ID   GCS2_BRASO              Reviewed;         408 AA.
AC   A4YLK4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   25-MAY-2022, entry version 70.
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=BRADO0861;
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=114615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278;
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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=CAL74780.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CU234118; CAL74780.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011924033.1; NC_009445.1.
DR   AlphaFoldDB; A4YLK4; -.
DR   SMR; A4YLK4; -.
DR   STRING; 114615.BRADO0861; -.
DR   EnsemblBacteria; CAL74780; CAL74780; BRADO0861.
DR   KEGG; bra:BRADO0861; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_0_1_5; -.
DR   OrthoDB; 991285at2; -.
DR   Proteomes; UP000001994; 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..408
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000323502"
SQ   SEQUENCE   408 AA;  45569 MW;  0B541AD12094548B CRC64;
     MDPKILERLR LGLSDDERRL VIRSATGGEE VTEYSFGIEE EYFLVDAKTL DVAIRTPDDL
     FDAANWSTGG QAMREMLQAQ LEVATNVHVD VGDAREELKF LRREVASVAG QYGLTILACS
     THPTALWRNS QPTPKPRYAE MMEDLRIVGQ RNMLCGMHVH VQLPDPDRRF AVMRAMIPYI
     PVFIALSASS PFWNSRETGL KGYRLAAYDE LPRTGLPELF TSKKQYDRYV AALTKSGVMP
     DESHVWWAMR PSLRHPTLEL RAPDVCTAVD DAVAIASLYR ALARHLYLNP ELADAVGNVE
     RAIAVENKWR AQRYGTDCLF VTEDGPVTGQ EILNRTIADV AEHAEALGCL AEVERCRTIM
     QFGSSADYQL QAYRESGGQL AAVTQWIAAA TVSRAEPPQS QPSVEPVR