ID   GCS24_RHOJR             Reviewed;         385 AA.
AC   Q0RZ64;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-4 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-4 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-4 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-4 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=RHA1_ro08378;
OS   Rhodococcus jostii (strain RHA1).
OG   Plasmid pRHL1.
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: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; CP000432; ABG99422.1; -; Genomic_DNA.
DR   RefSeq; WP_007300000.1; NC_008269.1.
DR   AlphaFoldDB; Q0RZ64; -.
DR   SMR; Q0RZ64; -.
DR   EnsemblBacteria; ABG99422; ABG99422; RHA1_ro08378.
DR   KEGG; rha:RHA1_ro08378; -.
DR   HOGENOM; CLU_044848_0_0_11; -.
DR   OMA; HIHIGCP; -.
DR   Proteomes; UP000008710; Plasmid pRHL1.
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; Plasmid; Reference proteome.
FT   CHAIN           1..385
FT                   /note="Putative glutamate--cysteine ligase 2-4"
FT                   /id="PRO_0000291512"
SQ   SEQUENCE   385 AA;  41527 MW;  E36B03C8E4D5927B CRC64;
     MATTTVPTKP RRDEIPTLGV EEEFVLVDPH TGRPSLSNTD VIASGRELGI TLQPELSRCQ
     IETATSIGTH IRDLRDQLCE SRAVTADAAA RTGCQLLAVG TPMYSPPHDS ITDTPRHRRI
     AEQFGALATG VMCGCHVHVG VPGREQAIQI INHLRPWLPT LLALTANSPI ADGCDTGYAS
     WRYILFGHWP SAGPPPYFDS AAHYDAALAK MLESGAILDN RMVFWDVRAA DHPPTVEVRI
     SDVPATVEET MTLTTLVHAL VITAADAIER GTPAPTVDHE ALRGACWRAA RDGLSGHGFD
     LTTMGLIPAP RLIYQLLTHV KPVLVELGEC GQVTGSLAAV LEHGNGAIRQ RRTLARHGRV
     ADVIAECARR TFEGCLTEPD DALPL