ID   GCS2_PSEF5              Reviewed;         387 AA.
AC   Q4K7H5;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=PFL_4726;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY93957.1; -; Genomic_DNA.
DR   RefSeq; WP_011062983.1; NC_004129.6.
DR   AlphaFoldDB; Q4K7H5; -.
DR   SMR; Q4K7H5; -.
DR   STRING; 220664.PFL_4726; -.
DR   EnsemblBacteria; AAY93957; AAY93957; PFL_4726.
DR   KEGG; pfl:PFL_4726; -.
DR   PATRIC; fig|220664.5.peg.4835; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_1_6; -.
DR   OMA; LIFGLHV; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000008540; 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; Reference proteome.
FT   CHAIN           1..387
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000291510"
SQ   SEQUENCE   387 AA;  43199 MW;  0F7E38A2F8EC8DB3 CRC64;
     MSAFDPGQPQ HLGIEEEYLL TDLQSRCMVA EPPPEVLRDC REALGQNFAY EMFQGQIEVA
     SPVFDHSAQA GAYLRQVRSA LDQALASHGL GFICAGSHPL ADWHEQRATP QAHFRQLFNE
     FALAARRSVL SGLHVHAQVP AAVDRIAVMN EVLPWTPLLL ALSLSSPFWQ GHDSGYLSYR
     QVACDEWPRM GIPEYLHDHQ AFDDYLRLLR GIGALGAEDN AWWGIRPALR YPTLELRMTD
     ACPRVADAQT LAGLFAVMVR HACLLPAAGS QYTQAQRWLL KENRVQARRR GAQGRYLMSP
     DQAPMNLGQW LELAEQVFGD TAQALGEEPL FERARQLLRG GCSAERQLSC HAAQPAESDR
     EARCRAVVDL LLWESRDSEP ESTNAPP