EGTB_MYCS2
ID EGTB_MYCS2 Reviewed; 428 AA.
AC A0R5N0; I7GG92;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Hercynine oxygenase {ECO:0000255|HAMAP-Rule:MF_02035};
DE EC=1.14.99.50 {ECO:0000269|PubMed:20420449, ECO:0000269|PubMed:25597398};
DE AltName: Full=Gamma-glutamyl hercynylcysteine S-oxide synthase {ECO:0000255|HAMAP-Rule:MF_02035};
GN Name=egtB {ECO:0000303|PubMed:20420449};
GN OrderedLocusNames=MSMEG_6249, MSMEI_6088;
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, COFACTOR, SUBSTRATE SPECIFICITY, GENE NAME,
RP 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).
RN [5]
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP REACTION MECHANISM.
RX PubMed=25597398; DOI=10.1002/anie.201410045;
RA Goncharenko K.V., Vit A., Blankenfeldt W., Seebeck F.P.;
RT "Structure of the sulfoxide synthase EgtB from the ergothioneine
RT biosynthetic pathway.";
RL Angew. Chem. Int. Ed. 54:2821-2824(2015).
CC -!- FUNCTION: Catalyzes the oxidative sulfurization of hercynine (N-
CC alpha,N-alpha,N-alpha-trimethyl-L-histidine) into hercynyl-gamma-L-
CC glutamyl-L-cysteine sulfoxide, a step in the biosynthesis pathway of
CC ergothioneine. Cannot use the alternative thiols cysteine, N-
CC acetylcysteine, or glutathione instead of gamma-glutamylcysteine as
CC substrates, and histidine is a poor sulfur acceptor substrate compared
CC to hercynine. {ECO:0000269|PubMed:20420449}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-L-glutamyl-L-cysteine + hercynine + O2 = gamma-L-
CC glutamyl-hercynylcysteine S-oxide + H2O; Xref=Rhea:RHEA:42672,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:15781,
CC ChEBI:CHEBI:58173, ChEBI:CHEBI:82703; EC=1.14.99.50;
CC Evidence={ECO:0000269|PubMed:20420449, ECO:0000269|PubMed:25597398};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:20420449, ECO:0000269|PubMed:25597398};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=43 uM for hercynine {ECO:0000269|PubMed:25597398};
CC KM=78 uM for gamma-L-glutamyl-cysteine {ECO:0000269|PubMed:25597398};
CC Note=kcat is 1.2 sec(-1). {ECO:0000269|PubMed:25597398};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000305|PubMed:20420449}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25597398}.
CC -!- SIMILARITY: Belongs to the EgtB family. {ECO:0000305}.
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DR EMBL; CP000480; ABK70251.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42519.1; -; Genomic_DNA.
DR RefSeq; WP_011731158.1; NZ_SIJM01000027.1.
DR RefSeq; YP_890468.1; NC_008596.1.
DR AlphaFoldDB; A0R5N0; -.
DR SMR; A0R5N0; -.
DR STRING; 246196.MSMEI_6088; -.
DR EnsemblBacteria; ABK70251; ABK70251; MSMEG_6249.
DR EnsemblBacteria; AFP42519; AFP42519; MSMEI_6088.
DR GeneID; 66737532; -.
DR KEGG; msg:MSMEI_6088; -.
DR KEGG; msm:MSMEG_6249; -.
DR PATRIC; fig|246196.19.peg.6088; -.
DR eggNOG; COG1262; Bacteria.
DR OMA; CRGTFRN; -.
DR OrthoDB; 1377603at2; -.
DR BioCyc; MetaCyc:MON-17985; -.
DR BRENDA; 1.14.99.50; 3512.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
DR GO; GO:0044875; F:gamma-glutamyl hercynylcysteine sulfoxide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0052704; P:ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide; IDA:UniProtKB.
DR Gene3D; 1.20.120.450; -; 1.
DR Gene3D; 3.90.1580.10; -; 1.
DR HAMAP; MF_02035; EgtB; 1.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR024775; DinB-like.
DR InterPro; IPR034660; DinB/YfiT-like.
DR InterPro; IPR017806; EgtB.
DR InterPro; IPR032890; EgtB_Actinobacteria.
DR InterPro; IPR005532; SUMF_dom.
DR InterPro; IPR042095; SUMF_sf.
DR Pfam; PF12867; DinB_2; 1.
DR Pfam; PF03781; FGE-sulfatase; 1.
DR SUPFAM; SSF109854; SSF109854; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR TIGRFAMs; TIGR03440; egtB_TIGR03440; 1.
PE 1: Evidence at protein level;
KW Iron; Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..428
FT /note="Hercynine oxygenase"
FT /id="PRO_0000413647"
FT BINDING 46
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:G7CFI3"
FT BINDING 82..85
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000250|UniProtKB:G7CFI3"
FT BINDING 129
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:G7CFI3"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:G7CFI3"
FT BINDING 411
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000250|UniProtKB:G7CFI3"
FT BINDING 415
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000250|UniProtKB:G7CFI3"
SQ SEQUENCE 428 AA; 47766 MW; 96ECEB89337CE85A CRC64;
MIARETLADE LALARERTLR LVEFDDAELH RQYNPLMSPL VWDLAHIGQQ EELWLLRDGN
PDRPGMLAPE VDRLYDAFEH SRASRVNLPL LPPSDARAYC ATVRAKALDT LDTLPEDDPG
FRFALVISHE NQHDETMLQA LNLREGPPLL DTGIPLPAGR PGVAGTSVLV PGGPFVLGVD
ALTEPHSLDN ERPAHVVDIP SFRIGRVPVT NAEWREFIDD GGYDQPRWWS PRGWAHRQEA
GLVAPQFWNP DGTRTRFGHI EEIPGDEPVQ HVTFFEAEAY AAWAGARLPT EIEWEKACAW
DPVAGARRRF PWGSAQPSAA LANLGGDARR PAPVGAYPAG ASAYGAEQML GDVWEWTSSP
LRPWPGFTPM IYERYSTPFF EGTTSGDYRV LRGGSWAVAP GILRPSFRNW DHPIRRQIFS
GVRLAWDV
