EGTA_MYCS2
ID EGTA_MYCS2 Reviewed; 423 AA.
AC A0R5N1; I7FMI3;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Glutamate--cysteine ligase EgtA;
DE EC=6.3.2.2 {ECO:0000250|UniProtKB:P9WPK7};
DE AltName: Full=Gamma-glutamylcysteine synthetase;
DE Short=GCS;
DE Short=Gamma-ECS;
GN Name=egtA {ECO:0000303|PubMed:20420449};
GN OrderedLocusNames=MSMEG_6250, MSMEI_6089;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, GENE NAME, AND PATHWAY.
RC STRAIN=ATCC 607 / DSM 43465 / JCM 20379 / NBRC 3207 / NRRL B-692;
RX PubMed=20420449; DOI=10.1021/ja101721e;
RA Seebeck F.P.;
RT "In vitro reconstitution of Mycobacterial ergothioneine biosynthesis.";
RL J. Am. Chem. Soc. 132:6632-6633(2010).
CC -!- FUNCTION: Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC)
CC (By similarity). This compound is used as substrate for the
CC biosynthesis of the low-molecular thiol compound ergothioneine
CC (PubMed:20420449). {ECO:0000250|UniProtKB:P9WPK7,
CC ECO:0000269|PubMed:20420449}.
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:0000250|UniProtKB:P9WPK7};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000305|PubMed:20420449}.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC EgtA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP42520.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK74415.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42520.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011731159.1; NZ_SIJM01000027.1.
DR RefSeq; YP_890469.1; NC_008596.1.
DR AlphaFoldDB; A0R5N1; -.
DR SMR; A0R5N1; -.
DR STRING; 246196.MSMEI_6089; -.
DR PRIDE; A0R5N1; -.
DR EnsemblBacteria; ABK74415; ABK74415; MSMEG_6250.
DR EnsemblBacteria; AFP42520; AFP42520; MSMEI_6089.
DR GeneID; 66737533; -.
DR KEGG; msg:MSMEI_6089; -.
DR KEGG; msm:MSMEG_6250; -.
DR PATRIC; fig|246196.19.peg.6089; -.
DR eggNOG; COG3572; Bacteria.
DR OMA; GLTFREW; -.
DR OrthoDB; 991285at2; -.
DR BioCyc; MetaCyc:MON-17988; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; ISS:UniProtKB.
DR GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:InterPro.
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 InterPro; IPR011556; Glut_cys_lig_pln_type.
DR PANTHER; PTHR34378; PTHR34378; 1.
DR PANTHER; PTHR34378:SF1; PTHR34378:SF1; 1.
DR Pfam; PF04107; GCS2; 1.
DR PIRSF; PIRSF017901; GCL; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR TIGRFAMs; TIGR03444; EgtA_Cys_ligase; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..423
FT /note="Glutamate--cysteine ligase EgtA"
FT /id="PRO_0000413645"
SQ SEQUENCE 423 AA; 45157 MW; A3617D96F4B30AB6 CRC64;
MALPARSDSG CAVPVEFTSA EQAAAHIGAN SLQDGPIGRV GLEIEAHCFD LSNPTRRPSW
DELSAVIADV PPLPGGSRIT VEPGGAVELS GPPYDGPLAA VAALQADRAV LRAEFARRNL
GLVLLGTDPL RPTRRVNPGA RYSAMEQFFT ASGTAEAGAA MMTATASVQV NLDAGPRDGW
AERVRLAHAL GPTMIAITAN SPMLGGQFTG WCSTRQRVWG QLDSARCGPV LGVDGDDPAS
EWARYALRAP VMLVNSPDAV PVTNWVPFAD WADGRAVLGG RRPTEADLDY HLTTLFPPVR
PRRWLEIRYL DSVPDALWPA AVFTLTTLLD DPVAAESAAE ATRPVATAWD RAARMGLTDR
HLHTAALTCV RLAAERAPAE LEESMTLLMR SVQQRRSPAD DFSDRVVARG IAAAVRELAK
GEL
