ID   GSH1_SACD2              Reviewed;         530 AA.
AC   Q21EP1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=Sde_3583;
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(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; CP000282; ABD82838.1; -; Genomic_DNA.
DR   RefSeq; WP_011470053.1; NC_007912.1.
DR   AlphaFoldDB; Q21EP1; -.
DR   SMR; Q21EP1; -.
DR   STRING; 203122.Sde_3583; -.
DR   EnsemblBacteria; ABD82838; ABD82838; Sde_3583.
DR   KEGG; sde:Sde_3583; -.
DR   eggNOG; COG2918; Bacteria.
DR   HOGENOM; CLU_020728_3_0_6; -.
DR   OMA; RYSWLLM; -.
DR   OrthoDB; 967793at2; -.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000001947; 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..530
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000025185"
SQ   SEQUENCE   530 AA;  60265 MW;  C55176AC2B39CD30 CRC64;
     MYEIQSFHAG LYDSKNAPVL TGIMRGIERE GLRIDRDGKL AQTPHPVALG SALTHPQITT
     DFSEALLEFI TPPTHRVEDL FKQLYDIQGY TLSKLDDELI WSSSMPCVLN DDATIPVAQY
     GSSNNGTMKT VYRVGLGHRY GRAMQTVAGL HYNFSLPDAF WSFLHREEYS LLDLQDFKDQ
     KYFALIRNFR RYYWLLVYLF GASPALCGSF IKGREHNLQP LIDERTLHLP YATSLRMGDL
     GYQSSAQESL YVCYNDKQSY ITTLCAAITT PIDEYKAIGL QDEKGEFKQL NTSLLQIENE
     FYSSIRPKRT AKHGETALSA LRNRGVEYIE VRCLDIDPFD PLGVNKPQVR FLDTFLLYCA
     LQDSPDTSPE ESANILRNQK TVVTEGRSPK ALIESFTKGK IPLKQAGEAL IKAMRPVAEL
     LDIAHETEEH TQSLETQLAA ILNPELTPSA RIISHLSAKK LPYAHYALAQ SRHHHETLLA
     KKPSNNTMQQ FEKMAAESLD KQTRLEQKNS GNFSEFLQEY YKQYQMCCDK