ID A0A1C3N0Y7_9ACTN Unreviewed; 411 AA.
AC A0A1C3N0Y7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=GA0070620_1739 {ECO:0000313|EMBL:SBV26252.1};
OS Micromonospora krabiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=307121 {ECO:0000313|EMBL:SBV26252.1, ECO:0000313|Proteomes:UP000199393};
RN [1] {ECO:0000313|Proteomes:UP000199393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45344 {ECO:0000313|Proteomes:UP000199393};
RA Varghese N.;
RL Submitted (JUN-2016) 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; LT598496; SBV26252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C3N0Y7; -.
DR STRING; 307121.GA0070620_1739; -.
DR PATRIC; fig|307121.4.peg.1783; -.
DR OrthoDB; 9780152at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000199393; Chromosome i.
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:UP000199393}.
FT REGION 65..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 43670 MW; 2A2641108AC3A794 CRC64;
MVTSPGLERA TILRESAAAA SHLARICFKT GPPTQVGVEL EWTVHDAADP ARSIDAGRLR
AALGRHSPTT LTPTSPADPL GHGSAVTLEP GGQVEVSTPP RTSVAALVRA TGADIAELTA
LLGAAGLALG SSGIDPHREP RPVLHTPRYR AMRRAFDGRG PAGRTMMDAT AGLQVCLDAG
EPDQVALRWA VAHAVGPPLL AAFATADRHA GRPTGWASAR MAAWLAIEPS RTRPVWSPQR
PDEDPTAAWV RYVLAAPLLC LRRPGTDWTP PPGVTFGDWL AGALPRPPTT DDLDYHVSTL
FPPVRPRGYL ELRYLDAQPG RGWTIPLAVL AALFADPATL HAAYVVSAPV AHRWHAAARR
GLADPALAAA AAQLLDLALA ALPRLDLPSD LYDEIHRGVR RRRAVAERGD R
//
