ID A0A2A7N5D9_MYCAG Unreviewed; 426 AA.
AC A0A2A7N5D9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ECO:0000313|EMBL:GFG53976.1};
GN ORFNames=CQY20_11125 {ECO:0000313|EMBL:PEG39104.1}, MAGR_54170
GN {ECO:0000313|EMBL:GFG53976.1};
OS Mycolicibacterium agri (Mycobacterium agri).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=36811 {ECO:0000313|EMBL:PEG39104.1, ECO:0000313|Proteomes:UP000220914};
RN [1] {ECO:0000313|EMBL:PEG39104.1, ECO:0000313|Proteomes:UP000220914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG37673 {ECO:0000313|EMBL:PEG39104.1,
RC ECO:0000313|Proteomes:UP000220914};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GFG53976.1, ECO:0000313|Proteomes:UP000465302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 6377 {ECO:0000313|EMBL:GFG53976.1,
RC ECO:0000313|Proteomes:UP000465302};
RX PubMed=31287781;
RA Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA Iida T., Fujita J., Nakamura S.;
RT "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT species based on 7547 genomic profiles.";
RL Emerg. Microbes Infect. 8:1043-1053(2019).
RN [3] {ECO:0000313|EMBL:GFG53976.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 6377 {ECO:0000313|EMBL:GFG53976.1};
RA Matsumoto Y., Motooka D., Nakamura S.;
RL Submitted (FEB-2020) 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:PEG39104.1}.
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DR EMBL; BLKS01000001; GFG53976.1; -; Genomic_DNA.
DR EMBL; PDCP01000016; PEG39104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A7N5D9; -.
DR OrthoDB; 9768004at2; -.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000220914; Unassembled WGS sequence.
DR Proteomes; UP000465302; 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:UP000220914}.
FT DOMAIN 10..137
FT /note="DinB-like"
FT /evidence="ECO:0000259|Pfam:PF12867"
FT DOMAIN 168..424
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 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 409
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT BINDING 413
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
SQ SEQUENCE 426 AA; 47916 MW; B885B068C04F0A54 CRC64;
MTERETLALQ LTKARKRTLR LVEIDDAELR RQYDPLMSPL VWDLAHIGWQ EELWLLRDND
PRRPGMLAPD VERLYDAFQN PRASRVDLPL LPPSDARTYC ATVRDKTLGV LDALPDDDPA
AAFNFGLTVS HENQHDETML QALNLRSGPP LLDPGTPLPH GRPDVAGTSV LVPGGPFLLG
VDAVTEPLSL DNERPAHWVD VPSFRIARVP VTNGEWQQFI DDGGYRERRW WSERGWAHRK
QAGLVAPQLW NGDGTRTRFG HVEDIPADEP VQHITYFEAE AYAAWAGARL PTEIEWEKAC
AWDPATGARR RFPWGASEPT DSLANLGGHA LRPAPVGAYP AGASAYGAEQ MLGDVWEWTS
SPLRPWPGFT PMLYEQYSQP FFDGDYKVLR GGSWAVAADI LRPSFRNWDH PIRRQIFSGL
RLAWDA
//
