GSH1_PSEMY
ID GSH1_PSEMY Reviewed; 526 AA.
AC A4XP63;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
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=Pmen_0356;
OS Pseudomonas mendocina (strain ymp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=399739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ymp;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Detter J.C., Bruce D., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Hersman L., Dubois J., Maurice P., Richardson P.;
RT "Complete sequence of Pseudomonas mendocina ymp.";
RL Submitted (APR-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000680; ABP83129.1; -; Genomic_DNA.
DR RefSeq; WP_011920618.1; NC_009439.1.
DR AlphaFoldDB; A4XP63; -.
DR SMR; A4XP63; -.
DR STRING; 399739.Pmen_0356; -.
DR EnsemblBacteria; ABP83129; ABP83129; Pmen_0356.
DR KEGG; pmy:Pmen_0356; -.
DR PATRIC; fig|399739.8.peg.365; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR OrthoDB; 967793at2; -.
DR UniPathway; UPA00142; UER00209.
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..526
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000025181"
SQ SEQUENCE 526 AA; 58638 MW; 90CC07019834F344 CRC64;
MSDLLSRRLA QLGEPANLSL LGECLHGIER ECLRVDHDGQ LALTPHPQAL GSALTHAQIT
TDYSESLLEF ITGTATDPAA TLAELESIHR FAYEKLGGEL LWSPSMPCAL PDEETIPIAR
YGSSNIGRLK YVYRKGLALR YGKTMQCIAG IHYNFSLPEA LWQLQQRSEG NTQSTRDYQS
ARYIALIRNF RRYSWLLMYL FGASPALDKG FMRGRPHQLQ ELDASTLYLP YATSLRMSDL
GYQSSAQSGL TPCYNDLASY TDSLRLAVGT PYPAYVEAGT KRGDEWLQLN TNILQIENEY
YSSIRPKRVT YSGERPIQAL TSRGVQYVEV RCLDINPFLP LGIDLPQARF IDAFLLFCAL
EDSPLLESGE CGACTSNFLK VVKEGRRPGL HLQRDGRSIE LKTWASELLE RIHPLCELLD
RSQGGNAHIE ALAQQQAKVA DVEMTPSAQV LAILRQGQSF TEFALQQSLR HAEYFRAEPL
SAEQQQAFEQ AAHDSLAEQA ELEAQPKGDF DAFVAAYQAS ILALAV
