EGTB_MYCT3
ID EGTB_MYCT3 Reviewed; 446 AA.
AC G7CFI3;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Hercynine oxygenase;
DE EC=1.14.99.50 {ECO:0000269|PubMed:25597398};
DE AltName: Full=Gamma-glutamyl hercynylcysteine S-oxide synthase {ECO:0000255|HAMAP-Rule:MF_02035};
DE AltName: Full=Sulfoxide synthase EgtB {ECO:0000303|PubMed:25597398};
GN Name=egtB {ECO:0000255|HAMAP-Rule:MF_02035};
GN ORFNames=KEK_08772 {ECO:0000312|EMBL:EHI13262.1};
OS Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP
OS 105390 / JCM 6362 / NCTC 10409 / 316) (Mycobacterium thermoresistibile).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1078020;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316;
RG Tuberculosis Structural Genomics Consortium;
RA Ioerger T.R.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 3-446 IN COMPLEXES WITH
RP N,N,N-TRIMETHYL-HISTIDINE; IRON; GAMMA-GLUTAMYLCYSTEINE; MANGANESE AND
RP N,N-DIMETHYL-HISTIDINE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, REACTION MECHANISM, AND MUTAGENESIS
RP OF ASP-416.
RX PubMed=25597398; DOI=10.1002/anie.201410045;
RA Goncharenko K.V., Vit A., Blankenfeldt W., Seebeck F.P.;
RT "Structure of the sulfoxide synthase EgtB from the ergothioneine
RT biosynthetic pathway.";
RL Angew. Chem. Int. Ed. 54:2821-2824(2015).
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:0000269|PubMed:25597398}.
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:0000269|PubMed:25597398};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:25597398};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=39 uM for hercynine {ECO:0000269|PubMed:25597398};
CC KM=44 uM for gamma-L-glutamyl-cysteine {ECO:0000269|PubMed:25597398};
CC KM=1.1 mM for N-glutaryl-cysteine {ECO:0000269|PubMed:25597398};
CC Note=kcat is 0.87 sec(-1) for the oxidative sulfurization of
CC hercynine with gamma-L-glutamyl-L-cysteine as sulfur donor. kcat is
CC 0.25 sec(-1) for the oxidative sulfurization of hercynine with N-
CC glutaryl-cysteine as sulfur donor. {ECO:0000269|PubMed:25597398};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000305|PubMed:25597398}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25597398}.
CC -!- SIMILARITY: Belongs to the EgtB family. {ECO:0000305}.
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DR EMBL; AGVE01000042; EHI13262.1; -; Genomic_DNA.
DR PDB; 4X8B; X-ray; 1.70 A; A/B=3-446.
DR PDB; 4X8D; X-ray; 1.98 A; A/B=3-446.
DR PDB; 4X8E; X-ray; 1.60 A; A/B=3-446.
DR PDBsum; 4X8B; -.
DR PDBsum; 4X8D; -.
DR PDBsum; 4X8E; -.
DR AlphaFoldDB; G7CFI3; -.
DR SMR; G7CFI3; -.
DR STRING; 1078020.KEK_08772; -.
DR PRIDE; G7CFI3; -.
DR EnsemblBacteria; EHI13262; EHI13262; KEK_08772.
DR PATRIC; fig|1078020.3.peg.1721; -.
DR eggNOG; COG1262; Bacteria.
DR OMA; CRGTFRN; -.
DR BRENDA; 1.14.99.50; 3515.
DR UniPathway; UPA01014; -.
DR Proteomes; UP000004915; 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; 3.90.1580.10; -; 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 Pfam; PF12867; DinB_2; 1.
DR Pfam; PF03781; FGE-sulfatase; 1.
DR SUPFAM; SSF109854; SSF109854; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR TIGRFAMs; TIGR03440; egtB_TIGR03440; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..446
FT /note="Hercynine oxygenase"
FT /id="PRO_0000433563"
FT BINDING 51
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:25597398,
FT ECO:0007744|PDB:4X8E"
FT BINDING 87..90
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000269|PubMed:25597398,
FT ECO:0007744|PDB:4X8D"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:25597398,
FT ECO:0007744|PDB:4X8E"
FT BINDING 138
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:25597398,
FT ECO:0007744|PDB:4X8E"
FT BINDING 416
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000269|PubMed:25597398,
FT ECO:0007744|PDB:4X8D"
FT BINDING 420
FT /ligand="gamma-L-glutamyl-L-cysteine"
FT /ligand_id="ChEBI:CHEBI:58173"
FT /evidence="ECO:0000269|PubMed:25597398,
FT ECO:0007744|PDB:4X8D"
FT MUTAGEN 416
FT /note="D->N: 200-fold reduction in affinity for gamma-
FT glutamylcysteine, but no significant change in that for
FT hercynine and in the reaction rate. Modifies the sulfur
FT donor specificity since N-glutaryl-cysteine is a 10-fold
FT better substrate than gamma-L-glutamyl-cysteine in the
FT mutant."
FT /evidence="ECO:0000269|PubMed:25597398"
FT HELIX 9..26
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 31..35
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4X8E"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 98..118
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 126..148
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:4X8E"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 279..289
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 296..304
FT /evidence="ECO:0007829|PDB:4X8E"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:4X8E"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 355..361
FT /evidence="ECO:0007829|PDB:4X8E"
FT TURN 378..381
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:4X8E"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:4X8E"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:4X8E"
SQ SEQUENCE 446 AA; 49412 MW; 09C16D506184D9D9 CRC64;
MTGVAVPHRA ELARQLIDAR NRTLRLVDFD DAELRRQYDP LMSPLVWDLA HIGQQEELWL
LRGGDPRRPG LLEPAVEQLY DAFVHPRASR VHLPLLSPAQ ARRFCATVRS AVLDALDRLP
EDADTFAFGM VVSHEHQHDE TMLQALNLRS GEPLLGSGTA LPPGRPGVAG TSVLVPGGPF
VLGVDLADEP YALDNERPAH VVDVPAFRIG RVPVTNAEWR AFIDDGGYRQ RRWWSDAGWA
YRCEAGLTAP QFWNPDGTRT RFGHVEDIPP DEPVQHVTYF EAEAYAAWAG ARLPTEIEWE
KACAWDPATG RRRRYPWGDA APTAALANLG GDALRPAPVG AYPAGASACG AEQMLGDVWE
WTSSPLRPWP GFTPMIYQRY SQPFFEGAGS GDYRVLRGGS WAVAADILRP SFRNWDHPIR
RQIFAGVRLA WDVDRQTARP GPVGGC
