ID   GCS21_RUBXD             Reviewed;         376 AA.
AC   Q1B017;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=Rxyl_0030;
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
RG   US DOE Joint Genome Institute;
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   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-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; CP000386; ABG03011.1; -; Genomic_DNA.
DR   RefSeq; WP_011563029.1; NC_008148.1.
DR   AlphaFoldDB; Q1B017; -.
DR   SMR; Q1B017; -.
DR   STRING; 266117.Rxyl_0030; -.
DR   EnsemblBacteria; ABG03011; ABG03011; Rxyl_0030.
DR   KEGG; rxy:Rxyl_0030; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_11; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   PhylomeDB; Q1B017; -.
DR   Proteomes; UP000006637; 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..376
FT                   /note="Putative glutamate--cysteine ligase 2-1"
FT                   /id="PRO_0000255811"
SQ   SEQUENCE   376 AA;  42005 MW;  21C9115C3ED417DB CRC64;
     MPVEFKLGNS GYTLGVEEEL CIVDASTGEL VPKIEEIMSR LPEDLAEAVS YELFQSVLEI
     KTPVCRTVGE AERVLRELRG RVGSWTAACG ASLASAGTHP FSRYRDQKVT EHERYRQVIE
     ELRWVATREV IFGQHVHVAV PGPEEAIQAH NRLAEQAPLL LALSANSPYW QGMDTGFESS
     RVQIFETFPR AGMPPAFPEY AAFEAYVDLM VECGAMDDYT FCWWDVRPHP KLGTIELRVL
     DSQTHLRHAV ALTALTQCIV ASSLEDEDAP KGPYHRDIAL ENKWRASRRG LDAAFFDVDE
     RRNVPARDLA RAAVERLRPH AQQLGCEEEL LGVLEIVEGG SGSRRQREIY EKSGDFLDVV
     AFLIEGTRPA LAGEPS