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Database: UniProt
Entry: A0A0M2K1H5_9MYCO
LinkDB: A0A0M2K1H5_9MYCO
Original site: A0A0M2K1H5_9MYCO 
ID   A0A0M2K1H5_9MYCO        Unreviewed;       432 AA.
AC   A0A0M2K1H5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=WN67_16020 {ECO:0000313|EMBL:KKF00980.1};
OS   Mycolicibacterium obuense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1807 {ECO:0000313|EMBL:KKF00980.1, ECO:0000313|Proteomes:UP000034150};
RN   [1] {ECO:0000313|EMBL:KKF00980.1, ECO:0000313|Proteomes:UP000034150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UC1 {ECO:0000313|EMBL:KKF00980.1,
RC   ECO:0000313|Proteomes:UP000034150};
RA   Greninger A.L., Cunningham G., Chiu C.Y., Miller S.;
RT   "Genome sequence of Mycobacterium obuense UC1.";
RL   Submitted (APR-2015) 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:KKF00980.1}.
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DR   EMBL; LAUZ02000058; KKF00980.1; -; Genomic_DNA.
DR   RefSeq; WP_046364035.1; NZ_LAUZ02000058.1.
DR   AlphaFoldDB; A0A0M2K1H5; -.
DR   STRING; 1807.MOBUDSM44075_01335; -.
DR   PATRIC; fig|1807.13.peg.4292; -.
DR   OrthoDB; 9768004at2; -.
DR   UniPathway; UPA01014; -.
DR   Proteomes; UP000034150; 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}.
FT   DOMAIN          11..138
FT                   /note="DinB-like"
FT                   /evidence="ECO:0000259|Pfam:PF12867"
FT   DOMAIN          167..430
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         415
FT                   /ligand="gamma-L-glutamyl-L-cysteine"
FT                   /ligand_id="ChEBI:CHEBI:58173"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
FT   BINDING         419
FT                   /ligand="gamma-L-glutamyl-L-cysteine"
FT                   /ligand_id="ChEBI:CHEBI:58173"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02035"
SQ   SEQUENCE   432 AA;  48259 MW;  841E8BD017EAAFA0 CRC64;
     MTTRELLAEE LTTARHRTLR LVDFDDAEVR RQYDPLMSPL VWDLAHIGQQ EELWLLRGGN
     PDRPGMLTRQ VDQLYDAFVH SRASRVDLPL LPPADARAYC ATVRNKVLDA LDALPDDHPE
     AFTFGMVASH ENQHDETMLQ ALNLRSGAPL LDRGAALPAG RPGLAGTWVE VPAGEFVLGV
     DPAAEPFSLD NERPAHTVDV PAFRIGRVPV TNGEWQQFID DGGYDERRWW TDAGWAHRQQ
     AGVIAPQFWN TGTLAGTRTR FGHIEDIPAD EPVQHVDFHE AQAYAAWAGA RLPTEIEWEK
     ACAWDPEVGR RRRYPWGSDT PSAERVNLGG DALRPAPVGA YPGGASAYGA EQMLGDVWEW
     TTSTLRPWPG FAPMVYEQYS SPFFDGITSG DYRVLRGGSW AVAPGILRPS FRNWDHPIRR
     QIFSGVRLAW DV
//
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