ID   GCS2_SALAI              Reviewed;         378 AA.
AC   A8M5J6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Sare_2729;
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000850; ABV98564.1; -; Genomic_DNA.
DR   RefSeq; WP_012182865.1; NC_009953.1.
DR   AlphaFoldDB; A8M5J6; -.
DR   SMR; A8M5J6; -.
DR   STRING; 391037.Sare_2729; -.
DR   PRIDE; A8M5J6; -.
DR   EnsemblBacteria; ABV98564; ABV98564; Sare_2729.
DR   GeneID; 5704470; -.
DR   KEGG; saq:Sare_2729; -.
DR   PATRIC; fig|391037.6.peg.2766; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   OMA; HIHIGCP; -.
DR   OrthoDB; 991285at2; -.
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.
FT   CHAIN           1..378
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000337703"
SQ   SEQUENCE   378 AA;  40873 MW;  D95F28984305FB2A CRC64;
     MTYRPATDGP DLASLTLGVE EEFLLLDAET GESMPVAARV LDGLSGVAHA QSRREFRHSM
     VEMVTPVLSD LAELRRHLVA LRTAAADAAE AAGARLVAVG ATPVNETHRT VPDEPRYHAM
     SRRFGPVAHD PAVCGCHVHV GLPDRELAVQ VCNHLRPWLP VVQAITANSP LHDGQDTGHA
     SWRAMQLERW PSIGPTPYFD SAADYDATVA DLIKAGIMLD AGMVYWYVRP SAAYPTVEIR
     VGDVCPTVDD TVLVAGLVRA LVATVAADVH DGARAPRIRG CLLSAAHWRA AHDGLDGDLV
     DLRTGRARPA WDLVDDLFAL VTPALERQGD RAYVRDQLAR VRAEGTGAVR QRRILDRSAC
     DVRAVLDHLA AQTRPAPV