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Ergothioneine biosynthesis protein 1 [Includes: L-histidine N(alpha)-methyltransferase (EC 2.1.1.44); Hercynylcysteine S-oxide synthase (EC 1.14.99.51)]

 EGT1_NEUCR              Reviewed;         876 AA.
Q7RX33;
09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
22-JAN-2014, sequence version 3.
25-APR-2018, entry version 82.
RecName: Full=Ergothioneine biosynthesis protein 1 {ECO:0000303|PubMed:22209968};
Includes:
RecName: Full=L-histidine N(alpha)-methyltransferase {ECO:0000305|PubMed:5484456};
EC=2.1.1.44 {ECO:0000305|PubMed:5484456};
Includes:
RecName: Full=Hercynylcysteine S-oxide synthase {ECO:0000305|PubMed:4276459};
EC=1.14.99.51 {ECO:0000269|PubMed:25275953, ECO:0000305|PubMed:4276459};
Name=egt-1 {ECO:0000303|PubMed:22209968}; ORFNames=NCU04343;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
[2]
CATALYTIC ACTIVITY.
PubMed=5484456;
Ishikawa Y., Melville D.B.;
"The enzymatic alpha-N-methylation of histidine.";
J. Biol. Chem. 245:5967-5973(1970).
[3]
CATALYTIC ACTIVITY.
PubMed=4276459;
Ishikawa Y., Israel S.E., Melville D.B.;
"Participation of an intermediate sulfoxide in the enzymatic
thiolation of the imidazole ring of hercynine to form ergothioneine.";
J. Biol. Chem. 249:4420-4427(1974).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22209968; DOI=10.1016/j.fgb.2011.12.007;
Bello M.H., Barrera-Perez V., Morin D., Epstein L.;
"The Neurospora crassa mutant NcDeltaEgt-1 identifies an ergothioneine
biosynthetic gene and demonstrates that ergothioneine enhances
conidial survival and protects against peroxide toxicity during
conidial germination.";
Fungal Genet. Biol. 49:160-172(2012).
[5]
FUNCTION.
PubMed=25446508; DOI=10.1016/j.fgb.2014.10.007;
Bello M.H., Mogannam J.C., Morin D., Epstein L.;
"Endogenous ergothioneine is required for wild type levels of
conidiogenesis and conidial survival but does not protect against 254
nm UV-induced mutagenesis or kill.";
Fungal Genet. Biol. 73:120-127(2014).
[6]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
PubMed=25275953; DOI=10.1021/ol502596z;
Hu W., Song H., Sae Her A., Bak D.W., Naowarojna N., Elliott S.J.,
Qin L., Chen X., Liu P.;
"Bioinformatic and biochemical characterizations of C-S bond formation
and cleavage enzymes in the fungus Neurospora crassa ergothioneine
biosynthetic pathway.";
Org. Lett. 16:5382-5385(2014).
-!- FUNCTION: Catalyzes the SAM-dependent triple methylation of the
alpha-amino group of histidine to form hercynine and subsequent
conjugation with cysteine and oxygen to form hercynylcysteine
sulfoxide, the first two steps in the biosynthesis pathway of
ergothioneine (PubMed:22209968). Ergothioneine is an antioxidant
against peroxide in conidia and contributes to conidial longevity
(PubMed:22209968, PubMed:25446508). {ECO:0000269|PubMed:22209968,
ECO:0000269|PubMed:25446508}.
-!- CATALYTIC ACTIVITY: 3 S-adenosyl-L-methionine + L-histidine = 3 S-
adenosyl-L-homocysteine + hercynine. {ECO:0000305|PubMed:5484456}.
-!- CATALYTIC ACTIVITY: Hercynine + L-cysteine + O(2) = S-hercyn-2-yl-
L-cysteine S-oxide + H(2)O. {ECO:0000269|PubMed:25275953,
ECO:0000305|PubMed:4276459}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:25275953};
Note=Binds 1 Fe(2+) ion per monomer.
{ECO:0000269|PubMed:25275953};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=436 uM for hercynine {ECO:0000269|PubMed:25275953};
KM=603 uM for cysteine {ECO:0000269|PubMed:25275953};
-!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
{ECO:0000269|PubMed:22209968}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O94632}.
Nucleus {ECO:0000250|UniProtKB:O94632}.
-!- DISRUPTION PHENOTYPE: Does not produce ergothioneine in either
conidia nor mycelia. {ECO:0000269|PubMed:22209968}.
-!- SIMILARITY: In the N-terminal section; belongs to the
methyltransferase superfamily. EgtD family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the EgtB family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CM002239; EAA27088.3; -; Genomic_DNA.
RefSeq; XP_956324.3; XM_951231.3.
EnsemblFungi; EAA27088; EAA27088; NCU04343.
GeneID; 3872471; -.
KEGG; ncr:NCU04343; -.
EuPathDB; FungiDB:NCU04343; -.
HOGENOM; HOG000167160; -.
InParanoid; Q7RX33; -.
KO; K20246; -.
OrthoDB; EOG092C3SV3; -.
BioCyc; MetaCyc:MONOMER-18845; -.
UniPathway; UPA01014; -.
Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0030745; F:dimethylhistidine N-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0052699; P:ergothioneine biosynthetic process; IEA:UniProtKB-UniPathway.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR019257; MeTrfase_dom.
InterPro; IPR017805; SAM_MeTrfase_EsaF-type_put.
InterPro; IPR005532; SUMF_dom.
Pfam; PF03781; FGE-sulfatase; 2.
Pfam; PF10017; Methyltransf_33; 1.
SUPFAM; SSF56436; SSF56436; 2.
TIGRFAMs; TIGR03439; methyl_EasF; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Iron; Metal-binding; Methyltransferase;
Nucleus; Oxidoreductase; Reference proteome; S-adenosyl-L-methionine;
Transferase.
CHAIN 1 876 Ergothioneine biosynthesis protein 1.
/FTId=PRO_0000434987.
REGION 36 350 L-histidine N(alpha)-methyltransferase.
{ECO:0000305}.
REGION 315 317 L-histidine binding.
{ECO:0000250|UniProtKB:A0R5M8}.
REGION 378 874 Hercynylcysteine S-oxide synthase.
{ECO:0000305}.
METAL 413 413 Iron; via tele nitrogen.
{ECO:0000250|UniProtKB:G7CFI3}.
METAL 506 506 Iron; via tele nitrogen.
{ECO:0000250|UniProtKB:G7CFI3}.
METAL 510 510 Iron; via tele nitrogen.
{ECO:0000250|UniProtKB:G7CFI3}.
BINDING 88 88 L-histidine.
{ECO:0000250|UniProtKB:A0R5M8}.
BINDING 119 119 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:A0R5M8}.
BINDING 125 125 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:A0R5M8}.
BINDING 146 146 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:A0R5M8}.
BINDING 202 202 L-histidine.
{ECO:0000250|UniProtKB:A0R5M8}.
BINDING 242 242 L-histidine.
{ECO:0000250|UniProtKB:A0R5M8}.
SEQUENCE 876 AA; 99025 MW; 694FEB44522B96BD CRC64;
MPSAESMTPS SALGQLKATG QHVLSKLQQQ TSNADIIDIR RVAVEINLKT EITSMFRPKD
GPRQLPTLLL YNERGLQLFE RITYLEEYYL TNDEIKILTK HATEMASFIP SGAMIIELGS
GNLRKVNLLL EALDNAGKAI DYYALDLSRE ELERTLAQVP SYKHVKCHGL LGTYDDGRDW
LKAPENINKQ KCILHLGSSI GNFNRSDAAT FLKGFTDVLG PNDKMLIGVD ACNDPARVYH
AYNDKVGITH EFILNGLRNA NEIIGETAFI EGDWRVIGEY VYDEEGGRHQ AFYAPTRDTM
VMGELIRSHD RIQIEQSLKY SKEESERLWS TAGLEQVSEW TYGNEYGLHL LAKSRMSFSL
IPSVYARSAL PTLDDWEALW ATWDVVTRQM LPQEELLEKP IKLRNACIFY LGHIPTFLDI
QLTKTTKQAP SEPAHFCKIF ERGIDPDVDN PELCHAHSEI PDEWPPVEEI LTYQETVRSR
LRGLYAHGIA NIPRNVGRAI WVGFEHELMH IETLLYMMLQ SDKTLIPTHI PRPDFDKLAR
KAESERVPNQ WFKIPAQEIT IGLDDPEDGS DINKHYGWDN EKPPRRVQVA AFQAQGRPIT
NEEYAQYLLE KNIDKLPASW ARLDNENISN GTTNSVSGHH SNRTSKQQLP SSFLEKTAVR
TVYGLVPLKH ALDWPVFASY DELAGCAAYM GGRIPTFEET RSIYAYADAL KKKKEAERQL
GRTVPAVNAH LTNNGVEITP PSSPSSETPA ESSSPSDSNT TLITTEDLFS DLDGANVGFH
NWHPMPITSK GNTLVGQGEL GGVWEWTSSV LRKWEGFEPM ELYPGYTADF FDEKHNIVLG
GSWATHPRIA GRKSFVNWYQ RNYPYAWVGA RVVRDL


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