ID D2S3Y1_GEOOG Unreviewed; 229 AA.
AC D2S3Y1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=Gobs_0203 {ECO:0000313|EMBL:ADB73009.1};
OS Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC
OS A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=526225 {ECO:0000313|EMBL:ADB73009.1, ECO:0000313|Proteomes:UP000001382};
RN [1] {ECO:0000313|EMBL:ADB73009.1, ECO:0000313|Proteomes:UP000001382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RX PubMed=21304698;
RA Ivanova N., Sikorski J., Jando M., Munk C., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Meincke L.,
RA Brettin T., Detter J.C., Detter J.C., Rohde M., Goeker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Geodermatophilus obscurus type strain (G-
RT 20).";
RL Stand. Genomic Sci. 2:158-167(2010).
RN [2] {ECO:0000313|Proteomes:UP000001382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M.,
RA Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Geodermatophilus obscurus DSM 43160.";
RL Submitted (JAN-2010) 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}.
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DR EMBL; CP001867; ADB73009.1; -; Genomic_DNA.
DR RefSeq; WP_012946450.1; NC_013757.1.
DR AlphaFoldDB; D2S3Y1; -.
DR STRING; 526225.Gobs_0203; -.
DR KEGG; gob:Gobs_0203; -.
DR eggNOG; COG0121; Bacteria.
DR HOGENOM; CLU_042555_3_0_11; -.
DR OrthoDB; 9804310at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000001382; 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; 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; 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:UP000001382}.
FT DOMAIN 2..229
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 229 AA; 24250 MW; 68BB2226CBB6651D CRC64;
MCRHLAWLGR PRTLSALVTE PPSSLLVQSY APRRQRYGTV NADGWGVGFF TPGRVQPARW
RSARPLWGDP SFASVAPVVS SGCVVAAVRS ATVGMPLEES AAAPFTDGRW LLSHNGRVDR
AVLPPVRDAE STVDSALLAA LVFDRGLDAL GATVREVGAA DPGARLNLLA ADGTRLLATT
WGDTLSALVT PDGTALASEP WDDDPRWADV PDHSLVEVTP DGLTLTPLP
//
