ID A0A161Z1I0_9NOCA Unreviewed; 281 AA.
AC A0A161Z1I0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=AWN90_38305 {ECO:0000313|EMBL:KZM72074.1};
OS Nocardia terpenica.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=455432 {ECO:0000313|EMBL:KZM72074.1, ECO:0000313|Proteomes:UP000076512};
RN [1] {ECO:0000313|EMBL:KZM72074.1, ECO:0000313|Proteomes:UP000076512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 0406 {ECO:0000313|EMBL:KZM72074.1,
RC ECO:0000313|Proteomes:UP000076512};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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:KZM72074.1}.
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DR EMBL; LWGR01000010; KZM72074.1; -; Genomic_DNA.
DR RefSeq; WP_067593414.1; NZ_KV411304.1.
DR AlphaFoldDB; A0A161Z1I0; -.
DR STRING; 455432.AWN90_38305; -.
DR OrthoDB; 9804310at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000076512; 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; 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:UP000076512};
KW Transferase {ECO:0000313|EMBL:KZM72074.1}.
FT DOMAIN 2..255
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 281 AA; 30261 MW; BF1F05087A6C80D6 CRC64;
MCRHLGYLGP AAPVGELLTR GTHSLREQGW APRDMRGGGT INADGFGVAW WVREPGDTLR
ASRYRNPAPI WTDPAVDEVL PQLWSTAVVA AVRSATVGMP VERSACAPFT HGRWAFSHNG
VVRDWQRVLT EVAAEFGVPS LLDAESRTDS AALWVIVRGL LETPGTAVGQ AADSFRAHDP
SVALARLARA VLARVPEARL NLLLSDGETL WATTVYHSLA VLVGEEAAVV ASEPYDDDPR
WRAVPEGRVV TVRPGSLVIA SLAGDDRGGD YLEAESERAR S
//