFDAMVRM LLQSGAMLDE GQVYWDVRPS ADFPTIEVRV ADVPATVADT
     VLFAAIVRAT VMTLLGDERD GAGVPRISAH ALDAAYWRSA RDGLDGIAID LAESHAPMPA
     RDLLGVLVDR ITPALRAVGD HDLVRDGLAR LDDEGNGAMR QRAAWRRRGE IADVIDAVAE
     ATLA