ID   GCS21_SACEN             Reviewed;         374 AA.
AC   A4FDR2;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=SACE_2909;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS   NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC   2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA   Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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; AM420293; CAM02187.1; -; Genomic_DNA.
DR   RefSeq; WP_009946332.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4FDR2; -.
DR   SMR; A4FDR2; -.
DR   STRING; 405948.SACE_2909; -.
DR   EnsemblBacteria; CAM02187; CAM02187; SACE_2909.
DR   KEGG; sen:SACE_2909; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   OMA; MLYWYAR; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000006728; 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..374
FT                   /note="Putative glutamate--cysteine ligase 2-1"
FT                   /id="PRO_0000291514"
SQ   SEQUENCE   374 AA;  40549 MW;  BFC4BF41F6F4976D CRC64;
     MLDLTLGVEE EFLLLDPGTL EPAAAADRFR AETDRGEVHR ELAPAQIESA TAVCRTLEEL
     HHDLSGLRRA LAADAAEQGY RLASVGVPPI GSAGPPPVTD SPRYRRMYET YGSIIEDQGV
     CGCHVHVGAL DLETALVAGN HLRPWLPALL LLTTNSPFFR GGDTGYASWR TTLWSRWPAA
     GPPPVLTSAR HYHYVVDCLL ASGAVLDSGM LYWYARPSHR VPTLEVRVAD AAATVDEAVL
     LAGLVRGLVG VALSDRPGPV RPVDDAVLRA ACWCSAHHGL EGFSLDVGTG RLVPSWHLVD
     DLVEHVRPVL ERYGDLDAVR ALLAKLRENG SAARRQREVF RRHRDIGEVV EHVLVETVPD
     ENAALPGRSI SPSA