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Database: UniProt
Entry: A1UMV0_MYCSK
LinkDB: A1UMV0_MYCSK
Original site: A1UMV0_MYCSK 
ID   A1UMV0_MYCSK            Unreviewed;       235 AA.
AC   A1UMV0;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase {ECO:0000256|HAMAP-Rule:MF_02036};
DE            EC=3.5.1.118 {ECO:0000256|HAMAP-Rule:MF_02036};
DE   AltName: Full=Gamma-glutamyl hercynylcysteine S-oxide hydrolase {ECO:0000256|HAMAP-Rule:MF_02036};
GN   Name=egtC {ECO:0000256|HAMAP-Rule:MF_02036};
GN   OrderedLocusNames=Mkms_4969 {ECO:0000313|EMBL:ABL94158.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL94158.1};
RN   [1] {ECO:0000313|EMBL:ABL94158.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL94158.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_02036}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02036};
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02036}.
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DR   EMBL; CP000518; ABL94158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UMV0; -.
DR   STRING; 189918.Mkms_4969; -.
DR   KEGG; mkm:Mkms_4969; -.
DR   HOGENOM; CLU_042555_3_0_11; -.
DR   OMA; RRAGPIW; -.
DR   OrthoDB; 9804310at2; -.
DR   UniPathway; UPA01014; -.
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   CDD; cd01908; YafJ; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   HAMAP; MF_02036; EgtC; 1.
DR   InterPro; IPR017808; EgtC.
DR   InterPro; IPR032889; EgtC_Actinobacteria.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   NCBIfam; TIGR03442; ergothioneine biosynthesis protein EgtC; 1.
DR   PANTHER; PTHR43187:SF2; GAMMA-GLUTAMYL-HERCYNYLCYSTEINE SULFOXIDE HYDROLASE; 1.
DR   PANTHER; PTHR43187; GLUTAMINE AMIDOTRANSFERASE DUG3-RELATED; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|HAMAP-Rule:MF_02036};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_02036}.
FT   DOMAIN          2..235
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   235 AA;  24855 MW;  54B7C15D4A79C8AC CRC64;
     MCRHLGWLGA PRSVSALILD PPYGLLVQSY APRRQKHGLM NADGWGVGFF SSDLPDDAAP
     CRWRSAAPLW GDASFASVAP ALRSACVVGA VRSASIGMPI EPTASAPFTD GSWLLSHNGL
     VDRAVLPLSA HAESTVDSAL LAALIFDRGM DRLGDTVTEV GARDPGARLN ILAANGSQMV
     ATTWGDTLSV LRTDDGVALA SEPYDDDPRW EEIPDRHLVR TDGSSVQLSA LRGPA
//
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