ID H3A0B4_LATCH Unreviewed; 313 AA.
AC H3A0B4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Uridine phosphorylase {ECO:0000256|RuleBase:RU361131};
DE EC=2.4.2.3 {ECO:0000256|RuleBase:RU361131};
GN Name=UPP1 {ECO:0000313|Ensembl:ENSLACP00000003085.2};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000003085.2, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000003085.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine
CC to uracil and ribose-1-phosphate which can then be utilized as carbon
CC and energy sources or in the rescue of pyrimidine bases for nucleotide
CC synthesis. Shows broad substrate specificity and can also accept
CC deoxyuridine and other analogous compounds.
CC {ECO:0000256|RuleBase:RU361131}.
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:0000256|RuleBase:RU361131};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC uracil from uridine (phosphorylase route): step 1/1.
CC {ECO:0000256|RuleBase:RU361131}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00010456, ECO:0000256|RuleBase:RU361131}.
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DR EMBL; AFYH01221367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01221368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01221369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01221370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01221371; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01221372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01221373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01221374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01221375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01221376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006010743.1; XM_006010681.2.
DR RefSeq; XP_014353008.1; XM_014497522.1.
DR RefSeq; XP_014353009.1; XM_014497523.1.
DR AlphaFoldDB; H3A0B4; -.
DR STRING; 7897.ENSLACP00000003085; -.
DR Ensembl; ENSLACT00000003115.2; ENSLACP00000003085.2; ENSLACG00000002763.2.
DR GeneID; 102365626; -.
DR KEGG; lcm:102365626; -.
DR CTD; 7378; -.
DR eggNOG; KOG3728; Eukaryota.
DR GeneTree; ENSGT00940000157781; -.
DR HOGENOM; CLU_054104_0_0_1; -.
DR InParanoid; H3A0B4; -.
DR OMA; MEHFANY; -.
DR OrthoDB; 22073at2759; -.
DR TreeFam; TF314310; -.
DR UniPathway; UPA00574; UER00633.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000002763; Expressed in pelvic fin and 1 other cell type or tissue.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004850; F:uridine phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009164; P:nucleoside catabolic process; IEA:UniProt.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd17763; UP_hUPP-like; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR010059; Uridine_phosphorylase_euk.
DR NCBIfam; TIGR01719; euk_UDPppase; 1.
DR PANTHER; PTHR43691; URIDINE PHOSPHORYLASE; 1.
DR PANTHER; PTHR43691:SF10; URIDINE PHOSPHORYLASE 1; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR PROSITE; PS01232; PNP_UDP_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR610059-51};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU361131};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361131}.
FT DOMAIN 57..307
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 97
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR610059-50"
FT BINDING 141..144
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR610059-50"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610059-50"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610059-50"
FT DISULFID 92..99
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR610059-51"
SQ SEQUENCE 313 AA; 34726 MW; B021E1F22BC996DE CRC64;
MGPVCTVEEK RKIEQPLQDG SIHLSNPYIE RMKQDVLYHF ELGTGTHDFP AMFGDVKFVC
VGGSPSRMKA FIKYIAGELE LGDPNDDYPN ICAGTDRYCM YKVGPVLSVS HGMGIPSMAI
MLHELIKLLY HAKCTDVIII RIGTSGGIGL EPGSVVITEQ SVNAHFKAQF EQVILGKTVV
RSTHLDDKIA QELLECSKEM NKFNTVIGNT MCTLDFYEGQ ARLDGAFCSY TEKEKLDYLM
AAFKSGVRNI EMESSVFAAM CLLSGVRAAV VCVTLLDRLV DDQISSPHDV LVEYQERPQK
LVAYFIKKCL AKA
//
