GSH1_SALPB
ID GSH1_SALPB Reviewed; 518 AA.
AC A9N0B5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Glutamate--cysteine ligase {ECO:0000255|HAMAP-Rule:MF_00578};
DE EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_00578};
DE AltName: Full=Gamma-ECS {ECO:0000255|HAMAP-Rule:MF_00578};
DE Short=GCS {ECO:0000255|HAMAP-Rule:MF_00578};
DE AltName: Full=Gamma-glutamylcysteine synthetase {ECO:0000255|HAMAP-Rule:MF_00578};
GN Name=gshA {ECO:0000255|HAMAP-Rule:MF_00578}; OrderedLocusNames=SPAB_03503;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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_00578};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00578}.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 1 family.
CC Type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00578}.
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DR EMBL; CP000886; ABX68849.1; -; Genomic_DNA.
DR RefSeq; WP_000611821.1; NC_010102.1.
DR AlphaFoldDB; A9N0B5; -.
DR SMR; A9N0B5; -.
DR KEGG; spq:SPAB_03503; -.
DR PATRIC; fig|1016998.12.peg.3302; -.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR BioCyc; SENT1016998:SPAB_RS14270-MON; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000008556; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding.
FT CHAIN 1..518
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000082360"
SQ SEQUENCE 518 AA; 58384 MW; 9766882B28965C47 CRC64;
MIPDVSQALA WLEKHPQALK GIQRGLERET LRVNADGTLA TTGHPEALGS ALTHKWITTD
FAEALLEFIT PVDGDIQHML TFMRDLHRYT ARKLGDERMW PLSMPCYIAE GQDIELAQYG
TSNTGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPMAFW QAKCGVTEGE AAKEKISAGY
FRLIRNYYRF GWVIPYLFGA SPAICSSFLQ GKPTTLPFEK TDCGMYYLPY ATSLRLSDLG
YTNKSQSNLG ITFNDLHEYV AGLKRAIKTP SEEYARIGVE KDGKRLQINS NVLQIENELY
APIRPKRVTR SGESPSDALL RGGIEYIEVR SLDINPFSPI GVDEQQVRFL DLFMVWCVLA
DAPEMSSDEL LCTRTNWNRV ILEGRKPGLT LGIGCETAQF PLPKVGKDLF RDLKRVAQTL
DSIHGGEEYQ KVCDELVACF DNPELTFSAR ILRSMIDEGI GGTGKAFGEA YRNLLREEPL
EILQEEEFIA ERDASVRRQQ EIEAADTEPF AAWLAKHA
