ID   EGTE_MYCTO              Reviewed;         395 AA.
AC   Q7D515;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Probable hercynylcysteine sulfoxide lyase {ECO:0000255|HAMAP-Rule:MF_02038};
DE            EC=4.4.-.- {ECO:0000255|HAMAP-Rule:MF_02038};
GN   Name=egtE {ECO:0000255|HAMAP-Rule:MF_02038}; OrderedLocusNames=MT3803;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
RN   [2]
RP   FUNCTION, PATHWAY, AND OPERON STRUCTURE.
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=26774486; DOI=10.1016/j.celrep.2015.12.056;
RA   Saini V., Cumming B.M., Guidry L., Lamprecht D.A., Adamson J.H.,
RA   Reddy V.P., Chinta K.C., Mazorodze J.H., Glasgow J.N.,
RA   Richard-Greenblatt M., Gomez-Velasco A., Bach H., Av-Gay Y., Eoh H.,
RA   Rhee K., Steyn A.J.;
RT   "Ergothioneine maintains redox and bioenergetic homeostasis essential for
RT   drug susceptibility and virulence of Mycobacterium tuberculosis.";
RL   Cell Rep. 14:572-585(2016).
CC   -!- FUNCTION: Probably catalyzes the conversion of hercynylcysteine
CC       sulfoxide to ergothioneine (By similarity). ERG is one of the major
CC       redox buffers which protects bacteria against redox stressors and
CC       antibiotics; loss of ERG or mycothiol (MSH, the other major redox
CC       buffer in this bacteria) leads to respiratory alterations and
CC       bioenergetic deficiencies that negatively impact virulence
CC       (PubMed:26774486). {ECO:0000255|HAMAP-Rule:MF_02038,
CC       ECO:0000305|PubMed:26774486}.
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:0000255|HAMAP-Rule:MF_02038};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02038};
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02038, ECO:0000305|PubMed:26774486}.
CC   -!- INDUCTION: Not part of the egtA-egtB-egtC-egtD operon
CC       (PubMed:26774486). {ECO:0000269|PubMed:26774486}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. EgtE subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_02038}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000516; AAK48170.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7D515; -.
DR   SMR; Q7D515; -.
DR   EnsemblBacteria; AAK48170; AAK48170; MT3803.
DR   KEGG; mtc:MT3803; -.
DR   HOGENOM; CLU_003433_2_1_11; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:1990411; F:hercynylcysteine sulfoxide lyase activity (ergothioneine-forming); IEA:RHEA.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProt.
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   2: Evidence at transcript level;
KW   Lyase; Pyridoxal phosphate.
FT   CHAIN           1..395
FT                   /note="Probable hercynylcysteine sulfoxide lyase"
FT                   /id="PRO_0000439069"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         220
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02038"
SQ   SEQUENCE   395 AA;  41021 MW;  3243D27BE8EAFC1B CRC64;
     MQDEAMRRSG ANSPAGDSLA DRWRAARPPV AGLHLDSAAC SRQSFAALDA AAQHARHEAE
     VGGYVAAEAA AAVLDAGRAA VAALSGLPDA EVVFTTGSLH ALDLLLGSWP GENRTLACLP
     GEYGPNLAVM AAHGFDVRPL PTLQDGRVAL DDAAFMLADD PPDLVHLTVV ASHRGVAQPL
     AMVAQLCTEL KLPLVVDAAQ GLGHVDCAVG ADVTYASSRK WIAGPRGVGV LAVRPELMER
     LRARLPAPDW MPPLTVAQQL GFGEANVAAR VGFSVALGEH LACGPQAIRA RLAELGDIAR
     TVLADVSGWR VVEAVDEPSA ITTLAPIDGA DPAAVRAWLL SQRRIVTTYA GVERAPLELP
     APVLRISPHV DNTADDLDAF AEALVAATAA TSGER