GCS2_SALTY
ID GCS2_SALTY Reviewed; 372 AA.
AC Q8ZR41;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=STM0583;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL19534.1; -; Genomic_DNA.
DR RefSeq; NP_459575.1; NC_003197.2.
DR RefSeq; WP_001196903.1; NC_003197.2.
DR PDB; 1TT4; X-ray; 2.80 A; A/B=1-372.
DR PDBsum; 1TT4; -.
DR AlphaFoldDB; Q8ZR41; -.
DR SMR; Q8ZR41; -.
DR STRING; 99287.STM0583; -.
DR PaxDb; Q8ZR41; -.
DR EnsemblBacteria; AAL19534; AAL19534; STM0583.
DR GeneID; 1252103; -.
DR KEGG; stm:STM0583; -.
DR PATRIC; fig|99287.12.peg.615; -.
DR HOGENOM; CLU_044848_1_1_6; -.
DR OMA; LIFGLHV; -.
DR PhylomeDB; Q8ZR41; -.
DR BioCyc; SENT99287:STM0583-MON; -.
DR EvolutionaryTrace; Q8ZR41; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..372
FT /note="Putative glutamate--cysteine ligase 2"
FT /id="PRO_0000218217"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:1TT4"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 37..41
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:1TT4"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1TT4"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1TT4"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 69..89
FT /evidence="ECO:0007829|PDB:1TT4"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:1TT4"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:1TT4"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:1TT4"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1TT4"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1TT4"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:1TT4"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 247..267
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 274..279
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:1TT4"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:1TT4"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:1TT4"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 319..325
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 328..339
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:1TT4"
FT HELIX 358..368
FT /evidence="ECO:0007829|PDB:1TT4"
SQ SEQUENCE 372 AA; 41597 MW; B448A5897F5CA496 CRC64;
MALNDFHVSE PYTLGIELEM QVINPPGYDL SQDSSTLIDA VKPQLTAGEI KHDITESMLE
MATGVCRDID QAAAQLSAMQ HVILQAASEH HLGICGGGTH PFQKWQRQEV CDNERYQRTL
ENFGYLIQQA TVFGQHVHVG CANGDDAIYL LHGLSHFVPH FIALSAASPY MQGADTRFAC
ARLNIFSAFP DNGPMPWVSN WQEFAGLFRR LSYTTMIDSI KDLHWDIRPS PAFGTVEVRV
MDTPLTLDHA INMAGLIQAT AHWLLTERPF KPQEQDYLLY KFNRFQACRY GLEGVLTDAY
TGDRRRLADD TLRLLDNVTP SARKLGADSA IDALRLQVKK GGNEAQYMRE FIADGGSLIG
LVQKHCEIWA GQ
