ID   GCS21_PAEAT             Reviewed;         384 AA.
AC   A1R1K8;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=AAur_0300;
OS   Paenarthrobacter aurescens (strain TC1).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX   NCBI_TaxID=290340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1;
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA   Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT   aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(2006).
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; CP000474; ABM09426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1R1K8; -.
DR   SMR; A1R1K8; -.
DR   STRING; 290340.AAur_0300; -.
DR   EnsemblBacteria; ABM09426; ABM09426; AAur_0300.
DR   KEGG; aau:AAur_0300; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_11; -.
DR   OMA; WQRWPSA; -.
DR   Proteomes; UP000000637; 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..384
FT                   /note="Putative glutamate--cysteine ligase 2-1"
FT                   /id="PRO_0000291481"
SQ   SEQUENCE   384 AA;  41450 MW;  7C6521C3C56CAB76 CRC64;
     MGRVAVRTFG VEEELLIADP VDGMPLALAS GILDVAGFSE TDNSSDAGPS LKSEFKQEQI
     EVNSLPCRTA KELRAEIRAG RALADSAARA VGARVAALAT PPVFHATPTA GNQRYAAMGT
     EFGLISREQL TCGFHVHVSI ESPEEGVAVL DRMRHWLPVL LALSANSPFW MGADTGFASY
     RTQIWNRWPT AGPMDVFGSA DGYRQVLSEL LGTGVPLDEG MIYFDARLSR GHPTVEVRIA
     DVCLYAEDAL TIAILARALV ETSASEWRKG EPPSGVMTPV IRMANWKASR FGVTNQLLHP
     LEQAPFAAAD VAGALLRHIR RALTESGDLA LARTGVANIL RRGTGERLQR QAYGRRFRLS
     DVVSTAIAST HNYGERSDAG LLSR