ID   GCS2_CHLAA              Reviewed;         390 AA.
AC   A9WAH5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=Caur_3581;
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
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; CP000909; ABY36765.1; -; Genomic_DNA.
DR   RefSeq; WP_012259418.1; NC_010175.1.
DR   RefSeq; YP_001637154.1; NC_010175.1.
DR   AlphaFoldDB; A9WAH5; -.
DR   SMR; A9WAH5; -.
DR   STRING; 324602.Caur_3581; -.
DR   EnsemblBacteria; ABY36765; ABY36765; Caur_3581.
DR   KEGG; cau:Caur_3581; -.
DR   PATRIC; fig|324602.8.peg.4032; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_0; -.
DR   InParanoid; A9WAH5; -.
DR   OMA; LIFGLHV; -.
DR   Proteomes; UP000002008; 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:0016879; F:ligase activity, forming carbon-nitrogen bonds; IBA:GO_Central.
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..390
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000337696"
SQ   SEQUENCE   390 AA;  44492 MW;  906D9DA9B6666742 CRC64;
     MSVYNPNDAD FAFTLGIEEE YQIVDPETRE LRSYITQILE PGRTILREQI KPEMHQSIVE
     VGTRPCRTIS EARAEIVRLR SAIAGLAARH NLRIVAAGTH PFSSWMQQEI TPDERYHMVV
     GEMQDAALQL LIFGMHCHIG MPNNEVAIEL MNVARYICPH LLALSTSSPF WMGRNTGFKS
     YRSVIFSTFP RTGIPPTFHS ASEFERYVQL LVNTGCIDNG KKIWWDLRPH PFFGTLEFRV
     CDIATKVEEC LALAATMQAL IVKFYTMFEE NTTFRVYRRA LINENKWRAQ RWGLDGKLID
     FGKRKEVEAK ALVHEIVELV DDVVDMLGSR REVEYLLKIV ENGTSADRQL RVFAETNDLK
     AVVDNLMVET MEGVPAMAFE ADVQSQAAHS