GCS2_SALA4
ID GCS2_SALA4 Reviewed; 372 AA.
AC B5EYH4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 62.
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 Name=ybdK; OrderedLocusNames=SeAg_B0622;
OS Salmonella agona (strain SL483).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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 -!- SUBUNIT: Homodimer. {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; CP001138; ACH49509.1; -; Genomic_DNA.
DR RefSeq; WP_001196911.1; NC_011149.1.
DR AlphaFoldDB; B5EYH4; -.
DR SMR; B5EYH4; -.
DR EnsemblBacteria; ACH49509; ACH49509; SeAg_B0622.
DR KEGG; sea:SeAg_B0622; -.
DR HOGENOM; CLU_044848_1_1_6; -.
DR OMA; LIFGLHV; -.
DR Proteomes; UP000008819; 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..372
FT /note="Putative glutamate--cysteine ligase 2"
FT /id="PRO_1000148227"
SQ SEQUENCE 372 AA; 41671 MW; E69FC95F57D3FB34 CRC64;
MALNDFHVSE PYTLGIELEM QVINPPGYDL SQDSSTLIDA VKPQLTAGEI KHDITESMLE
MATGVCRDID QAAAQLSAMQ HVILQAASEH HLGICGGGTH PFQKWQRQEV CDNERYQRTL
ENFGYLIQQA TVFGQHVHVG CANGDDAIYL LHGLSHFVPH FIALSAASPY MQGSDTRFAC
ARLNIFSAFP DNGPMPWVSN WQEFAGLFRR LSYTTMIDSI KDLHWDIRPS PAFGTVEVRV
MDTPLTLDHA INMAGLIQAT AHWLLTERPF KPQEQDYLLY KFNRFQACRY GLEGVLTDVY
TGDRRRLADD TLRLLDNVTP SARKLGADSA IDALRLQVKK GGNEAQYMRE FIADGGSLIG
LVQKHCEIWT GQ