ID A0A2U3P874_9MYCO Unreviewed; 429 AA.
AC A0A2U3P874;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-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=MNAB215_2134 {ECO:0000313|EMBL:SPM39940.1};
OS Mycobacterium numidiamassiliense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1841861 {ECO:0000313|EMBL:SPM39940.1, ECO:0000313|Proteomes:UP000240424};
RN [1] {ECO:0000313|EMBL:SPM39940.1, ECO:0000313|Proteomes:UP000240424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB215 {ECO:0000313|EMBL:SPM39940.1,
RC ECO:0000313|Proteomes:UP000240424};
RG Urmite Genomes;
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; FUEZ01000004; SPM39940.1; -; Genomic_DNA.
DR RefSeq; WP_077078828.1; NZ_FUEZ01000004.1.
DR AlphaFoldDB; A0A2U3P874; -.
DR STRING; 1841861.GCA_900157365_00451; -.
DR OrthoDB; 9780152at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000240424; Unassembled WGS sequence.
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:UP000240424}.
SQ SEQUENCE 429 AA; 45410 MW; 230C940D0065FE99 CRC64;
MTLAAITAAT SQPDAARLLE AEMADSSAAA QYIADGCLVD GPLGRVGLEV EAHCFDPLDP
RRRPSWTEIT DVIELLPPLP CGSAVTVEPG GAVELSGPPR DGVVAAIDAM NRDQAVLRKA
FADVGLGLVF LGADPLRSPK RVNPGARYRA MERFFAASHS GEAGAGVMTS TAAGQGNVDA
GPQSGWAARV RLAHALGPTM IAIAANSPLL GGEFTGWVST RQRVWGAMDS ARCGPILGAS
GDEPGTDWAR YALKAPVMLV NNPEAVPVTH WVPFTDWVEG RELLGGRRPT VADLDYHLTT
LFPPVRPRRW LEIRYLDSVP DDLWSAVAFT LVTLLDDPVA ADRAAEVVEP VATAWDTAAR
LGLRDRRLLA AANRCVAIAA ERTPAELTDA MQRLLDNVAQ GRCPGDEFAD QVVDHGIAAT
VSQLAQGGL
//
