GSH1_PSEU5
ID GSH1_PSEU5 Reviewed; 525 AA.
AC A4VG81;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=PST_0276;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RX PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Nitrogen fixation island and rhizosphere competence traits in the genome
RT of root-associated Pseudomonas stutzeri A1501.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP77982.1; -; Genomic_DNA.
DR RefSeq; WP_011911514.1; NC_009434.1.
DR AlphaFoldDB; A4VG81; -.
DR SMR; A4VG81; -.
DR STRING; 379731.PST_0276; -.
DR EnsemblBacteria; ABP77982; ABP77982; PST_0276.
DR KEGG; psa:PST_0276; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000000233; 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..525
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000025184"
SQ SEQUENCE 525 AA; 58500 MW; 7053B9D23533F4A2 CRC64;
MSALLTHRLA LLAKAPHLPL LNQCLHGIER ECLRVDAHGH LAMTPHPIAL GSALTHPQIT
TDYSEALLEF ITGTDQDPRN TLAELEAIHR FTYAKLGDEY LWSPSMPCPL PSEADIPIAE
YGSSNIGRLK HVYRQGLALR YGKTMQCIAG IHYNFSLPEA LWPVLQADDG DTRTERDYRS
ARYIGLIRNF RRYSWLLMYL FGASPALDAG FLRGRPHQLE ALDADTLYLP YATSLRMSDL
GYQNNAQAGL TPCYDDLSSY TESLYRAVST PYAPYEAMGI KDAAGNWQQL NTNVLQIENE
YYSNIRPKRV TATGERPLQA LRARGIQYIE VRCLDINPFL PLGIDLAESR FLDAFLLFCA
LADSPCLADG ECGAATDNFL KVVKEGRRPG LQLQRCGEAV PLGEWAGQLL DEIAEVAALL
DRSHGDSRHA EALAEQRAKV ADSSLTPSAR VLEQLRTNGE SFSQFAMRQT LAHADYFRSQ
APSADELQQF ETAARQSLER QAAMEATDTL DFDSFVADYQ RSLSL
