ID   GCS22_NOCSJ             Reviewed;         369 AA.
AC   A1SLX8;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Noca_3311;
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; ABL82813.1; -; Genomic_DNA.
DR   RefSeq; WP_011756747.1; NC_008699.1.
DR   AlphaFoldDB; A1SLX8; -.
DR   SMR; A1SLX8; -.
DR   STRING; 196162.Noca_3311; -.
DR   PRIDE; A1SLX8; -.
DR   EnsemblBacteria; ABL82813; ABL82813; Noca_3311.
DR   KEGG; nca:Noca_3311; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   OMA; WQRWPSA; -.
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..369
FT                   /note="Putative glutamate--cysteine ligase 2-2"
FT                   /id="PRO_0000291504"
SQ   SEQUENCE   369 AA;  39404 MW;  43F0D97D2B037612 CRC64;
     MRTVGVEEEF LLVDADRSRP IPAASRALRV ATEWGVAGGQ VGAGALVHEL QEQQLEIYTA
     PQVRMASLET ELRAWRAAAA AAAAAVGARL VASATSPVAV EPHRVRSPRY DRMAERFGIV
     TDEQLTCGCH VHVAVGSTAE AVGVLDRIRV WLPALLALSA NSPFWQGRDT GYASFRIQAL
     GRWPLSGPTE LFGTAAAYQE LVERVLAAQV VLDQGMLYFD ARASHRFPTV EIRVADVCLD
     VRDTVLIAAL CRALVETSAA RWAAGEAPPQ VPAVLLRLAT WHASRWGVSA DLLDPMTARP
     LPAAEVVGRL VEHARPALRR SGDDGLVADG IARILEHGNG ATWQRDVFAG SGRLDEVVSA
     LALVTSGGA