ID   EGTC_MYCTO              Reviewed;         233 AA.
AC   Q8VIV2;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase;
DE            EC=3.5.1.118 {ECO:0000250|UniProtKB:A0R5M9};
DE   AltName: Full=Gamma-glutamyl hercynylcysteine S-oxide hydrolase;
GN   Name=egtC {ECO:0000303|PubMed:26774486}; OrderedLocusNames=MT3805;
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, INDUCTION, 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: Catalyzes the hydrolysis of the gamma-glutamyl amide bond of
CC       hercynyl-gamma-L-glutamyl-L-cysteine sulfoxide to produce
CC       hercynylcysteine sulfoxide, a step in the biosynthesis pathway of
CC       ergothioneine (By similarity). ERG is one of the major redox buffers
CC       which protects bacteria against redox stressors and antibiotics; loss
CC       of ERG or mycothiol (MSH, the other major redox buffer in this
CC       bacteria) leads to respiratory alterations and bioenergetic
CC       deficiencies that negatively impact virulence (PubMed:26774486).
CC       {ECO:0000250|UniProtKB:A0R5M9, ECO:0000305|PubMed:26774486}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gamma-L-glutamyl-hercynylcysteine S-oxide + H2O = L-glutamate
CC         + S-(hercyn-2-yl)-L-cysteine S-oxide; Xref=Rhea:RHEA:42684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:82703,
CC         ChEBI:CHEBI:82706; EC=3.5.1.118;
CC         Evidence={ECO:0000250|UniProtKB:A0R5M9};
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000250|UniProtKB:A0R5M9, ECO:0000305|PubMed:26774486}.
CC   -!- INDUCTION: Expressed in log phase, part of the egtA-egtB-egtC-egtD
CC       operon, which does not include egtE (PubMed:26774486).
CC       {ECO:0000269|PubMed:26774486}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK48172.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK48172.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_042507709.1; NC_002755.2.
DR   AlphaFoldDB; Q8VIV2; -.
DR   SMR; Q8VIV2; -.
DR   EnsemblBacteria; AAK48172; AAK48172; MT3805.
DR   KEGG; mtc:MT3805; -.
DR   HOGENOM; CLU_042555_3_0_11; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
DR   GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_02036; EgtC; 1.
DR   InterPro; IPR017808; EgtC.
DR   InterPro; IPR026869; EgtC-like.
DR   InterPro; IPR032889; EgtC_Actinobacteria.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   Pfam; PF13230; GATase_4; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR03442; TIGR03442; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   2: Evidence at transcript level;
KW   Glutamine amidotransferase; Hydrolase.
FT   CHAIN           1..233
FT                   /note="Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase"
FT                   /id="PRO_0000439068"
FT   DOMAIN          2..233
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT   ACT_SITE        2
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
SQ   SEQUENCE   233 AA;  24601 MW;  A89C7EBEBE2416C8 CRC64;
     MCRHLGWLGA QVAVSSLVLD PPQGLRVQSY APRRQKHGLM NADGWGVGFF DGAIPRRWRS
     AAPLWGDTSF HSVAPALRSH CILAAVRSAT VGMPIEVSAT PPFTDGHWLL AHNGVVDRAV
     LPAGPAAESV CDSAILAATI FAHGLDALGD TIVKVGAADP NARLNILAAN GSRLIATTWG
     DTLSILRRAD GVVLASEPYD DDSGWGDVPD RHLVEVTQKG VTLTALDRAK GPR