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Database: UniProt
Entry: Q744N7_MYCPA
LinkDB: Q744N7_MYCPA
Original site: Q744N7_MYCPA 
ID   Q744N7_MYCPA            Unreviewed;       232 AA.
AC   Q744N7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 90.
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=MAP_0304c {ECO:0000313|EMBL:AAS02621.1};
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS02621.1, ECO:0000313|Proteomes:UP000000580};
RN   [1] {ECO:0000313|EMBL:AAS02621.1, ECO:0000313|Proteomes:UP000000580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS02621.1; -; Genomic_DNA.
DR   RefSeq; WP_003873351.1; NZ_CP106873.1.
DR   AlphaFoldDB; Q744N7; -.
DR   STRING; 262316.MAP_0304c; -.
DR   KEGG; mpa:MAP_0304c; -.
DR   eggNOG; COG0121; Bacteria.
DR   HOGENOM; CLU_042555_3_0_11; -.
DR   OMA; RRAGPIW; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000000580; 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   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; IPR026869; EgtC-like.
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   Pfam; PF13230; GATase_4; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000580}.
FT   DOMAIN          2..232
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   232 AA;  24776 MW;  BDE10C151E21BE60 CRC64;
     MCRHLGWLGA DATVSSLMLE PPFGLRVQSY APRRQKHGLL NADGWGAGFF DAEVPRRWRS
     PAPLWGDVSF ESVAPALHSH CVVAAVRSAT VGMPIEISAT APFTDGRWLL SHNGVVDRSV
     LPVTSRAESV CDSAILAAVI LERGLDALGE VIVEIGAADP AARLNILAAN GSRLLATAWG
     DTLSILRRAD GVVVASEPYD DDSDWEDVPD RHLVDVTADG VTLTPLDHPK GF
//
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