YOW5_SCHPO
ID YOW5_SCHPO Reviewed; 747 AA.
AC Q9USY1;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Pseudouridine-metabolizing bifunctional protein C1861.05;
DE Includes:
DE RecName: Full=Pseudouridine-5'-phosphate glycosidase {ECO:0000250|UniProtKB:P33025};
DE Short=PsiMP glycosidase {ECO:0000250|UniProtKB:P33025};
DE EC=4.2.1.70 {ECO:0000250|UniProtKB:P33025};
DE Includes:
DE RecName: Full=Pseudouridine kinase {ECO:0000250|UniProtKB:P30235};
DE EC=2.7.1.83 {ECO:0000250|UniProtKB:P30235};
GN ORFNames=SPBC1861.05;
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).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the phosphorylation of
CC pseudouridine to pseudouridine 5'-phosphate (PsiMP), and the reversible
CC cleavage of pseudouridine 5'-phosphate to ribose 5-phosphate and
CC uracil. Is involved in a pseudouridine degradation pathway.
CC {ECO:0000250|UniProtKB:P30235, ECO:0000250|UniProtKB:P33025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribose 5-phosphate + uracil = H2O + psi-UMP;
CC Xref=Rhea:RHEA:18337, ChEBI:CHEBI:15377, ChEBI:CHEBI:17568,
CC ChEBI:CHEBI:58380, ChEBI:CHEBI:78346; EC=4.2.1.70;
CC Evidence={ECO:0000250|UniProtKB:P33025};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pseudouridine = ADP + H(+) + psi-UMP;
CC Xref=Rhea:RHEA:22448, ChEBI:CHEBI:15378, ChEBI:CHEBI:17802,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58380, ChEBI:CHEBI:456216;
CC EC=2.7.1.83; Evidence={ECO:0000250|UniProtKB:P30235};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P33025};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the pseudouridine-5'-
CC phosphate glycosidase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the carbohydrate
CC kinase PfkB family. {ECO:0000305}.
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DR EMBL; CU329671; CAB52741.1; -; Genomic_DNA.
DR PIR; T39744; T39744.
DR RefSeq; NP_596722.1; NM_001022647.2.
DR AlphaFoldDB; Q9USY1; -.
DR SMR; Q9USY1; -.
DR BioGRID; 276314; 46.
DR STRING; 4896.SPBC1861.05.1; -.
DR MaxQB; Q9USY1; -.
DR PaxDb; Q9USY1; -.
DR PRIDE; Q9USY1; -.
DR EnsemblFungi; SPBC1861.05.1; SPBC1861.05.1:pep; SPBC1861.05.
DR GeneID; 2539763; -.
DR KEGG; spo:SPBC1861.05; -.
DR PomBase; SPBC1861.05; -.
DR VEuPathDB; FungiDB:SPBC1861.05; -.
DR eggNOG; KOG3009; Eukaryota.
DR HOGENOM; CLU_012201_3_0_1; -.
DR InParanoid; Q9USY1; -.
DR OMA; YTHGFPY; -.
DR PhylomeDB; Q9USY1; -.
DR PRO; PR:Q9USY1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050225; F:pseudouridine kinase activity; ISS:PomBase.
DR GO; GO:0004730; F:pseudouridylate synthase activity; ISO:PomBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0001522; P:pseudouridine synthesis; IC:PomBase.
DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IC:PomBase.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.1790.10; -; 1.
DR HAMAP; MF_01876; PsiMP_glycosidase; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR022830; Indigdn_synthA-like.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR007342; PsuG.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR42909; PTHR42909; 1.
DR Pfam; PF04227; Indigoidine_A; 1.
DR Pfam; PF00294; PfkB; 2.
DR SUPFAM; SSF110581; SSF110581; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycosidase; Hydrolase; Kinase; Lyase; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..747
FT /note="Pseudouridine-metabolizing bifunctional protein
FT C1861.05"
FT /id="PRO_0000362159"
FT REGION 1..379
FT /note="Pseudouridine-5'-phosphate glycosidase"
FT REGION 380..747
FT /note="Pseudouridine kinase"
FT ACT_SITE 61
FT /note="Proton donor; for PsiMP glycosidase activity"
FT /evidence="ECO:0000250|UniProtKB:P33025"
FT ACT_SITE 196
FT /note="Nucleophile; for PsiMP glycosidase activity"
FT /evidence="ECO:0000250|UniProtKB:P33025"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P33025"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P33025"
FT BINDING 175
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P33025"
FT BINDING 177..179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P33025"
SQ SEQUENCE 747 AA; 80759 MW; 6AD61E36FE7D9420 CRC64;
MLIVMNRGCR LVSRIPLGFR RLKRNPNPGL RNILCRRYSP LALSKEVTEA LKNNVPVVAL
ESTIITHGMP YPQNEELAIQ VESKVRSMGA VPATIALLNG QCTIGLEQFQ LSELAKSGET
AYKVSRRDLS YVASQRLNGG TTVAATMILA RAAGIDVFAT GGIGGVHRGA ENSMDISADL
IELGRTRVAV VSAGVKSILD IGRTLEVLET QGVPVVTLGP PKSAFPAFFS RESKFQSPLS
LETPQLIANM LFSNIQLGQE CGTLVAIPTP HHCSIDYEKM EALIETCLQR SVQLGITGKN
VTPWLLGELL RESKGKSLNT NIDLVLNNAE KASLIAKELA VLKEKSSFFP TNTGNTFETK
PVKQDFFYGK VSDKGVSSSK KKITETTSKP AEVVCVGSVS IDSVLKLDNP LTSKFLGTSH
PCHSEQAFGG VAHNMALASS LMGASTKLVS CVGTKSVPTS SIKEYLTKSS LQHTIVEKSN
FTSCSYTAIN DCNGNLLLAG ADMAIMENLS YSEIKDDLND AKYICFDGNI SPSLMLDITT
SKSSKQRVVF EPTSGPKTLK ILKVLSVASI DFITPNKFEL DVLFQAMKDG NFFENESWWQ
KLNSFGITSS FYNEIERFTK STGIEEITEN GILQKCFHLL PFIKNIIVKL GPNGALLISS
EKLQGVNSNS ASLFTPGNVT VKYYPVPKVI ATPVNASGTG DTFIGTFTAL LSKGWGMDDA
IDTAQKAAGL TLQCNFSVNP EIKTLLK
