GCS2_SALG2
ID GCS2_SALG2 Reviewed; 372 AA.
AC B5R705;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
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 Name=ybdK; OrderedLocusNames=SG0587;
OS Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=550538;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=287/91 / NCTC 13346;
RX PubMed=18583645; DOI=10.1101/gr.077404.108;
RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT gallinarum 287/91 provides insights into evolutionary and host adaptation
RT pathways.";
RL Genome Res. 18:1624-1637(2008).
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; AM933173; CAR36483.1; -; Genomic_DNA.
DR RefSeq; WP_001196920.1; NC_011274.1.
DR AlphaFoldDB; B5R705; -.
DR SMR; B5R705; -.
DR EnsemblBacteria; CAR36483; CAR36483; SG0587.
DR KEGG; seg:SG0587; -.
DR HOGENOM; CLU_044848_1_1_6; -.
DR OMA; LIFGLHV; -.
DR Proteomes; UP000008321; 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_1000148230"
SQ SEQUENCE 372 AA; 41670 MW; D41011E580DD4A1F CRC64;
MALNDFHVSE PYTLGIELEM QVINPPSYDL SQDSSTLIDA VKPQLTAGEI KHDITESMLE
MATGVCRDID QAAAQLSAMQ HVILQAASEH HLGICGGGTH PFQKWQRQEV CDNERYQRTL
ENFGYLIQQA TVFGQHVHVG CANGDDAIYL LHGLSHFVPH FIALSAASPY MQGSDTRFAC
ARLNIFSAFP DNGPMPWVSN WQEFAGLFRR LSYTTMIDSI KDLHWDIRPN PAFGTVEVRV
MDTPLTLDHA INMAGLIQAT AHWLLTERPF KPQEQDYLLY KFNRFQACRY GLEGVITDAY
TGDRRRLADD TLRLLDNVTP SARKLGADSA IDALRLQVKK GGNEAQYMRE FIADGGSLIG
LVQKHCEIWA GQ