EGTE_MYCS2
ID EGTE_MYCS2 Reviewed; 371 AA.
AC A0R5M7; I7GFJ8;
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=Probable hercynylcysteine sulfoxide lyase {ECO:0000305|PubMed:20420449};
DE EC=4.4.-.- {ECO:0000305|PubMed:20420449};
GN Name=egtE {ECO:0000303|PubMed:20420449};
GN OrderedLocusNames=MSMEG_6246, MSMEI_6085;
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, PATHWAY, AND GENE NAME.
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).
RN [5]
RP ROLE OF ERGOTHIONEINE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=23629716; DOI=10.1128/aac.02572-12;
RA Sao Emani C., Williams M.J., Wiid I.J., Hiten N.F., Viljoen A.J.,
RA Pietersen R.D., van Helden P.D., Baker B.;
RT "Ergothioneine is a secreted antioxidant in Mycobacterium smegmatis.";
RL Antimicrob. Agents Chemother. 57:3202-3207(2013).
CC -!- FUNCTION: Probably catalyzes the conversion of hercynylcysteine
CC sulfoxide to ergothioneine. Ergothioneine is a secreted antioxidant
CC that protects mycobacterium from oxidative stress.
CC {ECO:0000305|PubMed:20420449, ECO:0000305|PubMed:23629716}.
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:0000305|PubMed:20420449};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P23721};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000305|PubMed:20420449}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. EgtE subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFP42516.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK70212.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42516.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011731155.1; NZ_SIJM01000027.1.
DR RefSeq; YP_890465.1; NC_008596.1.
DR AlphaFoldDB; A0R5M7; -.
DR SMR; A0R5M7; -.
DR STRING; 246196.MSMEI_6085; -.
DR EnsemblBacteria; ABK70212; ABK70212; MSMEG_6246.
DR EnsemblBacteria; AFP42516; AFP42516; MSMEI_6085.
DR GeneID; 66737529; -.
DR KEGG; msg:MSMEI_6085; -.
DR KEGG; msm:MSMEG_6246; -.
DR PATRIC; fig|246196.19.peg.6085; -.
DR eggNOG; COG0520; Bacteria.
DR OMA; GTSRKWL; -.
DR OrthoDB; 446447at2; -.
DR BioCyc; MetaCyc:MON-17987; -.
DR BRENDA; 4.4.1.36; 3512.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:1990411; F:hercynylcysteine sulfoxide lyase activity (ergothioneine-forming); IEA:RHEA.
DR GO; GO:0052704; P:ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide; IDA:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR04343; egtE_PLP_lyase; 1.
PE 3: Inferred from homology;
KW Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..371
FT /note="Probable hercynylcysteine sulfoxide lyase"
FT /id="PRO_0000413653"
FT MOD_RES 203
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P23721"
SQ SEQUENCE 371 AA; 39033 MW; 13B7856383CB1458 CRC64;
MMLAQQWRDA RPKVAGLHLD SGACSRQSFA VIDATTAHAR HEAEVGGYVA AEAATPALDA
GRAAVASLIG FAASDVVYTS GSNHAIDLLL SSWPGKRTLA CLPGEYGPNL SAMAANGFQV
RALPVDDDGR VLVDEASHEL SAHPVALVHL TALASHRGIA QPAAELVEAC HNAGIPVVID
AAQALGHLDC NVGADAVYSS SRKWLAGPRG VGVLAVRPEL AERLQPRIPP SDWPIPMSVL
EKLELGEHNA AARVGFSVAV GEHLAAGPTA VRERLAEVGR LSRQVLAEVD GWRVVEPVDQ
PTAITTLEST DGADPASVRS WLIAERGIVT TACELARAPF EMRTPVLRIS PHVDVTVDEL
EQFAAALREA P