ID   GCS22_COREF             Reviewed;         369 AA.
AC   Q8FT06;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   25-MAY-2022, entry version 86.
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=CE2886;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC19696.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000035; BAC19696.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_006768756.1; NZ_GG700684.1.
DR   AlphaFoldDB; Q8FT06; -.
DR   SMR; Q8FT06; -.
DR   STRING; 196164.23494731; -.
DR   EnsemblBacteria; BAC19696; BAC19696; BAC19696.
DR   KEGG; cef:CE2886; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000001409; 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..369
FT                   /note="Putative glutamate--cysteine ligase 2-2"
FT                   /id="PRO_0000218194"
SQ   SEQUENCE   369 AA;  40448 MW;  6723A4AD3DD10720 CRC64;
     MRTFGVEEEL LLVDAVTFSP LPAGDRAVQL HTEAHEATGT DPGGYEITRE FQQEQFEVAY
     PPQTTLADQL ETIRAGRALA DTAASRVGGR VVALPTSPGP ISPHLVPNPR YQRISERFGF
     TVKEQLTCGF HIHVQVESPA EAVAVLDRVR VWLPVVLALS ANSPFWQGFD TDFASYRYQA
     WNRWPTAGPT DVFGSADAYE QHRAALLSAG VPLDPGMLYF DARVCEHHPT VEIRVADVCL
     EAEHTAVIAT LVRALVETVA REWAAGMPAP DVPASVLQLW SWRASRYGTE EELIDQATGQ
     PAPAAEVLAG FLSYLRPVLS EYGELEVVEA TVADILREGT GARRQRAAYA ARGRLVDVIT
     TALDITHRR