ID   GCS2_CLAMS              Reviewed;         383 AA.
AC   B0REM7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   25-MAY-2022, entry version 70.
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=CMS0754;
OS   Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS   / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=31964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX   PubMed=18192393; DOI=10.1128/jb.01598-07;
RA   Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA   Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA   Parkhill J., Ishimaru C.A.;
RT   "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT   sepedonicus suggests recent niche adaptation.";
RL   J. Bacteriol. 190:2150-2160(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAQ00874.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM849034; CAQ00874.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; B0REM7; -.
DR   SMR; B0REM7; -.
DR   STRING; 31964.CMS0754; -.
DR   EnsemblBacteria; CAQ00874; CAQ00874; CMS0754.
DR   KEGG; cms:CMS0754; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_11; -.
DR   Proteomes; UP000001318; 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..383
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000337698"
SQ   SEQUENCE   383 AA;  42337 MW;  FA47741E3B1E09AA CRC64;
     MDGRTRMQID FARQPPSRVG IEWELACVDR GSGELAGVAP QILRSFPHDD AHPHVTGEFL
     TNTVEVVSAP HSRVGHAVDD LARLIERVVD VADPLGIDLM CAGTHPFSAW PDQDVTPDNE
     RYATLLDRTR WWGRQMMIWG VHVHVGIEDG SKALPILNAL LVHLPRFQAL SASSPFWSGQ
     ETGYASNRAL MFQQLPTAGL PPDLTTWADY ERLIGDMTHV GVIDHHSELR WDIRPAPKWG
     TLETRVFDGV STLGEIASLA ALVQCLVHDL SAALDRGEEL PRMQPWFVRE NKWRAARYGM
     DAIIIQDAAG EEALVGDDTR ALVERLSPTA DALGCEAELR GILDIVDRGA SYQRQLRVAE
     ENDGALAPVV THLVEELRSG LGR