ID A4T5Y8_MYCGI Unreviewed; 429 AA.
AC A4T5Y8;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Hercynine oxygenase {ECO:0000256|HAMAP-Rule:MF_02035};
DE EC=1.14.99.50 {ECO:0000256|HAMAP-Rule:MF_02035};
DE AltName: Full=Gamma-glutamyl hercynylcysteine S-oxide synthase {ECO:0000256|HAMAP-Rule:MF_02035};
GN Name=egtB {ECO:0000256|HAMAP-Rule:MF_02035};
GN OrderedLocusNames=Mflv_1316 {ECO:0000313|EMBL:ABP43798.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP43798.1};
RN [1] {ECO:0000313|EMBL:ABP43798.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43798.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP43798.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43798.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
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. {ECO:0000256|HAMAP-Rule:MF_02035}.
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:0000256|HAMAP-Rule:MF_02035};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02035};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00037882, ECO:0000256|HAMAP-Rule:MF_02035}.
CC -!- SIMILARITY: Belongs to the EgtB family. {ECO:0000256|HAMAP-
CC Rule:MF_02035}.
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DR EMBL; CP000656; ABP43798.1; -; Genomic_DNA.
DR AlphaFoldDB; A4T5Y8; -.
DR STRING; 350054.Mflv_1316; -.
DR KEGG; mgi:Mflv_1316; -.
DR eggNOG; COG1262; Bacteria.
DR HOGENOM; CLU_012431_9_2_11; -.
DR OrthoDB; 9768004at2; -.
DR UniPathway; UPA01014; -.
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; paralog of FGE (formylglycine-generating enzyme); 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 NCBIfam; TIGR03440; egtB_TIGR03440; 1.
DR PANTHER; PTHR23150:SF36; HERCYNINE OXYGENASE; 1.
DR PANTHER; PTHR23150; SULFATASE MODIFYING FACTOR 1, 2; 1.
DR Pfam; PF12867; DinB_2; 1.
DR Pfam; PF03781; FGE-sulfatase; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF109854; DinB/YfiT-like putative metalloenzymes; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_02035};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02035};
KW Monooxygenase {ECO:0000256|HAMAP-Rule:MF_02035};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_02035}.
FT DOMAIN 11..138
FT /note="DinB-like"
FT /evidence="ECO:0000259|Pfam:PF12867"
FT DOMAIN 167..427
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
FT BINDING 46
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 82..85
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 130
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 412
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 416
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
SQ SEQUENCE 429 AA; 47716 MW; B4705926D93DC3F2 CRC64;
MTTRETLAGE LIRARDRTLR LVDFDDAELR RQYDPLMSPL VWDLAHIGQQ EELWLLRGGD
PQRPGLLSAE VDQLYDAFVH SRAARVDLPL LPPTDARNYC ATVRGRALDT LEALPDGHPD
EFAYALVISH ENQHDETMLQ ALSLRSGAPL LDRGDPLPPG RSGVAGTSVL VTGGEFVLGV
DAVTEPFSLD NERPAHTVDV PDFRIGRVPV TNAEWRQFLD DGGYAQRRWW SDAGWTHRQQ
AGLTRPLFWN ADGTRTRFGH VEDIPGDEPV QHVTYYEAQA YAAWAGARLP TEIEWEKACA
WDPATGARRR FPWGTAEPTA DVANLGGGAL RPAPVGAFPA SASACGAEQM LGDVWEWTSS
PLRPWPGFTP MIYRQYSEPF FDGTASGEYR VLRGGSWAVA AGILRPSFRN WDHPIRRQIF
SGVRLAWDV
//
