ID   GCS22_NOCFA             Reviewed;         380 AA.
AC   Q5YNU2;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=NFA_52970;
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; BAD60149.1; -; Genomic_DNA.
DR   RefSeq; WP_011211831.1; NC_006361.1.
DR   AlphaFoldDB; Q5YNU2; -.
DR   SMR; Q5YNU2; -.
DR   STRING; 247156.NFA_52970; -.
DR   EnsemblBacteria; BAD60149; BAD60149; NFA_52970.
DR   GeneID; 61135872; -.
DR   KEGG; nfa:NFA_52970; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_1_11; -.
DR   OMA; LIFGLHV; -.
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..380
FT                   /note="Putative glutamate--cysteine ligase 2-2"
FT                   /id="PRO_0000218210"
SQ   SEQUENCE   380 AA;  42359 MW;  91842D188882D523 CRC64;
     MAGVVESVPF EGSPRPTIGI EWEVALVDKV TRDLSNTAAA VFDAVGDLRA WDGTPQVTKE
     LLRNTVEIVT GVHETVGAAV EDLRGTMDKV RRAADPLGVD VFCAGTHPFA QWSTQQLTRS
     PHYDELIERT QWWGRQMMIW GVHVHVGVSH REKVFPILNS LLTTFPHLLA LSASSPMWAG
     SDTGYASNRT LMFQQLPTAG LPFQFENWRQ FEHFVHDELK TGVFEQLGGL HWDIRPAPKW
     GTIEVRICDG IPTHAELAAI AAFIHCLIVD LDQRIEDGEQ PITLPPWHVQ ENKWRAARYG
     LDAIVITDAD SNERLVTDDL MDLLNRLEPT AKRLGCADEL AYVATIPERG ASYQRQRKVA
     AASQGDLVAV VDALVHELDR