EGTC_MYCS2
ID EGTC_MYCS2 Reviewed; 227 AA.
AC A0R5M9; I7FUF9;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase {ECO:0000305|PubMed:20420449};
DE EC=3.5.1.118 {ECO:0000269|PubMed:20420449};
DE AltName: Full=Gamma-glutamyl hercynylcysteine S-oxide hydrolase {ECO:0000305|PubMed:20420449};
GN Name=egtC {ECO:0000303|PubMed:20420449};
GN OrderedLocusNames=MSMEG_6248, MSMEI_6087;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, GENE NAME, AND PATHWAY.
RX PubMed=20420449; DOI=10.1021/ja101721e;
RA Seebeck F.P.;
RT "In vitro reconstitution of Mycobacterial ergothioneine biosynthesis.";
RL J. Am. Chem. Soc. 132:6632-6633(2010).
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:0000269|PubMed:20420449}.
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;
CC Evidence={ECO:0000269|PubMed:20420449};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000305|PubMed:20420449}.
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DR EMBL; CP000480; ABK74731.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42518.1; -; Genomic_DNA.
DR RefSeq; WP_011731157.1; NZ_SIJM01000027.1.
DR RefSeq; YP_890467.1; NC_008596.1.
DR PDB; 4ZFJ; X-ray; 1.75 A; A/B/C/D/E/F/G/H/I/J/K/L=1-227.
DR PDB; 4ZFK; X-ray; 1.82 A; A/B/C/D=1-227.
DR PDB; 4ZFL; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=2-227.
DR PDBsum; 4ZFJ; -.
DR PDBsum; 4ZFK; -.
DR PDBsum; 4ZFL; -.
DR AlphaFoldDB; A0R5M9; -.
DR SMR; A0R5M9; -.
DR STRING; 246196.MSMEI_6087; -.
DR EnsemblBacteria; ABK74731; ABK74731; MSMEG_6248.
DR EnsemblBacteria; AFP42518; AFP42518; MSMEI_6087.
DR GeneID; 66737531; -.
DR KEGG; msg:MSMEI_6087; -.
DR KEGG; msm:MSMEG_6248; -.
DR PATRIC; fig|246196.19.peg.6087; -.
DR eggNOG; COG0121; Bacteria.
DR OMA; FSHNGAV; -.
DR OrthoDB; 693464at2; -.
DR BioCyc; MetaCyc:MON-17986; -.
DR BRENDA; 3.5.1.118; 3512.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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:0052704; P:ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide; IDA:UniProtKB.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.20.10; -; 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 SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR03442; TIGR03442; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glutamine amidotransferase; Hydrolase; Reference proteome.
FT CHAIN 1..227
FT /note="Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase"
FT /id="PRO_0000413649"
FT DOMAIN 2..227
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 2
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT STRAND 3..13
FT /evidence="ECO:0007829|PDB:4ZFL"
FT HELIX 14..18
FT /evidence="ECO:0007829|PDB:4ZFL"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:4ZFL"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:4ZFL"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:4ZFL"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4ZFL"
FT HELIX 69..74
FT /evidence="ECO:0007829|PDB:4ZFL"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:4ZFL"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:4ZFL"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4ZFL"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:4ZFJ"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:4ZFL"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4ZFL"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:4ZFL"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:4ZFL"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:4ZFL"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:4ZFL"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:4ZFL"
FT STRAND 172..182
FT /evidence="ECO:0007829|PDB:4ZFL"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:4ZFL"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:4ZFL"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:4ZFL"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:4ZFL"
SQ SEQUENCE 227 AA; 24139 MW; 715B28231359B540 CRC64;
MCRHVAWLGA PRSLADLVLD PPQGLLVQSY APRRQKHGLM NADGWGAGFF DDEGVARRWR
SDKPLWGDAS FASVAPALRS RCVLAAVRSA TIGMPIEPSA SAPFSDGQWL LSHNGLVDRG
VLPLTGAAES TVDSAIVAAL IFSRGLDALG ATIAEVGELD PNARLNILAA NGSRLLATTW
GDTLSVLHRP DGVVLASEPY DDDPGWSDIP DRHLVDVRDA HVVVTPL
