ID   GCS2_BRADU              Reviewed;         426 AA.
AC   Q89NS0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   25-MAY-2022, entry version 85.
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=bll3764;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC49029.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000040; BAC49029.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_770404.1; NC_004463.1.
DR   AlphaFoldDB; Q89NS0; -.
DR   SMR; Q89NS0; -.
DR   STRING; 224911.27352024; -.
DR   EnsemblBacteria; BAC49029; BAC49029; BAC49029.
DR   KEGG; bja:bll3764; -.
DR   PATRIC; fig|224911.5.peg.3753; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_5; -.
DR   InParanoid; Q89NS0; -.
DR   OMA; HIHIGCP; -.
DR   Proteomes; UP000002526; 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..426
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000218188"
SQ   SEQUENCE   426 AA;  48097 MW;  2DC4D37D692D562C CRC64;
     MLRLDSSDDK QHLVIRSAGG RGKAAEYSFG IEEEYFLADR RSLDVAIQTP NELFESANWS
     TGGQAMREML QSQLEVATNV HVDVNDAREE LRFLRREVAN VAAQYGFVIM ACGTHPTAVW
     RMSQPSPKPR YEEMIEDLRS IGHRNMMCGM HVHVQLPDPE KRMAVMRAML PHLPLFIALS
     ASSPFWNSHK TGLKGYRLAA YSELPRTGLP ELFESRHDYD EYVGALQRSG VIPDESHIWW
     AMRPSMKHPT LELRAPDTCT FVDDAVAIAS LYRCLTRHLY RRPHLSKTVT VVERAIAVEN
     KWRAQRYGTD CIFASKDGPI TISELLSRLI DDIVEDADAL NCAAEVEHCR TIVERGSSAE
     FQLRAYRENG NDIAAVSRWI AASTISGRAL RSDAPRLRRH SARASFGNDN GIPEFAVSRA
     VSWRKA