GSH1_SHEAM
ID GSH1_SHEAM Reviewed; 526 AA.
AC A1S4F9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=Sama_1058;
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) 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; CP000507; ABL99265.1; -; Genomic_DNA.
DR RefSeq; WP_011759174.1; NC_008700.1.
DR AlphaFoldDB; A1S4F9; -.
DR SMR; A1S4F9; -.
DR STRING; 326297.Sama_1058; -.
DR EnsemblBacteria; ABL99265; ABL99265; Sama_1058.
DR KEGG; saz:Sama_1058; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR OrthoDB; 967793at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000009175; 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;
KW Reference proteome.
FT CHAIN 1..526
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000025186"
SQ SEQUENCE 526 AA; 57965 MW; F90923FAB15EEA73 CRC64;
MTAFNDRLGA LSDAEGRKAL AGLRRGLERE ALRITSCCQL ALDPHPKALG SALTHSRITT
DYSEALLEFI TPVSGNIEDL LEGLTETHAY TLKHLDGQKL WPVSMPCYVG DVKDIPIAQY
GTSNTGRMKT LYRKGLTYRY GALMQIISGV HFNFSLSSDL WPRLHALSGS SLSLDEFISE
SYFGLIRNYR RLVWVLPYLF GASPAICGSF LKGQKTSLEF EKTAGGTLYL PYATSLRMSD
LGYTNKEQAS LNISYDSLHD YLQGIREAIC LPSAKFAEIG VKVDGEYRQL NANVLQIENE
FYAPIRAKRV TRKGEKPSEA LARAGVEYIE VRALDVNPFS PVGVEASQLR FLDVFLLYCL
LSDSPKSDAV CESEITSNLR AVIHEGRKPG LALSRQGEPV TLKAWLLELF DEFDKLASLL
DIDGSDYAEA LAQWRMAVED PALTLSGRVH AAVVEQGMNH GDFVMGLAAK YQDFFLSYPL
SPGVEAGFQA EAASSLAAQA EIEASDEESF DEYLKGYFKG VPCALS
