ID   EGTE_MYCTU              Reviewed;         390 AA.
AC   O69668; L0TGH4;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 3.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Probable hercynylcysteine sulfoxide lyase;
DE            EC=4.4.-.- {ECO:0000250|UniProtKB:A0R5M7};
GN   Name=egtE; OrderedLocusNames=Rv3700c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Probably catalyzes the conversion of hercynylcysteine
CC       sulfoxide to ergothioneine. Ergothioneine is an antioxidant that
CC       protects mycobacteria from oxidative stress.
CC       {ECO:0000250|UniProtKB:A0R5M7, ECO:0000250|UniProtKB:Q7D515}.
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:0000250|UniProtKB:A0R5M7};
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:0000250|UniProtKB:A0R5M7}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. EgtE subfamily. {ECO:0000305}.
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DR   EMBL; AL123456; CCP46525.1; -; Genomic_DNA.
DR   PIR; E70793; E70793.
DR   RefSeq; NP_218217.1; NC_000962.3.
DR   RefSeq; WP_003901701.1; NZ_NVQJ01000028.1.
DR   AlphaFoldDB; O69668; -.
DR   SMR; O69668; -.
DR   STRING; 83332.Rv3700c; -.
DR   PaxDb; O69668; -.
DR   PRIDE; O69668; -.
DR   GeneID; 885161; -.
DR   KEGG; mtu:Rv3700c; -.
DR   PATRIC; fig|83332.111.peg.4115; -.
DR   TubercuList; Rv3700c; -.
DR   eggNOG; COG0520; Bacteria.
DR   InParanoid; O69668; -.
DR   OMA; GTSRKWL; -.
DR   PhylomeDB; O69668; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:1990411; F:hercynylcysteine sulfoxide lyase activity (ergothioneine-forming); IEA:RHEA.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR   GO; GO:0052704; P:ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide; ISS: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   1: Evidence at protein level;
KW   Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..390
FT                   /note="Probable hercynylcysteine sulfoxide lyase"
FT                   /id="PRO_0000413654"
FT   MOD_RES         215
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P23721"
SQ   SEQUENCE   390 AA;  40446 MW;  EE4C9BDCCAD5BF70 CRC64;
     MRRSGANSPA GDSLADRWRA ARPPVAGLHL DSAACSRQSF AALDAAAQHA RHEAEVGGYV
     AAEAAAAVLD AGRAAVAALS GLPDAEVVFT TGSLHALDLL LGSWPGENRT LACLPGEYGP
     NLAVMAAHGF DVRPLPTLQD GRVALDDAAF MLADDPPDLV HLTVVASHRG VAQPLAMVAQ
     LCTELKLPLV VDAAQGLGHV DCAVGADVTY ASSRKWIAGP RGVGVLAVRP ELMERLRARL
     PAPDWMPPLT VAQQLGFGEA NVAARVGFSV ALGEHLACGP QAIRARLAEL GDIARTVLAD
     VSGWRVVEAV DEPSAITTLA PIDGADPAAV RAWLLSQRRI VTTYAGVERA PLELPAPVLR
     ISPHVDNTAD DLDAFAEALV AATAATSGER