ID   GCS23_RHOJR             Reviewed;         793 AA.
AC   Q0S8V5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-3;
DE            EC=6.3.2.2;
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-3;
DE            Short=GCS 2-3;
DE            Short=Gamma-GCS 2-3;
GN   OrderedLocusNames=RHA1_ro04240;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC   -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC       glutamate--cysteine ligase activity. {ECO:0000250}.
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   -!- SIMILARITY: In the C-terminal section; belongs to the glutamate--
CC       cysteine ligase type 2 family. YbdK subfamily. {ECO:0000305}.
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DR   EMBL; CP000431; ABG96031.1; -; Genomic_DNA.
DR   RefSeq; WP_011596695.1; NC_008268.1.
DR   AlphaFoldDB; Q0S8V5; -.
DR   SMR; Q0S8V5; -.
DR   STRING; 101510.RHA1_ro04240; -.
DR   EnsemblBacteria; ABG96031; ABG96031; RHA1_ro04240.
DR   KEGG; rha:RHA1_ro04240; -.
DR   PATRIC; fig|101510.16.peg.4267; -.
DR   eggNOG; COG1473; Bacteria.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_019405_0_0_11; -.
DR   OMA; TWTESTE; -.
DR   Proteomes; UP000008710; 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:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR006336; GCS2.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011793; YbdK.
DR   PANTHER; PTHR11014; PTHR11014; 1.
DR   Pfam; PF04107; GCS2; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR01891; amidohydrolases; 1.
DR   TIGRFAMs; TIGR02050; gshA_cyan_rel; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..793
FT                   /note="Putative glutamate--cysteine ligase 2-3"
FT                   /id="PRO_0000323510"
FT   REGION          1..407
FT                   /note="Carboxylate-amine ligase"
FT   REGION          367..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..793
FT                   /note="Peptidase M20"
SQ   SEQUENCE   793 AA;  85751 MW;  769EE190DCDCDB59 CRC64;
     MLASDPRKVG VEEEFHLIDL KTRRLTTRAP ELLARLPDDV YVDELQQCVV EVNSGVYADL
     DGLRSDLERH RRLLVDAAED LGIGVAAAGS VPLALPAEMH VTGTQRYGRM LADYQVLARE
     QLICGTQVHV DLPDRDEAVQ VAHRVAPHMP VLLALSASSP FRSDGADTGY ASARTLLWLR
     WPSTGPAAPV SSAAEYGALI DDLVASGVIS DPGMAYFDVR PSVKLPTLEL RVCDSCPRLD
     TVLLVAALFR ALVEREVEGL RAGRKGVEVL PTLTRAALWR AARSGLEEEL VDVTVPQARP
     ASELVGDFVN SLRPQLEETG DWDRVVELSA EATAHGSSAA RQRQALGRRG RLTDVVDLLL
     AETAGRTEHL PDVEVPPPRE PGPKSTGAGR TRRYWSARFW DRGDTADMTW TESTELDEKK
     LVEWRRDLHA HPELSFEERR TTGVVRDHLV GLGLEPVLMP GGTGLWCDVG PETGECIALR
     ADLDALPVAE TTGLPFESRV PGVSHACGHD AHTTMLMGAA SVLTKYPPPT RVRLVFQPAE
     ETTPGGAVDT IAAGALDGVS KIFALHCDPH LEVGKLSTRT GPITSSNDSV TVRLWSAGGH
     TARPHLTGDL IHATAVLVTG LASVLDRRID ARTATVLTWG KVAAGQVANS VPESGELVGT
     LRSASRETWA SLEPLVTDAI CHLLAPYNVR YELSYLRGVP PVVNDPDCTA DLREAIESVV
     GFDHLAEAHQ SSGGEDFAWY LEKVPGAMAR LGVWDGTGTR QELHQPGFNL DERAMIHGVR
     TLVALTRLED QSG