GSH1_ECOLI
ID GSH1_ECOLI Reviewed; 518 AA.
AC P0A6W9; P06980; P78228;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glutamate--cysteine ligase;
DE EC=6.3.2.2;
DE AltName: Full=Gamma-ECS;
DE Short=GCS;
DE AltName: Full=Gamma-glutamylcysteine synthetase;
GN Name=gshA; Synonyms=gsh-I; OrderedLocusNames=b2688, JW2663;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B;
RX PubMed=2872655; DOI=10.1093/nar/14.11.4393;
RA Watanabe K., Yamano Y., Murata K., Kimura A.;
RT "The nucleotide sequence of the gene for gamma-glutamylcysteine synthetase
RT of Escherichia coli.";
RL Nucleic Acids Res. 14:4393-4400(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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 -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family.
CC Type 1 subfamily. {ECO:0000305}.
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DR EMBL; X03954; CAA27583.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75735.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16555.1; -; Genomic_DNA.
DR PIR; A65049; SYECEC.
DR RefSeq; NP_417173.1; NC_000913.3.
DR RefSeq; WP_000611804.1; NZ_LN832404.1.
DR PDB; 1V4G; X-ray; 2.50 A; A/B/C/D=1-518.
DR PDB; 1VA6; X-ray; 2.10 A; A/B=1-518.
DR PDB; 2D32; X-ray; 2.40 A; A/B/C/D=1-518.
DR PDB; 2D33; X-ray; 2.60 A; A/B/C/D=1-518.
DR PDBsum; 1V4G; -.
DR PDBsum; 1VA6; -.
DR PDBsum; 2D32; -.
DR PDBsum; 2D33; -.
DR AlphaFoldDB; P0A6W9; -.
DR SMR; P0A6W9; -.
DR BioGRID; 4262271; 16.
DR BioGRID; 849281; 2.
DR DIP; DIP-48212N; -.
DR IntAct; P0A6W9; 5.
DR STRING; 511145.b2688; -.
DR DrugBank; DB04464; N-Formylmethionine.
DR jPOST; P0A6W9; -.
DR PaxDb; P0A6W9; -.
DR PRIDE; P0A6W9; -.
DR DNASU; 944881; -.
DR EnsemblBacteria; AAC75735; AAC75735; b2688.
DR EnsemblBacteria; BAA16555; BAA16555; BAA16555.
DR GeneID; 944881; -.
DR KEGG; ecj:JW2663; -.
DR KEGG; eco:b2688; -.
DR PATRIC; fig|1411691.4.peg.4051; -.
DR EchoBASE; EB0413; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR InParanoid; P0A6W9; -.
DR OMA; RYSWLLM; -.
DR PhylomeDB; P0A6W9; -.
DR BioCyc; EcoCyc:GLUTCYSLIG-MON; -.
DR BioCyc; MetaCyc:GLUTCYSLIG-MON; -.
DR BRENDA; 6.3.2.2; 2026.
DR SABIO-RK; P0A6W9; -.
DR UniPathway; UPA00142; UER00209.
DR EvolutionaryTrace; P0A6W9; -.
DR PRO; PR:P0A6W9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IMP:EcoCyc.
DR GO; GO:0071288; P:cellular response to mercury ion; IMP:EcoCyc.
DR GO; GO:0006750; P:glutathione biosynthetic process; IMP:EcoCyc.
DR GO; GO:0006972; P:hyperosmotic response; IMP:EcoCyc.
DR HAMAP; MF_00578; Glu_cys_ligase; 1.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR007370; Glu_cys_ligase.
DR InterPro; IPR006334; Glut_cys_ligase.
DR PANTHER; PTHR38761; PTHR38761; 1.
DR Pfam; PF04262; Glu_cys_ligase; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR01434; glu_cys_ligase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glutathione biosynthesis; Ligase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..518
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_0000192524"
FT CONFLICT 100
FT /note="W -> L (in Ref. 1; CAA27583)"
FT /evidence="ECO:0000305"
FT CONFLICT 494..495
FT /note="AS -> GF (in Ref. 1; CAA27583)"
FT /evidence="ECO:0000305"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 23..33
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1V4G"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1VA6"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 76..91
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2D32"
FT HELIX 123..139
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 169..190
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:2D32"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1VA6"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1V4G"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 256..267
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 344..359
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 367..372
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 402..424
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 428..437
FT /evidence="ECO:0007829|PDB:1VA6"
FT TURN 438..441
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 447..457
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 464..476
FT /evidence="ECO:0007829|PDB:1VA6"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:2D32"
FT HELIX 485..505
FT /evidence="ECO:0007829|PDB:1VA6"
FT HELIX 510..514
FT /evidence="ECO:0007829|PDB:1VA6"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:2D33"
SQ SEQUENCE 518 AA; 58269 MW; 4E58C447B4D7FF16 CRC64;
MIPDVSQALA WLEKHPQALK GIQRGLERET LRVNADGTLA TTGHPEALGS ALTHKWITTD
FAEALLEFIT PVDGDIEHML TFMRDLHRYT ARNMGDERMW PLSMPCYIAE GQDIELAQYG
TSNTGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPMAFW QAKCGDISGA DAKEKISAGY
FRVIRNYYRF GWVIPYLFGA SPAICSSFLQ GKPTSLPFEK TECGMYYLPY ATSLRLSDLG
YTNKSQSNLG ITFNDLYEYV AGLKQAIKTP SEEYAKIGIE KDGKRLQINS NVLQIENELY
APIRPKRVTR SGESPSDALL RGGIEYIEVR SLDINPFSPI GVDEQQVRFL DLFMVWCALA
DAPEMSSSEL ACTRVNWNRV ILEGRKPGLT LGIGCETAQF PLPQVGKDLF RDLKRVAQTL
DSINGGEAYQ KVCDELVACF DNPDLTFSAR ILRSMIDTGI GGTGKAFAEA YRNLLREEPL
EILREEDFVA EREASERRQQ EMEAADTEPF AVWLEKHA
