ID A0A101S5V6_9ACTN Unreviewed; 257 AA.
AC A0A101S5V6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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_1 {ECO:0000313|EMBL:AYC36936.1};
GN Synonyms=egtC {ECO:0000256|HAMAP-Rule:MF_02036};
GN ORFNames=AQJ54_12880 {ECO:0000313|EMBL:KUN67926.1}, DWG14_01146
GN {ECO:0000313|EMBL:AYC36936.1};
OS Streptomyces griseorubiginosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67304 {ECO:0000313|EMBL:KUN67926.1, ECO:0000313|Proteomes:UP000054375};
RN [1] {ECO:0000313|EMBL:KUN67926.1, ECO:0000313|Proteomes:UP000054375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40469 {ECO:0000313|EMBL:KUN67926.1,
RC ECO:0000313|Proteomes:UP000054375};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseorubiginosus DSM 40469, type
RT strain for the species Streptomyces griseorubiginosus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AYC36936.1, ECO:0000313|Proteomes:UP000265765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3E-1 {ECO:0000313|EMBL:AYC36936.1,
RC ECO:0000313|Proteomes:UP000265765};
RA Kang H.J., Kim S.B.;
RT "Production of Trimethoprim by Streptomyces sp. 3E-1.";
RL Submitted (SEP-2018) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP032427; AYC36936.1; -; Genomic_DNA.
DR EMBL; LMWV01000007; KUN67926.1; -; Genomic_DNA.
DR RefSeq; WP_062237204.1; NZ_KQ948736.1.
DR AlphaFoldDB; A0A101S5V6; -.
DR KEGG; sge:DWG14_01146; -.
DR OrthoDB; 9804310at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000054375; Unassembled WGS sequence.
DR Proteomes; UP000265765; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:AYC36936.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054375};
KW Transferase {ECO:0000313|EMBL:KUN67926.1}.
FT DOMAIN 2..257
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 257 AA; 27724 MW; 55AF031973992FB2 CRC64;
MCRHLAWLGP EEPLGRLLVE PPHSLYRQSW APRRQRHGTV NADGFGVGWY AEGDPVPARY
RRAGPIWADL SFADLARVVR SPAVLAAVRD ATLAGADAEA AAAPYASGPW LFSHNGAVKG
WPDSLAPLTG TVPPADLLSM EARNDSAFVW ALVLNRLRGG DEEGQALADT VLEVAEAAPG
SRLNLLLTNG ESIAATAWGD TLWYLQRAGL GTVVASEPYD DDPHWQEVPD RTLLAASRTD
VLLTPLKSLE PLKEPRT
//