ID   GCS22_FRACC             Reviewed;         861 AA.
AC   Q2J8X3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Putative glutamate--cysteine ligase 2-2;
DE            EC=6.3.2.2;
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2-2;
DE            Short=GCS 2-2;
DE            Short=Gamma-GCS 2-2;
GN   OrderedLocusNames=Francci3_2911;
OS   Frankia casuarinae (strain DSM 45818 / CECT 9043 / CcI3).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=106370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45818 / CECT 9043 / CcI3;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
CC   -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC       glutamate--cysteine ligase activity. {ECO:0000250}.
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   -!- SIMILARITY: In the N-terminal section; belongs to the glutamate--
CC       cysteine ligase type 2 family. YbdK subfamily. {ECO:0000305}.
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DR   EMBL; CP000249; ABD12269.1; -; Genomic_DNA.
DR   RefSeq; WP_011437298.1; NZ_LRTJ01000017.1.
DR   AlphaFoldDB; Q2J8X3; -.
DR   SMR; Q2J8X3; -.
DR   STRING; 106370.Francci3_2911; -.
DR   EnsemblBacteria; ABD12269; ABD12269; Francci3_2911.
DR   KEGG; fra:Francci3_2911; -.
DR   eggNOG; COG2170; Bacteria.
DR   eggNOG; COG2308; Bacteria.
DR   HOGENOM; CLU_017048_0_0_11; -.
DR   OMA; DSAWFEH; -.
DR   OrthoDB; 991285at2; -.
DR   PhylomeDB; Q2J8X3; -.
DR   Proteomes; UP000001937; 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; IPR025841; CP_ATPgrasp_2.
DR   InterPro; IPR006336; GCS2.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR011793; YbdK.
DR   Pfam; PF14403; CP_ATPgrasp_2; 1.
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..861
FT                   /note="Putative glutamate--cysteine ligase 2-2"
FT                   /id="PRO_0000323508"
FT   REGION          1..372
FT                   /note="Carboxylate-amine ligase"
FT   REGION          373..861
FT                   /note="Unknown"
SQ   SEQUENCE   861 AA;  93068 MW;  3B17BAF2A66E8C2F CRC64;
     MSDARIVAVG VEEEFHILDL TTRQLVPRAE EVLRRLDGDS FSPELLKSVV ETNSQPTADL
     LELRTNLLDL RRRLAEVTGE LGLGPAAAGT VPIVDMDLLD VSRDDRYEQM TEDYQIVARE
     QLICGAQVHV DVADRDLAMA VVAWTAPWLP MLLALSASSP FWMGADSGYA SMRTLVWQRW
     PTAGVAGSFR TAAEYDQLVA DLIKSGVISD PGMVYFDVRP SAHLPTVELR ICDACPDVDN
     VILIAGLFRA LVCQAIEEIE AGGQAPPPRA ELLRAATWRA ARSGLEGDLV DILGAGPIPA
     QAMLRRLLTE VRPQLERFDD WELIDNLAEQ AVGRGSSAHR QRRAFARRGL LTDVADLVLA
     ETRDVPPAGA AAALGSAPAV SASDQIAPRL LERYQPTGYD EIVDARGAVR PQYRAVMRTL
     ERLGPGILDE RVGTREAEQN DRGIVFRASG DSASRPFPFD LVPRIIAADD WTTLTTGLSQ
     RVRALEAFLH DIYGERAAVA DGIVPAWVVN DAPSLRHGGR AVGPDAIRVT VAGIDLVRGG
     DGGWLVLEDN LRVPSGIAYA MEGRRLAESV LPELGPPAGI LRLDGIPALL HEALVAAAPA
     AATGDPAVAV LTGGKTDAAY FEHSLLAEKM GVALVEPADL LVDDNDVVYR IDGSRRCRVD
     VLYRRMDEDD LFGALGAAGT PLGLPLLRAI RARRVGIANA LGNGVGDDKV VYAYVPRMVT
     YYLGEQPVLD DVPTYVCGDP EQCEHVLDNL DQLVVKPVDG YGGSGVVIGP HAEPYRLTEV
     RERILANPRQ WIGQELVSLS THPTWHDSHL EPCAVDLRVF VYAGREPRVV PAALSRVAPP
     GSLIVNSSQG GGSKDTWIPR R