ID   GCS22_SACEN             Reviewed;         391 AA.
AC   A4FHB5;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
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=SACE_4171;
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; CAM03440.1; -; Genomic_DNA.
DR   RefSeq; WP_009946756.1; NZ_PDBV01000001.1.
DR   AlphaFoldDB; A4FHB5; -.
DR   SMR; A4FHB5; -.
DR   STRING; 405948.SACE_4171; -.
DR   EnsemblBacteria; CAM03440; CAM03440; SACE_4171.
DR   KEGG; sen:SACE_4171; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   OMA; CCGCHVH; -.
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..391
FT                   /note="Putative glutamate--cysteine ligase 2-2"
FT                   /id="PRO_0000291515"
SQ   SEQUENCE   391 AA;  41094 MW;  80A7379EBDEB6053 CRC64;
     MGLQEHPVTP AERQPPVRGG VTIGVEEEFL LVDAASGQLA PHAEAVLAEA ANGPLGAPDA
     VLHAEMLNSQ VEAATGCCRT LEELRSQLVA ARTSLDRAAS VAGARIVSSG TPVLAVEGTG
     TSNGQRFADI AERYRAVASD YHVCGCHVHV GVPDRDTAVA VVNHLRPWLP TLLAISANSP
     FHLGHDTGHA SWRGVQQRLY PGSGVPPHFP SRDAYDREVA RLVDCGALVD DRMSFWMARP
     SPHLPTVELR VADALITAEE TVLQAALSRA LVRAALDDLA AGREGDEVSD QVAAAAVWNA
     SRYGLRGPAV DPVPARRVPA LEMVERLLRR VGPALEQTGD SALVREALAH VTGVGTGSER
     QRAAAAAGGP REVVAMLAAA TAPGRADRLR T