ID   GCS2_SALTO              Reviewed;         378 AA.
AC   A4X7Y6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Strop_2542;
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(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; CP000667; ABP54986.1; -; Genomic_DNA.
DR   RefSeq; WP_012013767.1; NC_009380.1.
DR   AlphaFoldDB; A4X7Y6; -.
DR   SMR; A4X7Y6; -.
DR   STRING; 369723.Strop_2542; -.
DR   EnsemblBacteria; ABP54986; ABP54986; Strop_2542.
DR   KEGG; stp:Strop_2542; -.
DR   PATRIC; fig|369723.5.peg.2618; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   OMA; HIHIGCP; -.
DR   Proteomes; UP000000235; 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..378
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000337704"
SQ   SEQUENCE   378 AA;  40999 MW;  5AAAAF8FE75DED11 CRC64;
     MTYRPATDPP DLDTLTLGVE EEFLLLDSDT GESMPVAARV LDGLSGTAYE QSRREFRHSM
     VEMVTPVVSD LAELRRHLVA LRTAAAEAAE SAGAHLVAVG ATPVNETHRT VPDEPRYHAM
     SRRFGPVAHD PAVCGCHVHV GLPDRELAVQ VCNHLRPWLP VVQAITANSP LHDGQDTGHA
     SWRAMQLERW PSIGPTPYFD SAADYDATVA DLIKAGIMLD AGMVYWYVRP SAAFPTVEIR
     VGDVCPTVDD TVLVAALVRA LVATLAADVR DGARATRIRG CLVSAAHWRA AHDGLDGDLV
     DLRTGHARPA WDLVDELFAL VAPALERQGD RAYVLDQLAR LRDEGTGAAR QRRILERTGC
     DVRAVLAHLA AQTRPVPA