ID   Q0S4Q5_RHOJR            Unreviewed;       248 AA.
AC   Q0S4Q5;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=RHA1_ro05702 {ECO:0000313|EMBL:ABG97481.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG97481.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG97481.1; -; Genomic_DNA.
DR   RefSeq; WP_011597828.1; NC_008268.1.
DR   AlphaFoldDB; Q0S4Q5; -.
DR   KEGG; rha:RHA1_ro05702; -.
DR   PATRIC; fig|101510.16.peg.5746; -.
DR   eggNOG; COG0121; Bacteria.
DR   HOGENOM; CLU_042555_3_0_11; -.
DR   OrthoDB; 9804310at2; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000008710; 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:UP000008710}.
FT   DOMAIN          2..248
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   248 AA;  26884 MW;  E1F75A9499D3982E CRC64;
     MCRHLGYLGP EQSVGDLLSR GENSLLRQSY APRDMRGGGT VNADGFGVGW WGSGGFSRYR
     SAQPLWSDPV VRETLPNIRS RAVVAAARSA TVGMPVQHTA CAPFSDETWA FSHNGVVRGW
     PESLGALAAE LPVNDLLQLE APTDSAALWL LLRRALGEQD PEKAMSALVQ DVVAAAPNSR
     LNLLLGNGSE LWATTWHHSL SALVDDERAI VMSEPYDDNP AWQSIPDRHF VSARPGHLIV
     TPLEMGAR
//