ID   GSH1_SERP5              Reviewed;         520 AA.
AC   A8GA13;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Spro_0847;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-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}.
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DR   EMBL; CP000826; ABV39953.1; -; Genomic_DNA.
DR   RefSeq; WP_012005294.1; NC_009832.1.
DR   AlphaFoldDB; A8GA13; -.
DR   SMR; A8GA13; -.
DR   STRING; 399741.Spro_0847; -.
DR   EnsemblBacteria; ABV39953; ABV39953; Spro_0847.
DR   KEGG; spe:Spro_0847; -.
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..520
FT                   /note="Glutamate--cysteine ligase"
FT                   /id="PRO_1000061183"
SQ   SEQUENCE   520 AA;  58781 MW;  08514A768F7DE1F4 CRC64;
     MIPDVSQALS WLEAHPHALK GIRRGIERET LRVTEDGKLA TTGHPEKLGA ALTHHWITTD
     FAEALLEFIT PVDDNLDHLL TFLRDIHRHV ARNLGEERMW PLSMPCFIEA EQDIELAQFG
     SSNIGRMKTL YREGLKNRYG ALMQTISGVH YNFSLPLEFW QAWAGVKDAE SGKEQISAGY
     FRLIRNYYRF GWVIPYLFGA SPAICSSFLK GRETALPFER TEQGMCYLPY ATSLRLSDLG
     YTNKSQSNLG ITFNDLQSYV EGLKRAIVTP SEEFAKLGVK DGDRHLQLNS NVLQIENELY
     APIRPKRVTK SGETPSDALL RGGIEYIEVR SLDINPFSPI GVDAVQARFL DLFLIWCVLA
     DAPEMSSDEL LCTRKNWNRV ILEGRKPGQT IGIGCDDSRE PLAKVGKALF DDLRRVAEVL
     DSEAGDRQYQ QVCDELVAAF DDPELTFSAR ILKAMKEEGT GRVGLQLAEQ YRQMLIEEPL
     EILTETELAK EQEASWQRQR NVEASDTLSF EEFLKQHGGS