ID   GCS2_CHLAD              Reviewed;         390 AA.
AC   B8GCV1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
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=Cagg_0203;
OS   Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=326427;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-66 / DSM 9485;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL   Submitted (DEC-2008) 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; CP001337; ACL23151.1; -; Genomic_DNA.
DR   RefSeq; WP_012615517.1; NC_011831.1.
DR   AlphaFoldDB; B8GCV1; -.
DR   SMR; B8GCV1; -.
DR   STRING; 326427.Cagg_0203; -.
DR   EnsemblBacteria; ACL23151; ACL23151; Cagg_0203.
DR   KEGG; cag:Cagg_0203; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_0; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000002508; 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.
FT   CHAIN           1..390
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_1000185844"
SQ   SEQUENCE   390 AA;  44501 MW;  C2CF22A9D4A96C6A CRC64;
     MSVYNPNDAD FAFTIGIEEE YQIVDPETRE LRSYITQILE PGRTILREQI KPEMHQSIVE
     VGTRPCRTIS EARAEIVRLR GAIAGLAARH NLRIVAAGTH PFSSWMQQEI TPDERYRMVV
     GEMQEAALQL LIFGMHCHIG MPNNEVAIEL MNVARYICPH LLALSTSSPF WMGRNTGFKS
     YRSVIFSTFP RTGIPPTFHS ASEFERYVQL LINTGCIDNG KKIWWDLRPH PFFGTLEFRV
     CDIATKVEEC LALAATMQAL IVKFYTMFEE NTTFRVYRRA LINENKWRAQ RWGLDGKLID
     FGKRKEVEAK ALVHEIVELV DDVVDMLGSR KEVEYLLTIV DQGTSADRQL RVFAETNDLK
     AVVDSLMNET IEGVPVMTFD TESSVQTAHS