ID A0A1W0BDL5_9NOCA Unreviewed; 432 AA.
AC A0A1W0BDL5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=B0T46_13005 {ECO:0000313|EMBL:ONM48296.1};
OS Nocardia donostiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1538463 {ECO:0000313|EMBL:ONM48296.1, ECO:0000313|Proteomes:UP000188836};
RN [1] {ECO:0000313|EMBL:ONM48296.1, ECO:0000313|Proteomes:UP000188836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X1655 {ECO:0000313|EMBL:ONM48296.1,
RC ECO:0000313|Proteomes:UP000188836};
RX PubMed=26914251; DOI=10.1007/s10482-016-0667-8;
RA Ercibengoa M., Bell M., Marimon J.M., Humrighouse B., Klenk H.P.,
RA Potter G., Perez-Trallero E.;
RT "Nocardia donostiensis sp. nov., isolated from human respiratory
RT specimens.";
RL Antonie Van Leeuwenhoek 109:653-660(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}.
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:ONM48296.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MUMY01000010; ONM48296.1; -; Genomic_DNA.
DR RefSeq; WP_077116860.1; NZ_MUMY01000010.1.
DR AlphaFoldDB; A0A1W0BDL5; -.
DR STRING; 1538463.B0T36_13335; -.
DR OrthoDB; 9780152at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000188836; 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:UP000188836}.
SQ SEQUENCE 432 AA; 46086 MW; 9D0885813A5C5D05 CRC64;
MAVTLEHHGS VVGVRRGLSS RAAAEAYIGG VCFKLGPPLL IGAELEWLTA HSAYRRPGAV
APRPPLDLVA AALGPYAPQT IAPASPARPL PGGSRVTIEP GGQIELSSAA CPDAARLCAR
LDSDTRLLRQ LLGTKSIRLV WAAADTGRRP QRMLRLPRYH AMERYLGGIG PFGALMMCNT
AATQVSVDAG TDPAELAARW QTLYMIGPAL LAAFARSPAL CGAPPGVWAS QRMRTWLRLD
YARTRPPVQE WADPVSGYAR WALDAPLLCV RRPAPARQET DGECAWSAPP GATFADWISG
ALDDEVGRRP GYDDLDYHLT TLFPPVRAAG HLEVRYLDAQ PGDSWSVPIR VIEALMSTSA
VVRDASTLAA PTAGRWLDAA RHGLADPQIR TVATDLLETA AEHATTAAAP AIHAAARRCR
AGRPPEESGD RA
//
