EGT2_SCHPO
ID EGT2_SCHPO Reviewed; 392 AA.
AC O94431;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Hercynylcysteine sulfoxide lyase {ECO:0000250|UniProtKB:A7UX13};
DE EC=4.4.1.- {ECO:0000250|UniProtKB:A7UX13};
DE AltName: Full=Ergothioneine biosynthesis protein 2 {ECO:0000303|PubMed:24828577};
DE AltName: Full=PLP-binding cysteine desulfurase {ECO:0000303|PubMed:24828577};
DE AltName: Full=PLP-dependent C-S lyase {ECO:0000250|UniProtKB:A7UX13};
GN Name=egt2 {ECO:0000303|PubMed:24828577};
GN ORFNames=SPBC660.12c {ECO:0000312|PomBase:SPBC660.12c};
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 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 [3]
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 conversion of hercynylcysteine sulfoxide to
CC ergothioneine by cleaving the cysteine residue at the sulfur atom, the
CC last step in the biosynthesis pathway of ergothioneine.
CC {ECO:0000305|PubMed:24828577}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H(+) + S-(hercyn-2-yl)-L-cysteine S-oxide = A +
CC ergothioneine + NH4(+) + pyruvate; Xref=Rhea:RHEA:42688,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:28938, ChEBI:CHEBI:82706,
CC ChEBI:CHEBI:134344; Evidence={ECO:0000250|UniProtKB:A7UX13};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P23721};
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:24828577}.
CC -!- DISRUPTION PHENOTYPE: Shows substantial decrease in ergothioneine,
CC accompanied by accumulation of its immediate precursor,
CC hercynylcysteine sulfoxide. {ECO:0000269|PubMed:24828577}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. EgtE subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAA22532.1; -; Genomic_DNA.
DR PIR; T40624; T40624.
DR RefSeq; NP_595091.1; NM_001020998.2.
DR AlphaFoldDB; O94431; -.
DR SMR; O94431; -.
DR BioGRID; 277607; 10.
DR STRING; 4896.SPBC660.12c.1; -.
DR MaxQB; O94431; -.
DR PaxDb; O94431; -.
DR PRIDE; O94431; -.
DR EnsemblFungi; SPBC660.12c.1; SPBC660.12c.1:pep; SPBC660.12c.
DR GeneID; 2541092; -.
DR KEGG; spo:SPBC660.12c; -.
DR PomBase; SPBC660.12c; egt2.
DR VEuPathDB; FungiDB:SPBC660.12c; -.
DR eggNOG; KOG1549; Eukaryota.
DR HOGENOM; CLU_003433_3_0_1; -.
DR InParanoid; O94431; -.
DR OMA; DYTPYLC; -.
DR PhylomeDB; O94431; -.
DR BioCyc; MetaCyc:MON-18846; -.
DR BRENDA; 4.4.1.36; 5613.
DR UniPathway; UPA01014; -.
DR PRO; PR:O94431; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:1990411; F:hercynylcysteine sulfoxide lyase activity (ergothioneine-forming); IMP:PomBase.
DR GO; GO:1990412; F:hercynylselenocysteine lyase activity (selenoneine-forming); IMP:PomBase.
DR GO; GO:0052699; P:ergothioneine biosynthetic process; IMP:PomBase.
DR GO; GO:1903257; P:selenoneine biosynthetic process; IMP:PomBase.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lyase; Nucleus; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..392
FT /note="Hercynylcysteine sulfoxide lyase"
FT /id="PRO_0000310318"
FT MOD_RES 219
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P23721"
SQ SEQUENCE 392 AA; 44535 MW; F4594C9A9DF42913 CRC64;
MAENNVYGHE MKKHFMLDPD YVNVNNGSCG TESLAVYNKH VQLLKEAQSK PDFMCNAYMP
MYMEATRNEV AKLIGADSSN IVFCNSATDG ISTVLLTFPW EQNDEILMLN VAYPTCTYAA
DFAKNQHNLR LDVIDVGVEI DEDLFLKEVE QRFLQSKPRA FICDILSSMP VILFPWEKVV
KLCKKYNIVS IIDGAHAIGH IPMNLANVDP DFLFTNAHKW LNSPAACTVL YVSAKNHNLI
EALPLSYGYG LREKESIAVD TLTNRFVNSF KQDLPKFIAV GEAIKFRKSI GGEEKIQQYC
HEIALKGAEI ISKELGTSFI KPPYPVAMVN VEVPLRNIPS IETQKVFWPK YNTFLRFMEF
KGKFYTRLSG AVYLEESDFY YIAKVIKDFC SL
