ID   EGTC_MYCTU              Reviewed;         233 AA.
AC   O69670; L0TF00;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 109.
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; OrderedLocusNames=Rv3702c;
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: 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. Ergothioneine is an antioxidant that protects
CC       mycobacteria from oxidative stress. {ECO:0000250|UniProtKB:A0R5M9,
CC       ECO:0000250|UniProtKB:Q8VIV2}.
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}.
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DR   EMBL; AL123456; CCP46527.1; -; Genomic_DNA.
DR   PIR; G70793; G70793.
DR   RefSeq; NP_218219.1; NC_000962.3.
DR   RefSeq; WP_003419806.1; NZ_NVQJ01000028.1.
DR   AlphaFoldDB; O69670; -.
DR   SMR; O69670; -.
DR   STRING; 83332.Rv3702c; -.
DR   PaxDb; O69670; -.
DR   DNASU; 885224; -.
DR   GeneID; 885224; -.
DR   KEGG; mtu:Rv3702c; -.
DR   TubercuList; Rv3702c; -.
DR   eggNOG; COG0121; Bacteria.
DR   InParanoid; O69670; -.
DR   OMA; FSHNGAV; -.
DR   PhylomeDB; O69670; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0061672; C:glutathione hydrolase complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
DR   GO; GO:0008242; F:omega peptidase activity; IBA:GO_Central.
DR   GO; GO:0052704; P:ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide; ISS:UniProtKB.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006751; P:glutathione catabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Glutamine amidotransferase; Hydrolase; Reference proteome.
FT   CHAIN           1..233
FT                   /note="Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase"
FT                   /id="PRO_0000413650"
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;  24627 MW;  F4371315DA610B63 CRC64;
     MCRHLGWLGA QVAVSSLVLD PPQGLRVQSY APRRQKHGLM NADGWGVGFF DGAIPRRWRS
     PAPLWGDTSF HSVAPALRSH CILAAVRSAT VGMPIEVSAT PPFTDGHWLL AHNGVVDRAV
     LPAGPAAESV CDSAILAATI FAHGLDALGD TIVKVGAADP NARLNILAAN GSRLIATTWG
     DTLSILRRAD GVVLASEPYD DDSGWGDVPD RHLVEVTQKG VTLTALDRAK GPR