ID A0A3R9VD65_9ACTN Unreviewed; 440 AA.
AC A0A3R9VD65;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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 ORFNames=EF918_14260 {ECO:0000313|EMBL:RSS80309.1};
OS Streptomyces sp. WAC06614.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2487416 {ECO:0000313|EMBL:RSS80309.1, ECO:0000313|Proteomes:UP000277644};
RN [1] {ECO:0000313|EMBL:RSS80309.1, ECO:0000313|Proteomes:UP000277644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC06614 {ECO:0000313|EMBL:RSS80309.1,
RC ECO:0000313|Proteomes:UP000277644};
RA Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT "Unmasking the antibiotic production potential of Actinomycetes through
RT CRISPR/Cas9 inactivate of ubiquitous gene clusters.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RSS80309.1}.
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DR EMBL; RPRY01000084; RSS80309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9VD65; -.
DR OrthoDB; 9768004at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000277644; Unassembled WGS sequence.
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; 1.20.120.450; dinb family like domain; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000277644}.
FT DOMAIN 20..151
FT /note="DinB-like"
FT /evidence="ECO:0000259|Pfam:PF12867"
FT DOMAIN 180..437
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
FT BINDING 57
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 91..94
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 143
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 422
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 426
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
SQ SEQUENCE 440 AA; 49162 MW; A0D6914BB5D6A525 CRC64;
MTTEAVRPAG PALRERALAA LTAARARTRL LTDAVTDEDL TAQHSPLMSP LVWDLAHIGN
QEELWLLRNV AGRDPLRPEI DPLYDAFAHP RADRPRLPLL GPAEARRYAA EVRGRVFDVL
ADSPLEGSPL LDAAFAFGMI AQHEQQHDET MLITHQLRRG EPVLSAPDPD PPAGPPPAVR
EVLVPGGPFT MGTSTEPWAL DNERPAHERE TVAFWIDTLP VTCADYQAFV ADGGYHEPSW
WAPEGWEQIR RHGIEAPLFW HREGTVWLRR RFGVTEPVPD DEPVLHVSWY EADAFARWAG
RRLPTEAEWE KAARHDPATG RSTRYPWGDA DPTPAHANLG QRHLRPAPAG SYPAGASPLG
VRQLIGDVWE WTASDFLPYP GFRAFPYREY SEVFFGPAHK VLRGGSFAVD PVACRGTFRN
WDLPVRRQIF SGFRTARDAA
//
