GSH1_PECCP
ID GSH1_PECCP Reviewed; 517 AA.
AC C6DCQ5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 60.
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=PC1_3207;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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; CP001657; ACT14230.1; -; Genomic_DNA.
DR RefSeq; WP_015841367.1; NC_012917.1.
DR AlphaFoldDB; C6DCQ5; -.
DR SMR; C6DCQ5; -.
DR STRING; 561230.PC1_3207; -.
DR EnsemblBacteria; ACT14230; ACT14230; PC1_3207.
DR KEGG; pct:PC1_3207; -.
DR eggNOG; COG2918; Bacteria.
DR HOGENOM; CLU_020728_3_0_6; -.
DR OMA; RYSWLLM; -.
DR OrthoDB; 967793at2; -.
DR UniPathway; UPA00142; UER00209.
DR Proteomes; UP000002736; 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..517
FT /note="Glutamate--cysteine ligase"
FT /id="PRO_1000212105"
SQ SEQUENCE 517 AA; 58265 MW; EB39DBA188A58316 CRC64;
MIPDISEALS WLEKHPLAVK GIQRGIERET LRVTANGHLA TTGHPEILGS ALAHPWITTD
FAEALLEFIT PVDNDVDHLL TFLRDIHRHV SRNLGDERMW PLSMPCFIDS EQNIELAQYG
SSNIGRFKTL YREGLKNRYG ALMQTISGVH YNFSLPLSFW QAREGVADAE SGKKAISAGY
FRLIRNYYRF GWVIPYLFGA SPAICSSFLK GRETALPFER TEKGMLYLPY ATSLRLSDLG
YTNKSQSNLG ITFNDLDTYV AALKRAIKTP SEEYAQVGMK KDGRYLQLNT NVLQIENELY
APIRPKRVTR AGETPSDALL RGGIEYIEVR SLDINPFSPT GVSESQVRFL DLFLIWCALA
DAPEMSADEL LCTRKNWNRV ILEGRKPGQT VGMRCETIQQ PIAEVGKSLF ADLRRVAEVL
DAENSQPHYQ QVCDELLVGF DDPETTFSGR LLTLMKQEGN GSVGLSLAEE YRKMLSSEPL
QVLTEEQLAA ASEHSWQRQR QIESEDTMSF DDYLAAN
