GSH1_BUCBP
ID GSH1_BUCBP Reviewed; 521 AA.
AC Q89AD8;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
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; OrderedLocusNames=bbp_368;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27085.1; -; Genomic_DNA.
DR RefSeq; WP_011091486.1; NC_004545.1.
DR AlphaFoldDB; Q89AD8; -.
DR SMR; Q89AD8; -.
DR STRING; 224915.bbp_368; -.
DR EnsemblBacteria; AAO27085; AAO27085; bbp_368.
DR GeneID; 56470907; -.
DR KEGG; bab:bbp_368; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR OrthoDB; 967793at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000000601; 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..521
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_0000192522"
SQ SEQUENCE 521 AA; 61433 MW; 1FD19D58646C89BB CRC64;
MIPKIYKKIK WLQSNPLILK KILRGIEREA LRTDIHGTII NTAYPQDKIG SALTHKWITT
DFSESLLEFI TPTNASTNYI LKFLNDTHKF VNDNLIQEYF WPFSIPPCKK YMHSIKLSKY
GTSNLGQVKT LYRKGLKHRY GILMNIISGV HYNFSLPRIF WNHWKKIHHK NTQYNTTSEG
YLCLIRNYYK FGWIIPYLFG ASPAVEPLFI KNKKHNYKFK KHHGMLYLPW STSLRLSDLG
HTNQSIKKLK LTFNSLSEYV LALEHGIKTP SKQFKNLGLY DQFGNFKQIN TNLLQTENEL
YTYIRPKQKL KNCESLSAAL RNRGIEYVEI RALDINPFTS TGVDKNQILL LDLFLIWCVL
ADSPKISSQE FHFFLKNWHT IITKGRKPKQ KININIYNTK NTIQTIGKTI LYDLFYIAEI
LDSLSNNNNY QETCKNLILY FDYPELTYSE KLLNKFMCYG IYETGANLFV KYKQKLHNDS
FKILSKKDLN NEMMKSNNSQ KLIEKQDTLN FKEYLNLYYT K