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Database: UniProt
Entry: A0A169PEQ6_STRLU
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ID   A0A169PEQ6_STRLU        Unreviewed;       397 AA.
AC   A0A169PEQ6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Glutamate--cysteine ligase EgtA {ECO:0000256|HAMAP-Rule:MF_02034};
DE            EC=6.3.2.2 {ECO:0000256|HAMAP-Rule:MF_02034};
DE   AltName: Full=Gamma-glutamylcysteine synthase {ECO:0000256|HAMAP-Rule:MF_02034};
DE            Short=GCS {ECO:0000256|HAMAP-Rule:MF_02034};
DE            Short=Gamma-ECS {ECO:0000256|HAMAP-Rule:MF_02034};
GN   Name=egtA {ECO:0000256|HAMAP-Rule:MF_02034};
GN   ORFNames=SLA_6652 {ECO:0000313|EMBL:BAU87518.1};
OS   Streptomyces laurentii.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=39478 {ECO:0000313|EMBL:BAU87518.1, ECO:0000313|Proteomes:UP000217676};
RN   [1] {ECO:0000313|EMBL:BAU87518.1, ECO:0000313|Proteomes:UP000217676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31255 {ECO:0000313|EMBL:BAU87518.1,
RC   ECO:0000313|Proteomes:UP000217676};
RA   Doi K., Fujino Y., Nagayoshi Y., Ohshima T., Ogata S.;
RT   "Complete Genome Sequence of Thiostrepton-Producing Streptomyces laurentii
RT   ATCC 31255.";
RL   Genome Announc. 4:e00360-16(2016).
CC   -!- FUNCTION: Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC).
CC       This compound is used as substrate for the biosynthesis of the low-
CC       molecular thiol compound ergothioneine. {ECO:0000256|HAMAP-
CC       Rule:MF_02034}.
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:0000256|ARBA:ARBA00029283, ECO:0000256|HAMAP-
CC         Rule:MF_02034, ECO:0000256|PIRNR:PIRNR017901};
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02034}.
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC       EgtA subfamily. {ECO:0000256|HAMAP-Rule:MF_02034,
CC       ECO:0000256|PIRNR:PIRNR017901}.
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DR   EMBL; AP017424; BAU87518.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A169PEQ6; -.
DR   KEGG; slau:SLA_6652; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000217676; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.590.20; -; 1.
DR   HAMAP; MF_02034; EgtA; 1.
DR   InterPro; IPR017809; EgtA_Actinobacteria.
DR   InterPro; IPR035434; GCL_bact_plant.
DR   InterPro; IPR006336; GCS2.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   NCBIfam; TIGR03444; EgtA_Cys_ligase; 1.
DR   PANTHER; PTHR34378; GLUTAMATE--CYSTEINE LIGASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR34378:SF1; GLUTAMATE--CYSTEINE LIGASE, CHLOROPLASTIC; 1.
DR   Pfam; PF04107; GCS2; 1.
DR   PIRSF; PIRSF017901; GCL; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02034,
KW   ECO:0000256|PIRNR:PIRNR017901};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_02034, ECO:0000256|PIRNR:PIRNR017901};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02034,
KW   ECO:0000256|PIRNR:PIRNR017901};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217676}.
SQ   SEQUENCE   397 AA;  42681 MW;  F9457FB98B8BB874 CRC64;
     MYLFQDGAAA HRGAELEWLV HDLRDPRLPV PPGRLAAAID TVRAVPLTAA LTFEPGGQLE
     LSSLPAASLM ECLDSLAADL RAVREALAPL CLGLGGYGVD PWHAPRARVL REPRYDAMEQ
     VFNRTGPSGR AMMCETASVQ VCLDAGVDGP GPLDFRRRWR LAHLLGAVLV AVFANSPVHG
     GRRTGWRSTR QSLWTDLDPA RALAPPADGD PRAEWASHVL DAPVLCVRPK DDGPWTVPEG
     LTFRDWLRTG RPRRADAEDL RYHLTTLFPP VRPRGHLELR MIDAQPGRDG WMIPVAVATA
     LFDDPVAAEA AERAVRPLAA LAGPDPAPRN PLWRAAARDG LAHPALRAAA LDVFGSALDA
     LPRVGASAAV TGAVAAFHER YVARGVCPAD ESLEVAS
//
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