ID A0A0M8YEZ0_9ACTN Unreviewed; 279 AA.
AC A0A0M8YEZ0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ORFNames=ADL05_00735 {ECO:0000313|EMBL:KOX24145.1};
OS Nocardiopsis sp. NRRL B-16309.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1519494 {ECO:0000313|EMBL:KOX24145.1, ECO:0000313|Proteomes:UP000037694};
RN [1] {ECO:0000313|Proteomes:UP000037694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16309 {ECO:0000313|Proteomes:UP000037694};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOX24145.1}.
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DR EMBL; LGEC01000002; KOX24145.1; -; Genomic_DNA.
DR RefSeq; WP_053614858.1; NZ_LGEC01000002.1.
DR AlphaFoldDB; A0A0M8YEZ0; -.
DR STRING; 1519494.ADL05_00735; -.
DR PATRIC; fig|1519494.3.peg.161; -.
DR OrthoDB; 9804310at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000037694; Unassembled WGS sequence.
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; IPR032889; EgtC_Actinobacteria.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR43187:SF2; GAMMA-GLUTAMYL-HERCYNYLCYSTEINE SULFOXIDE HYDROLASE; 1.
DR PANTHER; PTHR43187; GLUTAMINE AMIDOTRANSFERASE DUG3-RELATED; 1.
DR Pfam; PF13522; GATase_6; 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:UP000037694};
KW Transferase {ECO:0000313|EMBL:KOX24145.1}.
FT DOMAIN 2..279
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT REGION 56..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 29095 MW; A0411B169AC7AED7 CRC64;
MCRHLAYLGP PRTLHALLYA APHSLHVQSW APRRQRYGTV NADGFGVGWY PEPEASAGAA
PTGSSSAPGA QEAPGALGAP VPTWAPLRYR RAMPIWGDAS FADAARAISS GCVVAAVRDA
TIGFGSEESG AQPFRADRLL FSHNGAVKDD EALAAALSAP PPPGVLDARA PVDSAPLFAH
TVRLWRASGD LPGTLAAVVR HAREHSEGRY NLLASDGGTI VGTAAGDTLF TLREPDGGVF
VASEPFDDAP GWREVPDGSV VVASADRTEV HQIAEQSPQ
//
