EGT1_SCHPO
ID EGT1_SCHPO Reviewed; 773 AA.
AC O94632; O94367; Q1MTP5;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 4.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ergothioneine biosynthesis protein 1 {ECO:0000303|PubMed:24828577};
DE AltName: Full=Meiotically up-regulated gene 158 protein {ECO:0000303|PubMed:16303567};
DE Includes:
DE RecName: Full=L-histidine N(alpha)-methyltransferase {ECO:0000250|UniProtKB:Q7RX33};
DE EC=2.1.1.44 {ECO:0000250|UniProtKB:Q7RX33};
DE Includes:
DE RecName: Full=Hercynylcysteine S-oxide synthase {ECO:0000250|UniProtKB:Q7RX33};
DE EC=1.14.99.51 {ECO:0000250|UniProtKB:Q7RX33};
GN Name=egt1 {ECO:0000303|PubMed:24828577};
GN Synonyms=mug158 {ECO:0000303|PubMed:16303567};
GN ORFNames=SPBC1604.01 {ECO:0000312|PomBase:SPBC1604.01}, SPBC1677.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24828577; DOI=10.1371/journal.pone.0097774;
RA Pluskal T., Ueno M., Yanagida M.;
RT "Genetic and metabolomic dissection of the ergothioneine and selenoneine
RT biosynthetic pathway in the fission yeast, S. pombe, and construction of an
RT overproduction system.";
RL PLoS ONE 9:E97774-E97774(2014).
CC -!- FUNCTION: Catalyzes the SAM-dependent triple methylation of the alpha-
CC amino group of histidine to form hercynine and subsequent conjugation
CC with cysteine and oxygen to form hercynylcysteine sulfoxide, the first
CC two steps in the biosynthesis pathway of ergothioneine
CC (PubMed:24828577). May play a role in meiosis (PubMed:16303567).
CC {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:24828577}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-histidine + 3 S-adenosyl-L-methionine = 3 H(+) + hercynine +
CC 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:38471, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15781, ChEBI:CHEBI:57595, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; EC=2.1.1.44;
CC Evidence={ECO:0000250|UniProtKB:Q7RX33};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hercynine + L-cysteine + O2 = H2O + S-(hercyn-2-yl)-L-cysteine
CC S-oxide; Xref=Rhea:RHEA:42704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15781, ChEBI:CHEBI:35235, ChEBI:CHEBI:82706;
CC EC=1.14.99.51; Evidence={ECO:0000250|UniProtKB:Q7RX33};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q7RX33};
CC Note=Binds 1 Fe(2+) ion per monomer. {ECO:0000250|UniProtKB:Q7RX33};
CC -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC {ECO:0000269|PubMed:24828577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Completely lacks ergothioneine and its precursors
CC (trimethyl histidine/hercynine and hercynylcysteine sulfoxide).
CC {ECO:0000269|PubMed:24828577}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the methyltransferase
CC superfamily. EgtD family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the EgtB family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA22334.1; -; Genomic_DNA.
DR PIR; T39513; T39513.
DR RefSeq; NP_596639.2; NM_001022560.3.
DR AlphaFoldDB; O94632; -.
DR SMR; O94632; -.
DR STRING; 4896.SPBC1604.01.1; -.
DR MaxQB; O94632; -.
DR PaxDb; O94632; -.
DR EnsemblFungi; SPBC1604.01.1; SPBC1604.01.1:pep; SPBC1604.01.
DR GeneID; 2539656; -.
DR KEGG; spo:SPBC1604.01; -.
DR PomBase; SPBC1604.01; egt1.
DR VEuPathDB; FungiDB:SPBC1604.01; -.
DR eggNOG; ENOG502QS9T; Eukaryota.
DR HOGENOM; CLU_006921_0_1_1; -.
DR InParanoid; O94632; -.
DR OMA; FKHWHPT; -.
DR PhylomeDB; O94632; -.
DR BRENDA; 1.14.99.51; 5613.
DR UniPathway; UPA01014; -.
DR PRO; PR:O94632; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005509; F:calcium ion binding; ISS:PomBase.
DR GO; GO:0030745; F:dimethylhistidine N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0061686; F:hercynylcysteine sulfoxide synthase activity; IMP:PomBase.
DR GO; GO:0044876; F:hercynylselenocysteine synthase; IMP:PomBase.
DR GO; GO:0052706; F:histidine N-methyltransferase activity; IMP:PomBase.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0052699; P:ergothioneine biosynthetic process; IMP:PomBase.
DR GO; GO:1903253; P:hercynylcysteine sulfoxide biosynthetic process; IMP:PomBase.
DR GO; GO:1903255; P:hercynylselenocysteine biosynthetic process; IMP:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0052707; P:N-alpha,N-alpha,N-alpha-trimethyl-L-histidine biosynthesis from histidine; IMP:PomBase.
DR GO; GO:1903257; P:selenoneine biosynthetic process; IMP:PomBase.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.90.1580.10; -; 1.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR019257; MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR017805; SAM_MeTrfase_EasF-type_put.
DR InterPro; IPR005532; SUMF_dom.
DR InterPro; IPR042095; SUMF_sf.
DR Pfam; PF03781; FGE-sulfatase; 1.
DR Pfam; PF10017; Methyltransf_33; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR TIGRFAMs; TIGR03439; methyl_EasF; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Iron; Meiosis; Metal-binding; Methyltransferase; Monooxygenase;
KW Nucleus; Oxidoreductase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..773
FT /note="Ergothioneine biosynthesis protein 1"
FT /id="PRO_0000278511"
FT REGION 16..322
FT /note="L-histidine N(alpha)-methyltransferase"
FT /evidence="ECO:0000305"
FT REGION 347..772
FT /note="Hercynylcysteine S-oxide synthase"
FT /evidence="ECO:0000305"
FT BINDING 51
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 91
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 142..143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 172
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 212
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 287..289
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:A0R5M8"
FT BINDING 382
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:G7CFI3"
FT BINDING 476
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:G7CFI3"
FT BINDING 480
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:G7CFI3"
SQ SEQUENCE 773 AA; 89714 MW; 4E9EF9AC7A4D89C7 CRC64;
MTEIENIGAL EVLFSPESIE QSLKRCQLPS TLLYDEKGLR LFDEITNLKE YYLYESELDI
LKKFSDSIAN QLLSPDLPNT VIELGCGNMR KTKLLLDAFE KKGCDVHFYA LDLNEAELQK
GLQELRQTTN YQHVKVSGIC GCFERLLQCL DRFRSEPNSR ISMLYLGASI GNFDRKSAAS
FLRSFASRLN IHDNLLISFD HRNKAELVQL AYDDPYRITE KFEKNILASV NAVFGENLFD
ENDWEYKSVY DEDLGVHRAY LQAKNEVTVI KGPMFFQFKP SHLILIEESW KNSDQECRQI
IEKGDFKLVS KYESTIADYS TYVITKQFPA MLQLPLQPCP SLAEWDALRK VWLFITNKLL
NKDNMYTAWI PLRHPPIFYI GHVPVFNDIY LTKIVKNKAT ANKKHFWEWF QRGIDPDIED
PSKCHWHSEV PESWPSPDQL REYEKESWEY HIVKLCKAMD ELSTSEKRIL WLCYEHVAMH
VETTLYIYVQ SFQNANQTVS ICGSLPEPAE KLTKAPLWVN VPETEIAVGM PLTTQYTSVG
SNLQSSDLSA HENTDELFYF AWDNEKPMRK KLVSSFSIAN RPISNGEYLD FINKKSKTER
VYPKQWAEID GTLYIRTMYG LLPLDDYLGW PVMTSYDDLN NYASSQGCRL PTEDELNCFY
DRVLERTDEP YVSTEGKATG FQQLHPLALS DNSSNQIFTG AWEWTSTVLE KHEDFEPEEL
YPDYTRDFFD GKHNVVLGGS FATATRISNR RSFRNFYQAG YKYAWIGARL VKN
