ID A0A0M8VKS2_9ACTN Unreviewed; 438 AA.
AC A0A0M8VKS2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=ADL01_24175 {ECO:0000313|EMBL:KOV67809.1};
OS Streptomyces sp. NRRL WC-3618.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV67809.1, ECO:0000313|Proteomes:UP000037738};
RN [1] {ECO:0000313|EMBL:KOV67809.1, ECO:0000313|Proteomes:UP000037738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV67809.1,
RC ECO:0000313|Proteomes:UP000037738};
RA Noorani M.;
RL Submitted (JUL-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOV67809.1}.
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DR EMBL; LGDW01000314; KOV67809.1; -; Genomic_DNA.
DR RefSeq; WP_053744104.1; NZ_LGDW01000314.1.
DR AlphaFoldDB; A0A0M8VKS2; -.
DR PATRIC; fig|1519490.3.peg.5284; -.
DR OrthoDB; 9780152at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000037738; 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:UP000037738}.
SQ SEQUENCE 438 AA; 47660 MW; EC71E53AA303F850 CRC64;
MSDSVSDCST PRTALSEAEV EALVRGICFK TGPPRTLGVE VEWLVHELRR PQLPVTPERL
EAAYAALRTL PLRSALTVEP GGQLELSSAP AGSLMECIGS VSADLDAVRA VLREDGLGLV
GLGQDPWHSP RRFLHEPRYD ALEQCLDLTG PAGRAMMCTS ASVQVCLDAG HEEPGPLGHG
RRWWLANQLG PVLVAAFANS PLAEQGPTGW RSTRQVLWME IGAGRAGAPP LDADPRQAWA
RHVLDAPVMC VRRDSGPWYV PEDGLTFREW VRTGVPRPPT REDLDYHLTT LFPPVRPRGH
LELRMIDAQP GDDGWIVPLA VTAALFDDPE ATERAYRAVK PLAERALSQP APNNPLWADA
ARHGLADPEL REVALVCFSA ALDALPRLGA SQEVLDAVSA YVDRYVLQGR CPADDLLDQL
RGTDLLAHGT SYGKDLRT
//