ID   GCS21_NOCFA             Reviewed;         383 AA.
AC   Q5YW64;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=NFA_27300;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD57577.1; -; Genomic_DNA.
DR   RefSeq; WP_011209262.1; NC_006361.1.
DR   AlphaFoldDB; Q5YW64; -.
DR   SMR; Q5YW64; -.
DR   STRING; 247156.NFA_27300; -.
DR   EnsemblBacteria; BAD57577; BAD57577; NFA_27300.
DR   GeneID; 61133469; -.
DR   KEGG; nfa:NFA_27300; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   OMA; HIHIGCP; -.
DR   BioCyc; NFAR247156:NFA_RS13655-MON; -.
DR   Proteomes; UP000006820; 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..383
FT                   /note="Putative glutamate--cysteine ligase 2-1"
FT                   /id="PRO_0000218209"
SQ   SEQUENCE   383 AA;  41023 MW;  3A3E3DC98A553CB4 CRC64;
     MDAPTVGVEE EFLLVDPRTG APTARNEAVA HTAGELGIDL QLELTRCQVE TSTAVHSDIG
     ALFGQLRDLR CGVARCAQAN ESRLLAVAIP PTVPHEFPVT DTPRYRRIAE SFGMIAHEQG
     LCGCHVHVAV PDRETAVQVS NYLRPWLPML LALTANSAIY RGSDTGYASW RSILWRRWPS
     AGPPPYFRTA ADYDAMVTMM LSSGIVLDEK MVYWDARPSI NYPTIEVRVS DVPATVGETV
     LLAALVRATV HTARRFLAEG NTAPAVPAEV LRAAYWKAAR SGIGGDAVAP LDGRVLPARD
     LLDELLETVD PALEELGDRG FVSDALTALL ARGNGAQRQV RAFGADHDVA AVIAELGAAT
     LEGCAPEPAN SGGGEHVPVE GRH