ID A0A1P8Y9X3_9NOCA Unreviewed; 411 AA.
AC A0A1P8Y9X3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ECO:0000313|EMBL:AQA20872.1};
GN ORFNames=BTZ20_4588 {ECO:0000313|EMBL:AQA20872.1};
OS Rhodococcus sp. MTM3W5.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1805827 {ECO:0000313|EMBL:AQA20872.1, ECO:0000313|Proteomes:UP000187995};
RN [1] {ECO:0000313|EMBL:AQA20872.1, ECO:0000313|Proteomes:UP000187995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTM3W5.2 {ECO:0000313|EMBL:AQA20872.1,
RC ECO:0000313|Proteomes:UP000187995};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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; CP019572; AQA20872.1; -; Genomic_DNA.
DR RefSeq; WP_077043857.1; NZ_CP019572.1.
DR AlphaFoldDB; A0A1P8Y9X3; -.
DR STRING; 1805827.BTZ20_4588; -.
DR OrthoDB; 9780152at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000187995; 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}.
SQ SEQUENCE 411 AA; 43772 MW; 7021C3DD7A01C194 CRC64;
MAMAVDSRRL TTRAAAEAYV GGVCFKLGPP RLIGAELEWL TARDDPARGR PDLGDVAAAL
GPHAPTSIAP SSPALSLPSG SAVTIEPGGQ IELSSAPLSS AEDLCVALAA DEAVLRRLLT
AAGITVRSHA ADRSRHAERL LRLPRYRAME ERFDGIGPFG RLMMCNTAAT QVSVDAGADP
AEVAARWRLL HDAGPALLAA FACSPRLRGT PDGGWASQRM RTWLELDPDR TRPLHTADPI
ADYGRWALDV PLLCVTGGRG ADSDGDWSAP PGATFADWIA GALDAEIDRR PDPADLDYHL
TTLFPPVRAA GHLEVRYLDA QPGDLWRVPI AALAALLGNR DTVAEATAIA ASTAGRWRDG
AEFGLRDGEL RRAASELLFL AAARSPRFEE ELASAAERCC RGVTPAEEYD R
//