ID   GCS2_TRIV2              Reviewed;         387 AA.
AC   Q3M5M3;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=Ava_4113;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA23713.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3M5M3; -.
DR   SMR; Q3M5M3; -.
DR   STRING; 240292.Ava_4113; -.
DR   EnsemblBacteria; ABA23713; ABA23713; Ava_4113.
DR   KEGG; ava:Ava_4113; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_1_3; -.
DR   OMA; LIFGLHV; -.
DR   Proteomes; UP000002533; 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..387
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000291480"
SQ   SEQUENCE   387 AA;  43689 MW;  D106D79574641D3A CRC64;
     MGDIEFKSSP EFSLGMEIEL QLLNPDTLQL VDGISPLLAQ TPENSWIQPE FNQAMVEIAS
     QVCSNIPELE ANIVAILRDL KTRCQALGMT ICTAGTYPCC DRFASITPIP RYLSQQNTSG
     YLADLMMTCA LQLHVGMPSG DVAIDIMGRL KPYLPILLAL SASSPFWWGH DTSFASFRQR
     FLSSMRTYGI CPTFKNWQDF TNFFATAQNA GMFEIIRDIH WDLRPQPDFG TLEVRVMDAQ
     PTIKESMMLA AFIHSLIVDM YHHSQGKQTE FLLTPLPWLI ERENYFRASR WGLDANYIED
     EQGNSRPIRN IVKDILNVLA ETADTLGNSS YLFQLEKRLD QGASYIRQRR VFESTGSVKA
     VVASLVSELE AELAIKSRQE AVAYGWL