ID Q2J4D3_FRACC Unreviewed; 245 AA.
AC Q2J4D3;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=Francci3_4513 {ECO:0000313|EMBL:ABD13859.1};
OS Frankia casuarinae (strain DSM 45818 / CECT 9043 / HFP020203 / CcI3).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=106370 {ECO:0000313|EMBL:ABD13859.1, ECO:0000313|Proteomes:UP000001937};
RN [1] {ECO:0000313|EMBL:ABD13859.1, ECO:0000313|Proteomes:UP000001937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45818 / CECT 9043 / CcI3
RC {ECO:0000313|Proteomes:UP000001937};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CP000249; ABD13859.1; -; Genomic_DNA.
DR RefSeq; WP_011438867.1; NZ_LRTJ01000004.1.
DR AlphaFoldDB; Q2J4D3; -.
DR STRING; 106370.Francci3_4513; -.
DR KEGG; fra:Francci3_4513; -.
DR eggNOG; COG0121; Bacteria.
DR HOGENOM; CLU_042555_3_0_11; -.
DR OrthoDB; 9804310at2; -.
DR PhylomeDB; Q2J4D3; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000001937; 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:UP000001937}.
FT DOMAIN 2..245
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
SQ SEQUENCE 245 AA; 26554 MW; 5B79FA51E6D76758 CRC64;
MCRHLAWIGT PRTLAGLTLE RPYSLLRQSW SPRRMRHGTV NADGFGVGWY APALRAAPAR
FRRAVPMWTD ASYASIAGAV ASGCVLAAVR SATVGMPIEE SATAPFTDGH RLLSHNGRVD
PVAVRRMLRD RPDAPVPDST CDSALLAALV WEHAGKRPLA EAVAEVVLSL DAAGSGERAR
LNLLVVDGTQ IVATAWRDSL SYRREKDGVL VASEPDDDEP GWVDVPDHHL LVADTHQVTL
RNMIS
//
