ID A0A495W3R3_9PSEU Unreviewed; 412 AA.
AC A0A495W3R3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 28-JUN-2023, entry version 14.
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=C8E97_4682 {ECO:0000313|EMBL:RKT55994.1};
OS Saccharothrix australiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=2072 {ECO:0000313|EMBL:RKT55994.1, ECO:0000313|Proteomes:UP000282084};
RN [1] {ECO:0000313|EMBL:RKT55994.1, ECO:0000313|Proteomes:UP000282084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43800 {ECO:0000313|EMBL:RKT55994.1,
RC ECO:0000313|Proteomes:UP000282084};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) 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:RKT55994.1}.
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; RBXO01000001; RKT55994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495W3R3; -.
DR OrthoDB; 9780152at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000282084; 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 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:UP000282084}.
FT REGION 70..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 44134 MW; D6E95FECF1F71E2E CRC64;
MTAVRNTPPP GPTPAVFRDR AEAEAYVASV CFKHGPPRLL GVELEWTVHH REDPAKPLDR
DALAAALGRH APPTLVPDSP QQPLPGGTPL TVEPGGQVEI STPPSGSLTD LLKTVAADVD
HLTGLLEPAG LVLGHRGADP HRPPRRLLRV PRYAAMEHAF APLGPEGITM MCSTAGLQVC
LDLGHREDLA ARWAAVHALG PVLTALFANS PGVGGRRTDW ATARMRALYA TDPVRTRPGA
VCADPAAAWA RRIVDSPVIV VRRPGSDWLP RHRFTFAEWI DGALGTGPTS DDLDYHLTLQ
FPPVRPRGYL EVRYLDTPRH GGWVAPVVLL AALFSDRSLV DAVLAATRAA ANRWLAAARY
GLRDPVLARA ARDVVELGCA ALRATDLSVG QTDAIAEELH RTLAEQTGGS RP
//
