ID A0A1Z2KWY2_9ACTN Unreviewed; 441 AA.
AC A0A1Z2KWY2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SMD11_0805 {ECO:0000313|EMBL:ARZ66471.1};
OS Streptomyces albireticuli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1940 {ECO:0000313|EMBL:ARZ66471.1, ECO:0000313|Proteomes:UP000195755};
RN [1] {ECO:0000313|EMBL:ARZ66471.1, ECO:0000313|Proteomes:UP000195755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK11 {ECO:0000313|EMBL:ARZ66471.1,
RC ECO:0000313|Proteomes:UP000195755};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Yao L., Wang C.;
RT "Streptomyces albireticuli Genome sequencing and assembly.";
RL Submitted (JUN-2017) 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}.
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DR EMBL; CP021744; ARZ66471.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z2KWY2; -.
DR KEGG; salj:SMD11_0805; -.
DR OrthoDB; 9768004at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000195755; 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; 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}.
FT DOMAIN 18..149
FT /note="DinB-like"
FT /evidence="ECO:0000259|Pfam:PF12867"
FT DOMAIN 178..436
FT /note="Sulfatase-modifying factor enzyme"
FT /evidence="ECO:0000259|Pfam:PF03781"
FT REGION 308..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 55
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 89..92
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 141
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 145
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 421
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 425
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
SQ SEQUENCE 441 AA; 49084 MW; 3551E464039B09FE CRC64;
MTVPESDPAA LRRRAADALR TARARTHALT GCVDGPELTA QHSPLMSPLV WDLAHIGNQE
EQWLLRTVGG REALRPEIDS VYDAFEHPRA ERPRLPLLAP EEARGYVADV RDRVLDVLER
VPLSGAPLLE AGFAFGMIAQ HEQQHDETML ITHQLRRGPA VLSAPEPPGA APDAGALPAE
VLIEGGPFTM GTSAEPWALD NERPAHARFV PSYFLDTLPV SNGAYLRFVE DGGYADARWW
RPGGWEQVRR HGLAAPLFWR REGTGWVRRR FGAEEPVPLE EPVLHVSWYE AAAYAAWAGR
RLPTEAEWEK AARHDPASGR SRRYPWGDAD PTPDRANLGQ RHLRPAPVGA YAAGASPLGV
RQLIGDVWEW TSSDFLPYPG FRAFPYREYS EVFFGEAHKV LRGGSFAVDP VACRGTFRNW
DLPVRRQIFA GFRTARDAEP S
//
