ID   GCS2_CORGL              Reviewed;         376 AA.
AC   Q8NM44; Q6M2B3;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Cgl2736, cg3031;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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; BA000036; BAC00130.1; -; Genomic_DNA.
DR   EMBL; BX927156; CAF20758.1; -; Genomic_DNA.
DR   RefSeq; NP_601931.1; NC_003450.3.
DR   RefSeq; WP_003853704.1; NC_006958.1.
DR   AlphaFoldDB; Q8NM44; -.
DR   SMR; Q8NM44; -.
DR   STRING; 196627.cg3031; -.
DR   GeneID; 58309034; -.
DR   KEGG; cgb:cg3031; -.
DR   KEGG; cgl:Cgl2736; -.
DR   PATRIC; fig|196627.13.peg.2667; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_11; -.
DR   OMA; LIFGLHV; -.
DR   Proteomes; UP000000582; 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"
FT                   /id="PRO_0000218195"
SQ   SEQUENCE   376 AA;  42439 MW;  05793C0B0E24ECC7 CRC64;
     MGIEFKRSPR PTLGVEWEIA LVDPETRDLA PRAAEILEIV AKNHPEVHLE REFLQNTVEL
     VTGVCDTVPE AVAELSHDLD ALKEAADSLG LRLWTSGSHP FSDFRENPVS EKGSYDEIIA
     RTQYWGNQML IWGIHVHVGI SHEDRVWPII NALLTNYPHL LALSASSPAW DGLDTGYASN
     RTMLYQQLPT AGLPYQFQSW DEWCSYMADQ DKSGVINHTG SMHFDIRPAS KWGTIEVRVA
     DSTSNLRELS AIVALTHCLV VHYDRMIDAG EELPSLQQWH VSENKWRAAR YGLDAEIIIS
     RDTDEAMVQD ELRRLVAQLM PLANELGCAR ELELVLEILE RGGGYERQRR VFKETGSWKA
     AVDLACDELN DLKALD