ID   GCS2_DECAR              Reviewed;         384 AA.
AC   Q47E74;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=Daro_2114;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC   Dechloromonas.
OX   NCBI_TaxID=159087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCB;
RX   PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA   Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA   Lapidus A.;
RT   "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT   indications of a surprisingly complex life-style and cryptic anaerobic
RT   pathways for aromatic degradation.";
RL   BMC Genomics 10:351-351(2009).
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; CP000089; AAZ46857.1; -; Genomic_DNA.
DR   RefSeq; WP_011287859.1; NC_007298.1.
DR   AlphaFoldDB; Q47E74; -.
DR   SMR; Q47E74; -.
DR   STRING; 159087.Daro_2114; -.
DR   EnsemblBacteria; AAZ46857; AAZ46857; Daro_2114.
DR   KEGG; dar:Daro_2114; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_1_4; -.
DR   OMA; HIHIGCP; -.
DR   OrthoDB; 991285at2; -.
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.
FT   CHAIN           1..384
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000255799"
SQ   SEQUENCE   384 AA;  42825 MW;  F3218EE57E4D359B CRC64;
     MTTKALGDFK DSAAFSLGVE LELQLVSKRD FDLTRGATDL LGSLDYDERF GEIKLEITES
     MIEISTQPQS TVDGIAADLS GLRDTLRQHC ERNNIGICGG GTHPFHHWPE RRICPGDRFN
     DLYQRYGYLA KQFTVFGQHV HIGCTSADEA IWLTQAFGVY VPAFIALSAS SPFVDGVDSF
     YQSARLNAVS AFPLSGQCPP LGSWQEFTEH FAFLQACGIA QSIKDLYWDV RPKPEFGTVE
     IRVCDTPLTI EQATSLAALA QSLARWLLRT RPPLHTAKQA HVARYNKFQA CRYGFEAMIS
     DPVNLCQTPL KQTLADLLEA VSEDARELDC ADWLSPLKQA VAENTGDAAW LRARENQHGN
     LNDVVREASK RLMGKNDQFQ EKTK