AC   MF_02038;
DC   Protein; auto
TR   HAMAP; MF_02038; -; 1; level=0
XX
Names: EgtE
XX
ID   EGTE
DE   RecName: Full=Hercynylcysteine sulfoxide lyase;
DE            EC=4.4.1.36;
GN   Name=egtE;
XX
CC   -!- FUNCTION: Catalyzes a C-S bond cleavage, converting hercynylcysteine
CC       sulfoxide to 2-sulfenohercynine, a sulfenic acid intermediate that can
CC       be spontaneously reduced to ergothioneine. Ergothioneine is a secreted
CC       antioxidant that protects from oxidative stress.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-(hercyn-2-yl)-L-cysteine S-oxide + AH2 + H(+) =
CC         ergothioneine + pyruvate + A + NH4(+); Xref=Rhea:RHEA:42688,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:82706,
CC         ChEBI:CHEBI:134344; EC=4.4.1.36;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42689;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-(hercyn-2-yl)-L-cysteine S-oxide + H2O = 2-sulfenohercynine
CC         + pyruvate + NH4(+); Xref=Rhea:RHEA:52780, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:82706,
CC         ChEBI:CHEBI:136834;
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52781;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. EgtE subfamily.
XX
DR   Pfam; PF00266; Aminotran_5; 1; trigger=no
DR   NCBIfam; TIGR04343; egtE_PLP_lyase; 1; trigger=no
XX
KW   Lyase
KW   Pyridoxal phosphate
XX
GO   GO:0016846; F:carbon-sulfur lyase activity
GO   GO:0052699; P:ergothioneine biosynthetic process
XX
FT   From: EGTE_MYCS2 (A0R5M7)
FT   BINDING         48
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT   Condition: Y
FT   BINDING         82
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: S
FT   BINDING         83
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: N
FT   BINDING         106
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: Y
FT   BINDING         183
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: Q
FT   BINDING         183
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT   Condition: Q
FT   BINDING         200
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: S
FT   BINDING         202
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT   Condition: R
FT   BINDING         337
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT   Condition: R
FT   BINDING         348
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT   Condition: R
FT   MOD_RES         203
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Condition: K
XX
Size: 359-425;
Related: None;
Template: A0R5M7;
Scope:
 Bacteria; Actinomycetota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Version: 8
# Last updated date: 2025-06-17
# Created date: 2015-07-01
//