UPPA_SCHMA
ID UPPA_SCHMA Reviewed; 296 AA.
AC G4VGI0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Uridine phosphorylase A {ECO:0000303|PubMed:26898674};
DE Short=SmUPa {ECO:0000303|PubMed:26898674};
DE EC=2.4.2.3 {ECO:0000269|PubMed:26898674};
GN Name=UPPA {ECO:0000305|PubMed:26898674};
GN ORFNames=Smp_082430 {ECO:0000312|EMBL:CCD78101.1};
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183 {ECO:0000312|EMBL:CCD78101.1};
RN [1] {ECO:0000312|Proteomes:UP000008854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican {ECO:0000312|Proteomes:UP000008854};
RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA Zerlotini A., Dunne D.W., Berriman M.;
RT "A systematically improved high quality genome and transcriptome of the
RT human blood fluke Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN [2] {ECO:0007744|PDB:4TXH, ECO:0007744|PDB:4TXJ, ECO:0007744|PDB:4TXL}
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) IN APO FORM AND IN COMPLEX WITH
RP URIDINE; THYMINE AND 5-FLUOROURACIL, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=26898674; DOI=10.1016/j.biochi.2016.02.007;
RA da Silva Neto A.M., Torini de Souza J.R., Romanelo L., Cassago A.,
RA Serrao V.H., DeMarco R., Brandao-Neto J., Garratt R.C., Pereira H.D.;
RT "Analysis of two Schistosoma mansoni uridine phosphorylases isoforms
RT suggests the emergence of a protein with a non-canonical function.";
RL Biochimie 125:12-22(2016).
CC -!- FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine
CC and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate
CC (PubMed:26898674). The produced molecules are then utilized as carbon
CC and energy sources or in the rescue of pyrimidine bases for nucleotide
CC synthesis (Probable). {ECO:0000269|PubMed:26898674, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil;
CC Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.3;
CC Evidence={ECO:0000269|PubMed:26898674};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=31 uM for uridine {ECO:0000269|PubMed:26898674};
CC KM=48.9 uM for thymidine {ECO:0000269|PubMed:26898674};
CC Note=kcat is 35.9 sec(-1) for uridine. kcat is 0.41 sec(-1) for
CC thymidine. {ECO:0000269|PubMed:26898674};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC uracil from uridine (phosphorylase route): step 1/1.
CC {ECO:0000269|PubMed:26898674}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26898674}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. {ECO:0000305}.
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DR EMBL; HE601626; CCD78101.1; -; Genomic_DNA.
DR RefSeq; XP_018650718.1; XM_018798872.1.
DR PDB; 4TXH; X-ray; 1.89 A; A/B/C/D=1-296.
DR PDB; 4TXJ; X-ray; 1.66 A; A/B/C/D=1-296.
DR PDB; 4TXL; X-ray; 1.92 A; A/B/C/D=1-296.
DR PDB; 4TXM; X-ray; 1.93 A; A/B=1-296.
DR PDB; 4TXN; X-ray; 2.00 A; A/B/C/D=1-296.
DR PDBsum; 4TXH; -.
DR PDBsum; 4TXJ; -.
DR PDBsum; 4TXL; -.
DR PDBsum; 4TXM; -.
DR PDBsum; 4TXN; -.
DR AlphaFoldDB; G4VGI0; -.
DR SMR; G4VGI0; -.
DR STRING; 6183.Smp_082430.1; -.
DR EnsemblMetazoa; Smp_308140.1; Smp_308140.1; Smp_308140.
DR GeneID; 8343370; -.
DR KEGG; smm:Smp_082430; -.
DR WBParaSite; Smp_308140.1; Smp_308140.1; Smp_308140.
DR CTD; 8343370; -.
DR eggNOG; KOG3728; Eukaryota.
DR HOGENOM; CLU_054104_0_0_1; -.
DR InParanoid; G4VGI0; -.
DR OMA; FIHLCNP; -.
DR OrthoDB; 1423938at2759; -.
DR PhylomeDB; G4VGI0; -.
DR UniPathway; UPA00574; UER00633.
DR Proteomes; UP000008854; Unassembled WGS sequence.
DR ExpressionAtlas; G4VGI0; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0004850; F:uridine phosphorylase activity; IDA:UniProtKB.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006218; P:uridine catabolic process; IDA:UniProtKB.
DR CDD; cd17763; UP_hUPP-like; 1.
DR Gene3D; 3.40.50.1580; -; 1.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR010059; Uridine_phosphorylase_euk.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01719; euk_UDPppase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..296
FT /note="Uridine phosphorylase A"
FT /id="PRO_0000449952"
FT BINDING 46
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:Q16831"
FT BINDING 77
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:Q16831"
FT BINDING 121..124
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:Q16831"
FT BINDING 125..126
FT /ligand="uridine"
FT /ligand_id="ChEBI:CHEBI:16704"
FT /evidence="ECO:0000269|PubMed:26898674,
FT ECO:0007744|PDB:4TXJ, ECO:0007744|PDB:4TXL,
FT ECO:0007744|PDB:4TXM, ECO:0007744|PDB:4TXN"
FT BINDING 201..203
FT /ligand="uridine"
FT /ligand_id="ChEBI:CHEBI:16704"
FT /evidence="ECO:0000269|PubMed:26898674,
FT ECO:0007744|PDB:4TXJ, ECO:0007744|PDB:4TXL,
FT ECO:0007744|PDB:4TXN"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:4TXJ"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:4TXJ"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:4TXJ"
FT HELIX 32..36
FT /evidence="ECO:0007829|PDB:4TXJ"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:4TXJ"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:4TXJ"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:4TXJ"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:4TXJ"
FT HELIX 95..112
FT /evidence="ECO:0007829|PDB:4TXJ"
FT STRAND 118..130
FT /evidence="ECO:0007829|PDB:4TXJ"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:4TXJ"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:4TXJ"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:4TXJ"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:4TXJ"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:4TXJ"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:4TXJ"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4TXJ"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:4TXM"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:4TXJ"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:4TXJ"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:4TXJ"
FT STRAND 248..258
FT /evidence="ECO:0007829|PDB:4TXJ"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:4TXJ"
FT HELIX 269..276
FT /evidence="ECO:0007829|PDB:4TXJ"
FT HELIX 278..289
FT /evidence="ECO:0007829|PDB:4TXJ"
SQ SEQUENCE 296 AA; 32609 MW; 4FEA7C38C84516E8 CRC64;
MATVQPIVNS HLSELDEDVF HHFGFTTKSF DFKEKFGDVK FVCVCGSSGR IHNFAISMAK
LAGLALPVEN IAGSHARFVL YKVDHILFAD HGMGIPSALI MLHEVTKLLH YAGCKDVLFI
RLGTSGGLGV KPGTIVLSDR CVNTKLEPYN ELCILGKPVR RQTIVDLNTV NELKKLSENL
SLECSVVVGG TIAANDFYEE QGRLDGSICT FSKEEKLAFL QSAYEHGIRN MEMEGTAITS
HCYLTGHRAI LVCVTAVNRL EGDQITISTD EFTLFAQRPG QLVGEYLKRN NGIIVR
