ID   GCS23_NOCSJ             Reviewed;         376 AA.
AC   A1SN17;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=Noca_3702;
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) 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; CP000509; ABL83202.1; -; Genomic_DNA.
DR   RefSeq; WP_011757133.1; NC_008699.1.
DR   AlphaFoldDB; A1SN17; -.
DR   SMR; A1SN17; -.
DR   STRING; 196162.Noca_3702; -.
DR   EnsemblBacteria; ABL83202; ABL83202; Noca_3702.
DR   KEGG; nca:Noca_3702; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_1_11; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000000640; 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..376
FT                   /note="Putative glutamate--cysteine ligase 2-3"
FT                   /id="PRO_0000291505"
SQ   SEQUENCE   376 AA;  41962 MW;  7E834748CBCE9A1F CRC64;
     MRIDFHASPE PTLGVEWEFA LVDRRTRDLR NDATHLFARA KPRLPDPDKL HKELLRNTVE
     VVSGVCHTVG EAMADLRRTL EVVVPAGDDL DLDLYGGGTH PFASWTVQQL SEGHRYEELI
     NRTQWWGRQM LIWGVHVHVG MPERDRVMAV LSSLLNFHPH LQALSASSPI WSGIDTGYAS
     NRALMFQQLP TAGLPFQFER WSEFEAFVGD ELVTGVIEEL SEVRWDVRPA PRIGTLENRI
     CDGVPDLADL SSLVALMHCL VVDLDTRAAA GETLPTMPPW HVQENKWRAA RYGLDAIVIT
     DAESNERLVT EDLADHLERL APVADRLGCS EELAQVAQIP VRGASYQRQR AVAERTGGDL
     VAVVDSVVRE LRAGLG