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Protein

Ergothioneine biosynthesis protein 1

Gene

egt1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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:24828577). May play a role in meiosis (PubMed:16303567).2 Publications

Catalytic activityi

3 S-adenosyl-L-methionine + L-histidine = 3 S-adenosyl-L-homocysteine + hercynine.By similarity
Hercynine + L-cysteine + O2 = S-hercyn-2-yl-L-cysteine S-oxide + H2O.By similarity

Cofactori

Fe2+By similarityNote: Binds 1 Fe2+ ion per monomer.By similarity

Pathwayi: ergothioneine biosynthesis

This protein is involved in the pathway ergothioneine biosynthesis, which is part of Amino-acid biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway ergothioneine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511L-histidineBy similarity
Binding sitei85 – 851S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei91 – 911S-adenosyl-L-methionineBy similarity
Binding sitei112 – 1121S-adenosyl-L-methionineBy similarity
Binding sitei172 – 1721L-histidineBy similarity
Binding sitei212 – 2121L-histidineBy similarity
Metal bindingi382 – 3821Iron; via tele nitrogenBy similarity
Metal bindingi476 – 4761Iron; via tele nitrogenBy similarity
Metal bindingi480 – 4801Iron; via tele nitrogenBy similarity

GO - Molecular functioni

  • calcium ion binding Source: PomBase
  • dimethylhistidine N-methyltransferase activity Source: UniProtKB-EC
  • hercynylcysteine sulfoxide synthase Source: PomBase
  • hercynylselenocysteine synthase Source: PomBase
  • histidine N-methyltransferase activity Source: PomBase
  • monooxygenase activity Source: UniProtKB-KW

GO - Biological processi

  • ergothioneine biosynthetic process Source: PomBase
  • hercynylcysteine sulfoxide biosynthetic process Source: PomBase
  • hercynylselenocysteine biosynthetic process Source: PomBase
  • meiotic cell cycle Source: UniProtKB-KW
  • N-alpha,N-alpha,N-alpha-trimethyl-L-histidine biosynthesis from histidine Source: PomBase
  • selenoneine biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Monooxygenase, Oxidoreductase, Transferase

Keywords - Biological processi

Meiosis

Keywords - Ligandi

Iron, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA01014.

Names & Taxonomyi

Protein namesi
Recommended name:
Ergothioneine biosynthesis protein 11 Publication
Alternative name(s):
Meiotically up-regulated gene 158 protein1 Publication
Including the following 2 domains:
L-histidine N(alpha)-methyltransferaseBy similarity (EC:2.1.1.44By similarity)
Hercynylcysteine S-oxide synthaseBy similarity (EC:1.14.99.51By similarity)
Gene namesi
Name:egt11 Publication
Synonyms:mug1581 Publication
ORF Names:SPBC1604.01Imported, SPBC1677.01c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1604.01.
PomBaseiSPBC1604.01. egt1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • endoplasmic reticulum lumen Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Completely lacks ergothioneine and its precursors (trimethyl histidine/hercynine and hercynylcysteine sulfoxide).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 773773Ergothioneine biosynthesis protein 1PRO_0000278511Add
BLAST

Proteomic databases

MaxQBiO94632.

Interactioni

Protein-protein interaction databases

MINTiMINT-4685704.

Structurei

3D structure databases

ProteinModelPortaliO94632.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni16 – 322307L-histidine N(alpha)-methyltransferaseCuratedAdd
BLAST
Regioni142 – 1432S-adenosyl-L-methionine bindingBy similarity
Regioni287 – 2893L-histidine bindingBy similarity
Regioni347 – 772426Hercynylcysteine S-oxide synthaseCuratedAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the methyltransferase superfamily. EgtD family.Curated
In the C-terminal section; belongs to the EgtB family.Curated

Phylogenomic databases

InParanoidiO94632.
OMAiITNGEYA.
OrthoDBiEOG7CRTZ7.
PhylomeDBiO94632.

Family and domain databases

Gene3Di3.90.1580.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR019257. MeTrfase_dom.
IPR029063. SAM-dependent_MTases.
IPR017805. SAM_MeTrfase_EsaF-type_put.
IPR005532. SUMF_dom.
[Graphical view]
PfamiPF03781. FGE-sulfatase. 1 hit.
PF10017. Methyltransf_33. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
SSF56436. SSF56436. 1 hit.
TIGRFAMsiTIGR03439. methyl_EasF. 1 hit.

Sequencei

Sequence statusi: Complete.

O94632-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEIENIGAL EVLFSPESIE QSLKRCQLPS TLLYDEKGLR LFDEITNLKE
60 70 80 90 100
YYLYESELDI LKKFSDSIAN QLLSPDLPNT VIELGCGNMR KTKLLLDAFE
110 120 130 140 150
KKGCDVHFYA LDLNEAELQK GLQELRQTTN YQHVKVSGIC GCFERLLQCL
160 170 180 190 200
DRFRSEPNSR ISMLYLGASI GNFDRKSAAS FLRSFASRLN IHDNLLISFD
210 220 230 240 250
HRNKAELVQL AYDDPYRITE KFEKNILASV NAVFGENLFD ENDWEYKSVY
260 270 280 290 300
DEDLGVHRAY LQAKNEVTVI KGPMFFQFKP SHLILIEESW KNSDQECRQI
310 320 330 340 350
IEKGDFKLVS KYESTIADYS TYVITKQFPA MLQLPLQPCP SLAEWDALRK
360 370 380 390 400
VWLFITNKLL NKDNMYTAWI PLRHPPIFYI GHVPVFNDIY LTKIVKNKAT
410 420 430 440 450
ANKKHFWEWF QRGIDPDIED PSKCHWHSEV PESWPSPDQL REYEKESWEY
460 470 480 490 500
HIVKLCKAMD ELSTSEKRIL WLCYEHVAMH VETTLYIYVQ SFQNANQTVS
510 520 530 540 550
ICGSLPEPAE KLTKAPLWVN VPETEIAVGM PLTTQYTSVG SNLQSSDLSA
560 570 580 590 600
HENTDELFYF AWDNEKPMRK KLVSSFSIAN RPISNGEYLD FINKKSKTER
610 620 630 640 650
VYPKQWAEID GTLYIRTMYG LLPLDDYLGW PVMTSYDDLN NYASSQGCRL
660 670 680 690 700
PTEDELNCFY DRVLERTDEP YVSTEGKATG FQQLHPLALS DNSSNQIFTG
710 720 730 740 750
AWEWTSTVLE KHEDFEPEEL YPDYTRDFFD GKHNVVLGGS FATATRISNR
760 770
RSFRNFYQAG YKYAWIGARL VKN
Length:773
Mass (Da):89,714
Last modified:February 20, 2007 - v4
Checksum:i4E9EF9AC7A4D89C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22334.1.
PIRiT39513.
RefSeqiNP_596639.2. NM_001022560.3.

Genome annotation databases

EnsemblFungiiSPBC1604.01.1; SPBC1604.01.1:pep; SPBC1604.01.
GeneIDi2539656.
KEGGispo:SPBC1604.01.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA22334.1.
PIRiT39513.
RefSeqiNP_596639.2. NM_001022560.3.

3D structure databases

ProteinModelPortaliO94632.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4685704.

Proteomic databases

MaxQBiO94632.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1604.01.1; SPBC1604.01.1:pep; SPBC1604.01.
GeneIDi2539656.
KEGGispo:SPBC1604.01.

Organism-specific databases

EuPathDBiFungiDB:SPBC1604.01.
PomBaseiSPBC1604.01. egt1.

Phylogenomic databases

InParanoidiO94632.
OMAiITNGEYA.
OrthoDBiEOG7CRTZ7.
PhylomeDBiO94632.

Enzyme and pathway databases

UniPathwayiUPA01014.

Miscellaneous databases

NextBioi20800810.
PROiO94632.

Family and domain databases

Gene3Di3.90.1580.10. 1 hit.
InterProiIPR016187. C-type_lectin_fold.
IPR019257. MeTrfase_dom.
IPR029063. SAM-dependent_MTases.
IPR017805. SAM_MeTrfase_EsaF-type_put.
IPR005532. SUMF_dom.
[Graphical view]
PfamiPF03781. FGE-sulfatase. 1 hit.
PF10017. Methyltransf_33. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
SSF56436. SSF56436. 1 hit.
TIGRFAMsiTIGR03439. methyl_EasF. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "A large-scale screen in S. pombe identifies seven novel genes required for critical meiotic events."
    Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L., Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P., Smith G.R., Moreno S.
    Curr. Biol. 15:2056-2062(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEIOSIS.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. "Genetic and metabolomic dissection of the ergothioneine and selenoneine biosynthetic pathway in the fission yeast, S. pombe, and construction of an overproduction system."
    Pluskal T., Ueno M., Yanagida M.
    PLoS ONE 9:E97774-E97774(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiEGT1_SCHPO
AccessioniPrimary (citable) accession number: O94632
Secondary accession number(s): O94367, Q1MTP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: February 20, 2007
Last modified: February 17, 2016
This is version 90 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.