ID   GCS21_NOCSJ             Reviewed;         382 AA.
AC   A1SKY7;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-1 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=Noca_2970;
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; ABL82472.1; -; Genomic_DNA.
DR   RefSeq; WP_011756409.1; NC_008699.1.
DR   AlphaFoldDB; A1SKY7; -.
DR   SMR; A1SKY7; -.
DR   STRING; 196162.Noca_2970; -.
DR   PRIDE; A1SKY7; -.
DR   EnsemblBacteria; ABL82472; ABL82472; Noca_2970.
DR   KEGG; nca:Noca_2970; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   OMA; RSQVWGR; -.
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..382
FT                   /note="Putative glutamate--cysteine ligase 2-1"
FT                   /id="PRO_0000291503"
SQ   SEQUENCE   382 AA;  41061 MW;  500B737CF92DA89E CRC64;
     MVRKLGIEEE LLLFDPESGE VVPAAPSVLK EFREHGPGRQ RARAATDELD QELFRHQLET
     RTDPVRRAAD ALDQLVAARR TAGEAARAAG YAAGACGIVP LGGDRSVVSP NDRYRDMVDT
     YGEIARTGGT CGMHVHVDIG SDEEGVAVVD RIAPWLPVLV ALAANSPYVE GRDSGYASWR
     AQVWARWPSA GPTEQFGSVA GYREVCRMLL DVGAARDPGM LYFDARLSTG QPTVEVRVCD
     VGTDPAVAVT IGALVRALVE TAAEEWADGR PAAHWRAEAL RAAHWRASRF GMADSLVHPL
     ARGLRPARSV VAALVEAVEP ALAAAGDLEL VDVQLERAVN DNGATRQRAA FERTGSVRGV
     VDDVIARTEA SWQDHDSHAG RL