EGTB_MYCTU
ID EGTB_MYCTU Reviewed; 425 AA.
AC O69671; L0TDB1;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Hercynine oxygenase;
DE EC=1.14.99.50 {ECO:0000250|UniProtKB:A0R5N0};
DE AltName: Full=Gamma-glutamyl hercynylcysteine S-oxide synthase {ECO:0000250|UniProtKB:A0R5N0};
GN Name=egtB; OrderedLocusNames=Rv3703c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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. Ergothioneine is an antioxidant that protects
CC mycobacteria from oxidative stress. {ECO:0000250|UniProtKB:A0R5N0,
CC ECO:0000250|UniProtKB:Q7D513}.
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:0000250|UniProtKB:A0R5N0};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:A0R5N0};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000250|UniProtKB:A0R5N0}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:A0R5N0}.
CC -!- SIMILARITY: Belongs to the EgtB family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46528.1; -; Genomic_DNA.
DR PIR; H70793; H70793.
DR RefSeq; NP_218220.1; NC_000962.3.
DR RefSeq; WP_003419808.1; NZ_NVQJ01000028.1.
DR AlphaFoldDB; O69671; -.
DR SMR; O69671; -.
DR STRING; 83332.Rv3703c; -.
DR PaxDb; O69671; -.
DR DNASU; 885128; -.
DR GeneID; 45427701; -.
DR GeneID; 885128; -.
DR KEGG; mtu:Rv3703c; -.
DR TubercuList; Rv3703c; -.
DR eggNOG; COG1262; Bacteria.
DR InParanoid; O69671; -.
DR OMA; CRGTFRN; -.
DR PhylomeDB; O69671; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0008198; F:ferrous iron binding; ISS: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; ISS:UniProtKB.
DR GO; GO:0052704; P:ergothioneine biosynthesis from histidine via gamma-glutamyl-hercynylcysteine sulfoxide; ISS:UniProtKB.
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..425
FT /note="Hercynine oxygenase"
FT /id="PRO_0000413648"
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 408
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000250|UniProtKB:G7CFI3"
FT BINDING 412
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000250|UniProtKB:G7CFI3"
SQ SEQUENCE 425 AA; 47139 MW; D8CB6CB0C41E39CD CRC64;
MTSPEQLACH LARARARTLR LVDFDDAELC CQYDPLMSPL VWDLAHIGQQ EELWLLRGGD
PGQPGLLPPA VEGLYDAFEH SRASRVELPL LSPARARSYC ATVRSAALDA LAALPEDGDS
FVFAMVISHE NQHDETMLQA LNLRTGSPLL AATSALPAGR PRMAGTSVLV AGGPFVLGVD
AADEPCSLDN ERPAHVVDVP AFRIGRVPVT NGEWQDFIDD GGYTQSRWWS ERGWQHRQRA
GLTAPQFWRS GGRTRTRFGH VEDIPADEPV QHVSYFEAEA YAAWAGARLP TEVEWEKACA
WDPATGSRRR YPWGTEEPTD TYANLGGQTL RPAPVGAYPA GASACGAEQM LGDVWEWTTS
PLRPWPGFVP MVYERYSQPF FGGDYRVLRG GSWAVEPAIL RPSFRNWDHP YRRQIFAGVR
LAWDI
