ID   GCS2_ROSS1              Reviewed;         379 AA.
AC   A5UWI8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Putative glutamate--cysteine ligase 2 {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 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=RoseRS_2615;
OS   Roseiflexus sp. (strain RS-1).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=357808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-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   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Roseiflexus sp. RS-1.";
RL   Submitted (APR-2007) 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; CP000686; ABQ90991.1; -; Genomic_DNA.
DR   RefSeq; WP_011957335.1; NC_009523.1.
DR   AlphaFoldDB; A5UWI8; -.
DR   SMR; A5UWI8; -.
DR   STRING; 357808.RoseRS_2615; -.
DR   PRIDE; A5UWI8; -.
DR   EnsemblBacteria; ABQ90991; ABQ90991; RoseRS_2615.
DR   KEGG; rrs:RoseRS_2615; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_0; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000006554; 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..379
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000337702"
SQ   SEQUENCE   379 AA;  43187 MW;  2CCF0B29690B09A2 CRC64;
     MTSYNPASPD FPFTLGIEEE YQVVDPQTRE LRSYITQILD RGKMILREQI KPELHQSMVE
     VGTHPCRTIQ EARAEVVRLR SIIAGLARQH GLTIISAGTH PISSWMSQEI TPFERYKGVV
     EEMQQLALQL LIFGMHVHVG MPDDEVAIEL MNVARYFLPH ILALSTSSPF WMGRNTGFKS
     YRSALFANFP RTGIPPSFHS AAEFHNYVNL LIRTNCIDDA KKIYWDLRPH PYFGTLEFRV
     CDAATRVDEC IALAALMQAL TVKLHLMFSE NTTFRVYRRA VIMENKWRAQ RWGLDGKLID
     FGKRAEVDAR ALMYELVAFV DEVLDELGSR QEVEYLLKIA EGGSSADRQL AVFRETNDLN
     AVVDNLIVET LEGVPAYQA