ID   GCS2_GLOVI              Reviewed;         372 AA.
AC   Q7NI89;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=gll2294;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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; BA000045; BAC90235.1; -; Genomic_DNA.
DR   RefSeq; NP_925240.1; NC_005125.1.
DR   RefSeq; WP_011142291.1; NC_005125.1.
DR   AlphaFoldDB; Q7NI89; -.
DR   SMR; Q7NI89; -.
DR   STRING; 251221.35212862; -.
DR   EnsemblBacteria; BAC90235; BAC90235; BAC90235.
DR   KEGG; gvi:gll2294; -.
DR   PATRIC; fig|251221.4.peg.2329; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_3; -.
DR   InParanoid; Q7NI89; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   PhylomeDB; Q7NI89; -.
DR   Proteomes; UP000000557; 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..372
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000218199"
SQ   SEQUENCE   372 AA;  41518 MW;  1C3B685D3FB2BB01 CRC64;
     MTIPFQSSTA PTLGVEMELQ IIDPATGNLT PRGPELVTFC EEHPEVGLVV KPELVQATIE
     INTGICKDVA QVERDLTTQL TLLRSVCRER GVSFLSAGTH PFARWRERRY TQTPRYRALV
     DKHVWTARRM QIYGLHVHVG MPDGDTAIQV INQITQYAPM LLALSANSPF WEGDDTGLDS
     CRTKVFENLS SAGLPFRFEN WEGYENLINV LLETGSIGSQ REIWWDIRPH SDFGTIEVRI
     CDATRTLAEV LALTALVQCL AVYFRRLYEN GEEIRLLHPG IIRENKWRAC RWGLEGELID
     PLTLKGVPTR KLIEQTVGEM QSLAAELGCS AYLAAIPAIL ASGNGATRQR RIYSQSRSLV
     AVVADLEAGL AT