ID A0A2I2Z2X2_GORGO Unreviewed; 263 AA.
AC A0A2I2Z2X2;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|HAMAP-Rule:MF_03155};
DE Short=PNP {ECO:0000256|HAMAP-Rule:MF_03155};
DE EC=2.4.2.1 {ECO:0000256|HAMAP-Rule:MF_03155};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000041608.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000041608.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000041608.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000041608.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Purine nucleoside phosphorylase involved in purine salvage.
CC {ECO:0000256|HAMAP-Rule:MF_03155}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase +
CC alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03155};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000256|HAMAP-Rule:MF_03155}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_03155}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03155}.
CC -!- MISCELLANEOUS: Although this enzyme belongs to the family of MTA
CC phosphorylases based on sequence homology, it lacks several conserved
CC amino acids in the substrate binding pocket that confer specificity
CC towards MTA. {ECO:0000256|HAMAP-Rule:MF_03155}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03155}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03155}.
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DR EMBL; CABD030026202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030026203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I2Z2X2; -.
DR STRING; 9593.ENSGGOP00000041608; -.
DR Ensembl; ENSGGOT00000042861.1; ENSGGOP00000041608.1; ENSGGOG00000039775.1.
DR GeneTree; ENSGT00950000182991; -.
DR InParanoid; A0A2I2Z2X2; -.
DR OMA; CPKTREX; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000001519; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule.
DR CDD; cd09010; MTAP_SsMTAPII_like_MTIP; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 2.
DR HAMAP; MF_01963; MTAP; 1.
DR InterPro; IPR010044; MTAP.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR PANTHER; PTHR42679:SF5; PURINE NUCLEOSIDE PHOSPHORYLASE; 1.
DR PANTHER; PTHR42679; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1.
DR Pfam; PF01048; PNP_UDP_1; 2.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR PROSITE; PS01240; PNP_MTAP_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155};
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_03155};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03155};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW Rule:MF_03155}; Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03155}.
FT DOMAIN 11..128
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT DOMAIN 158..227
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 18
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 60..61
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 93..94
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 170
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 193..195
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT SITE 206
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
SQ SEQUENCE 263 AA; 28928 MW; FCBDB954E62272C2 CRC64;
MASSTTTTAM KIGVIGGTGL DDPEILEGRT EKYVDTPFSK PFDALILGKI KSVDCILLAR
HGRQHTILPS KVNYQATIWA LKEEGCTHVI GTTACGSLRE EIQPGDIVII DQFIDGTTMR
PQSLYDGSHC CARGVCHIPM GAKEVLIENA KKLGLCFMFC TWGVDVINMT TVPEVVLTKE
AGICYASIAM VTDYDCWKEH EEAVLVDWDL KTPKENASKA KRLLLTTIPQ IGSMEWSKTL
HGLKNIAQSS VLKFLQSIHL TKD
//
