EGTB_MYCTO
ID EGTB_MYCTO Reviewed; 425 AA.
AC Q7D513;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Hercynine oxygenase {ECO:0000255|HAMAP-Rule:MF_02035};
DE EC=1.14.99.50 {ECO:0000255|HAMAP-Rule:MF_02035};
DE AltName: Full=Gamma-glutamyl hercynylcysteine S-oxide synthase {ECO:0000255|HAMAP-Rule:MF_02035};
GN Name=egtB {ECO:0000255|HAMAP-Rule:MF_02035}; OrderedLocusNames=MT3806;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP FUNCTION, PATHWAY, INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=26774486; DOI=10.1016/j.celrep.2015.12.056;
RA Saini V., Cumming B.M., Guidry L., Lamprecht D.A., Adamson J.H.,
RA Reddy V.P., Chinta K.C., Mazorodze J.H., Glasgow J.N.,
RA Richard-Greenblatt M., Gomez-Velasco A., Bach H., Av-Gay Y., Eoh H.,
RA Rhee K., Steyn A.J.;
RT "Ergothioneine maintains redox and bioenergetic homeostasis essential for
RT drug susceptibility and virulence of Mycobacterium tuberculosis.";
RL Cell Rep. 14:572-585(2016).
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 (ERG) (By similarity). ERG is one of the major redox
CC buffers which protects bacteria against redox stressors and
CC antibiotics; loss of ERG or mycothiol (MSH, the other major redox
CC buffer in this bacteria) leads to respiratory alterations and
CC bioenergetic deficiencies that negatively impact virulence
CC (PubMed:26774486). {ECO:0000255|HAMAP-Rule:MF_02035,
CC ECO:0000305|PubMed:26774486}.
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:0000255|HAMAP-Rule:MF_02035};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02035};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02035, ECO:0000305|PubMed:26774486}.
CC -!- INDUCTION: Expressed in log phase, part of the egtA-egtB-egtC-egtD
CC operon, which does not include egtE (PubMed:26774486).
CC {ECO:0000269|PubMed:26774486}.
CC -!- SIMILARITY: Belongs to the EgtB family. {ECO:0000255|HAMAP-
CC Rule:MF_02035}.
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DR EMBL; AE000516; AAK48173.1; -; Genomic_DNA.
DR RefSeq; WP_003899647.1; NZ_KK341227.1.
DR AlphaFoldDB; Q7D513; -.
DR SMR; Q7D513; -.
DR EnsemblBacteria; AAK48173; AAK48173; MT3806.
DR KEGG; mtc:MT3806; -.
DR PATRIC; fig|83331.31.peg.4098; -.
DR HOGENOM; CLU_012431_9_2_11; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0044875; F:gamma-glutamyl hercynylcysteine sulfoxide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT CHAIN 1..425
FT /note="Hercynine oxygenase"
FT /id="PRO_0000439070"
FT BINDING 46
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02035"
FT BINDING 82..85
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02035"
FT BINDING 129
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02035"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02035"
FT BINDING 408
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02035"
FT BINDING 412
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02035"
SQ SEQUENCE 425 AA; 47170 MW; F3F6CF6AF92AEA80 CRC64;
MTSPEQLACH LARARARTLR LVDFDDAELC CQYDPLMSPL VWDLAHIGQQ EELWLLRGGD
PGQPGLLPPA VEGLYDAFEH SRASRVELPL LSPARARSYC ATVRSAALDA LAALPEDGDS
FVFAMVISHE NQHDETMLQA LNLRTGSPLL AATSALPAGR PRMAGTSVLV AGGPFVLGVD
AADEPCSLDN ERQAHVVDVP AFRIGRVPVT NGEWQDFIDD GGYTQSRWWS ERGWQHRQRA
GLTAPQFWRS GGRTRTRFGH VEDIPADEPV QHVSYFEAEA YAAWAGARLP TEVEWEKACA
WDPATGSRRR YPWGTEEPTD TYANLGGQTL RPAPVGAYPA GASACGAEQM LGDVWEWTTS
PLRPWPGFVP MVYERYSQPF FGGDYRVLRG GSWAVEPAIL RPSFRNWDHP YRRQIFAGVR
LAWDI
