UPPB_SCHMA
ID UPPB_SCHMA Reviewed; 296 AA.
AC G4VGH9;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Inactive uridine phosphorylase B {ECO:0000303|PubMed:26898674};
DE Short=SmUPb {ECO:0000303|PubMed:26898674};
GN Name=UPPB {ECO:0000305|PubMed:26898674};
GN ORFNames=Smp_082420 {ECO:0000312|EMBL:CCD78100.1};
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:CCD78100.1};
RN [1] {ECO:0000312|EMBL:CCD78100.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Puerto Rican {ECO:0000312|EMBL:CCD78100.1};
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:5CYF, ECO:0007744|PDB:5CYG}
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS), 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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26898674}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. {ECO:0000305}.
CC -!- CAUTION: Although this protein has high similarity to uridine
CC phosphorylases, it has no detectable catalytic activity. It contains
CC substitutions at Gly-126 and Gln-201, two conserved sites which are
CC known to be important for uridine binding.
CC {ECO:0000269|PubMed:26898674}.
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DR EMBL; HE601626; CCD78100.1; -; Genomic_DNA.
DR RefSeq; XP_018650717.1; XM_018798871.1.
DR PDB; 5CYF; X-ray; 1.98 A; A/B/C=1-296.
DR PDB; 5CYG; X-ray; 2.02 A; A/B=1-296.
DR PDBsum; 5CYF; -.
DR PDBsum; 5CYG; -.
DR AlphaFoldDB; G4VGH9; -.
DR SMR; G4VGH9; -.
DR GeneID; 8343369; -.
DR KEGG; smm:Smp_082420; -.
DR CTD; 8343369; -.
DR eggNOG; KOG3728; Eukaryota.
DR HOGENOM; CLU_054104_0_0_1; -.
DR InParanoid; G4VGH9; -.
DR OrthoDB; 1423938at2759; -.
DR PhylomeDB; G4VGH9; -.
DR BRENDA; 2.4.2.3; 5608.
DR Proteomes; UP000008854; Chromosome 3.
DR ExpressionAtlas; G4VGH9; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
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; Reference proteome.
FT CHAIN 1..296
FT /note="Inactive uridine phosphorylase B"
FT /id="PRO_0000449953"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:5CYF"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:5CYF"
FT HELIX 32..36
FT /evidence="ECO:0007829|PDB:5CYF"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:5CYF"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:5CYF"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:5CYF"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:5CYF"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5CYF"
FT HELIX 95..111
FT /evidence="ECO:0007829|PDB:5CYF"
FT STRAND 118..130
FT /evidence="ECO:0007829|PDB:5CYF"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:5CYF"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:5CYF"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:5CYF"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:5CYF"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:5CYF"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:5CYF"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:5CYF"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:5CYF"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:5CYF"
FT STRAND 248..258
FT /evidence="ECO:0007829|PDB:5CYF"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:5CYF"
FT HELIX 269..289
FT /evidence="ECO:0007829|PDB:5CYF"
SQ SEQUENCE 296 AA; 32701 MW; 39D43B180132A5B8 CRC64;
MATVQPIVNS HLSELDEDVF HHFGFTTKSF DFKEKFGDVK FVCVCGSSGR IHNFAISMAK
LAGLALPVEN IAGSHARFVL YKVDHILFAD HGIGIPSTLI LMHEVTKLLY YAGCKDVLFI
RLGTSDGLGV KPGTIVLSDR CVNTKLEPYN ELCILGKPVR RQTKVDSNAV NELKKLSENL
SLKCSVVVGG TITANDFYEE LGRLNGSICT FSKEEKLAFL QSVYDHGIRN MEMEGAAITS
HCNLTGHRAI LVCVTVVNRL ETDEVTTSTD EFKLFEQLPG QLVGEYLKRN NGIIVR
