ID   GCS2_STRCO              Reviewed;         363 AA.
AC   Q9KY07;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=SCO7331; ORFNames=SC410.10c, SC4G10.10c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939131; CAB92877.1; -; Genomic_DNA.
DR   RefSeq; NP_631385.1; NC_003888.3.
DR   RefSeq; WP_011031591.1; NZ_VNID01000019.1.
DR   AlphaFoldDB; Q9KY07; -.
DR   SMR; Q9KY07; -.
DR   STRING; 100226.SCO7331; -.
DR   GeneID; 1102769; -.
DR   KEGG; sco:SCO7331; -.
DR   PATRIC; fig|100226.15.peg.7435; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   InParanoid; Q9KY07; -.
DR   OMA; WQRWPSA; -.
DR   PhylomeDB; Q9KY07; -.
DR   Proteomes; UP000001973; 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:0016879; F:ligase activity, forming carbon-nitrogen bonds; IBA:GO_Central.
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..363
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000218222"
SQ   SEQUENCE   363 AA;  39895 MW;  A68F0F516509E81B CRC64;
     MRTVGVEEEL LLVDPATGEP RALSAAVLAR AFLDDSEQDV FEKELHEQML EFATHPQADM
     ERLHAEIVRC REEAGRHAGG IGCAVAALAT SPLPVTPSIG VNRRYEWMAE QYGVVVHEQL
     VLGCHVHVSV DSDEEGVAVI DRVRPWLPVL AALSANSPFW QGRDSSYSSY RSRVWQRWPS
     AGPTELFGSA ERYHRRVADM LATGTVLDDG MVYFDVRLSQ RYPTVEFRVA DVCLDASTAV
     VLAALARALV DTAAREWRAG AEPAEHSVSL LRLAAWRAAR SGLTSELLHP ATMRRMPAES
     VVRDLLEHAG EALAAAGDLE RVREGVEKLL RHGNGARVQR ELLARTGSLR EVVAACVRRT
     QAA