ID   GCS23_RUBXD             Reviewed;         363 AA.
AC   Q1AWB5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2-3 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=Rxyl_1350;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000386; ABG04313.1; -; Genomic_DNA.
DR   RefSeq; WP_011564330.1; NC_008148.1.
DR   AlphaFoldDB; Q1AWB5; -.
DR   SMR; Q1AWB5; -.
DR   STRING; 266117.Rxyl_1350; -.
DR   EnsemblBacteria; ABG04313; ABG04313; Rxyl_1350.
DR   KEGG; rxy:Rxyl_1350; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_11; -.
DR   OMA; WWELRPH; -.
DR   OrthoDB; 991285at2; -.
DR   PhylomeDB; Q1AWB5; -.
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..363
FT                   /note="Putative glutamate--cysteine ligase 2-3"
FT                   /id="PRO_0000255812"
SQ   SEQUENCE   363 AA;  39643 MW;  28687903356DD3F5 CRC64;
     METRFGASPP YTVGVEEEFQ LIDPRTRALT PKIEEVLAAG DGELPEGTLA SELSASCLEV
     RTPAYASVAE LARALPALRA RVRRLAERSG ARLVSAGAHP FSPAAEQPIT GKPRYRKVDE
     EMGWPARMQA IYGLHVHVAV PGGEEAVRAV SALARHVPLF IALSANSPFW EGRDTRLASV
     RAKVFGLIPR SGLPPRFASW EEFVRHVERL VRAGSIRDYT FCWWDVRPHP KLGTVELRAP
     DAQTDPGRTA ALAALCQCLA AAAEEFEPED PLLTEENKWR ATRHGLEAEL YDFSGQRTVA
     ARRAAEELVG RLLPVARELG CEAELEGVLE ISRSATGADR QRAVLAREGS LKSVVDYLAE
     ATA