GCS2_BRASB
ID GCS2_BRASB Reviewed; 408 AA.
AC A5ESE1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 25-MAY-2022, entry version 67.
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=BBta_7205;
OS Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX NCBI_TaxID=288000;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTAi1 / ATCC BAA-1182;
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=ABQ39085.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000494; ABQ39085.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_012047011.1; NC_009485.1.
DR AlphaFoldDB; A5ESE1; -.
DR SMR; A5ESE1; -.
DR STRING; 288000.BBta_7205; -.
DR EnsemblBacteria; ABQ39085; ABQ39085; BBta_7205.
DR KEGG; bbt:BBta_7205; -.
DR eggNOG; COG2170; Bacteria.
DR HOGENOM; CLU_044848_1_0_5; -.
DR OrthoDB; 991285at2; -.
DR Proteomes; UP000000246; 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.
FT CHAIN 1..408
FT /note="Putative glutamate--cysteine ligase 2"
FT /id="PRO_0000323501"
SQ SEQUENCE 408 AA; 45894 MW; CA0D56A8498DDD38 CRC64;
MDPRILERLR LGLSDDERRL VIRSATGGED VTEYSFGIEE EYFLADARTL DVAIRTPDDL
FEAANWSTGG QAMREMLQAQ IEVATNVHVD SRDAREELKF LRREVASVAG QYGLTILACS
THPTAMWRSS QPTPRPRYAE MMEDLRIVGQ RNMLCGMHVH VQLPDSERRF AVMRAMIPYI
PVFIALSASS PFWNSRETGL KGYRLAAYDE LPRTGLPELF TSKPEYDRYV AALTRSGVMP
DESHVWWAMR PSLRHPTLEL RAPDVCTSVD DAVAVASLYR ALARHLYLHP DLADAVGNVE
RAIAVENKWR AQRYGTDCLF VAEEGPVTGQ EILNRMIADI APHAEALDCL AEVERCRTIM
QFGSSADYQL QAYRESGGEL SAVLRWIEVA TVSRSDPPRT HAPVEPAQ
