ID   GCS2_PSEMY              Reviewed;         378 AA.
AC   A4XUP3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=Pmen_2301;
OS   Pseudomonas mendocina (strain ymp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=399739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ymp;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Hersman L., Dubois J., Maurice P., Richardson P.;
RT   "Complete sequence of Pseudomonas mendocina ymp.";
RL   Submitted (APR-2007) 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; CP000680; ABP85059.1; -; Genomic_DNA.
DR   RefSeq; WP_012018646.1; NC_009439.1.
DR   AlphaFoldDB; A4XUP3; -.
DR   SMR; A4XUP3; -.
DR   STRING; 399739.Pmen_2301; -.
DR   PRIDE; A4XUP3; -.
DR   EnsemblBacteria; ABP85059; ABP85059; Pmen_2301.
DR   KEGG; pmy:Pmen_2301; -.
DR   PATRIC; fig|399739.8.peg.2323; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_1_6; -.
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..378
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000337700"
SQ   SEQUENCE   378 AA;  42893 MW;  1E10D65229D8C387 CRC64;
     MTQSTFGIEE EYFLTDLTSR QVARRNVEAF ATACQYELGE RVTREMFAAQ FEVVTPVLHS
     LTDARQCLEG ARRALARLAR EFDCGVLAAG THPLGQWRRV RATDMPRYRA IFDDYRMVAS
     RSVLAGLHVH VGVAEGVDRI RLMNRLTPWL PLLLGLSASS PFWNGRPSGL MSYRQAVCDE
     WPRMGIPDHF ADEAEYQRYV QVMTDTGCIR SAANLWWNIR PSLRYPTLEL RIADACPRLD
     DALCLAGLFR AMVEHVQLTP HHAWCDDPLT RVLTLENRWR AKRQGLRGLF IEPASQRLLT
     FATWLEEVLE RIAIQVPASD RWILEHARNL ALHGGSAEAQ LAEYRGARAN GLEHGEALHQ
     VVDSLMAQTE LHPSQQLA