ID A0A1X0H2E0_9MYCO Unreviewed; 376 AA.
AC A0A1X0H2E0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Probable hercynylcysteine sulfoxide lyase {ECO:0000256|HAMAP-Rule:MF_02038};
DE EC=4.4.-.- {ECO:0000256|HAMAP-Rule:MF_02038};
GN Name=egtE {ECO:0000256|HAMAP-Rule:MF_02038};
GN ORFNames=BST36_19180 {ECO:0000313|EMBL:ORB20325.1};
OS Mycolicibacterium moriokaense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=39691 {ECO:0000313|EMBL:ORB20325.1, ECO:0000313|Proteomes:UP000192354};
RN [1] {ECO:0000313|EMBL:ORB20325.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP105393 {ECO:0000313|EMBL:ORB20325.1};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably catalyzes the conversion of hercynylcysteine
CC sulfoxide to ergothioneine. {ECO:0000256|HAMAP-Rule:MF_02038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H(+) + S-(hercyn-2-yl)-L-cysteine S-oxide = A +
CC ergothioneine + NH4(+) + pyruvate; 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; Evidence={ECO:0000256|HAMAP-Rule:MF_02038};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02038};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02038}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. EgtE subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_02038}.
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:ORB20325.1}.
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DR EMBL; MVIB01000020; ORB20325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X0H2E0; -.
DR OrthoDB; 9808002at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000192354; Unassembled WGS sequence.
DR GO; GO:1990411; F:hercynylcysteine sulfoxide lyase activity (ergothioneine-forming); IEA:RHEA.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_02038; EgtE; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR027563; EgtE.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04343; egtE_PLP_lyase; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|HAMAP-Rule:MF_02038};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02038}.
FT DOMAIN 22..366
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02038"
SQ SEQUENCE 376 AA; 39238 MW; 4BECD5B5F7450FF1 CRC64;
MTSEPESLGE KWRAARPAVA GIHLDSAACS RQSFAVIDAA AQHARHEAEV GGYVAAAAAA
PVLDAGRAAI AALTGLDSSG VVFTTGANNA LDLLLSSWPG ERTVACLPGE YGPNLAIMAA
NGFAVRTLPV DGEGRLDVDA ARRALAEDRP ALVHLTALAS HRGIAQPMAA LADVCRDLDL
ALVIDAAQAL GHLDCAVTPS AIYSSSRKWV AGPRGVGFLA LRDDLSRTLK PRLPPPEWGL
PLTVTERLEQ GEANVAARVG YSVALGEYLA AGPARIGERL AEVGGMTREA LADVRGWRVV
EAVDEPTAIT TLEPVDGADP QQVRAQLIAE HAIVTTYAET LRAPFEMASP VLRASPHVDV
TVEELGQFAK VLAAVT
//
