ID C3ZRV1_BRAFL Unreviewed; 286 AA.
AC C3ZRV1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00013834};
DE EC=2.4.2.1 {ECO:0000256|ARBA:ARBA00011886};
DE AltName: Full=Inosine phosphorylase {ECO:0000256|ARBA:ARBA00033072};
DE AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|ARBA:ARBA00031036};
DE Flags: Fragment;
GN ORFNames=BRAFLDRAFT_238286 {ECO:0000313|EMBL:EEN44751.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN44751.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN44751.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN44751.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC phosphate + guanine; Xref=Rhea:RHEA:27738, ChEBI:CHEBI:16235,
CC ChEBI:CHEBI:17172, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023929};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyinosine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC phosphate + hypoxanthine; Xref=Rhea:RHEA:27750, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:28997, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023950};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine;
CC Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235, ChEBI:CHEBI:16750,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023970};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate +
CC hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00023918};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000256|ARBA:ARBA00005058}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006751}.
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DR EMBL; GG666667; EEN44751.1; -; Genomic_DNA.
DR RefSeq; XP_002588740.1; XM_002588694.1.
DR AlphaFoldDB; C3ZRV1; -.
DR STRING; 7739.C3ZRV1; -.
DR eggNOG; KOG3984; Eukaryota.
DR InParanoid; C3ZRV1; -.
DR UniPathway; UPA00606; -.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IBA:GO_Central.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR CDD; cd09009; PNP-EcPNPII_like; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR011270; Pur_Nuc_Pase_Ino/Guo-sp.
DR InterPro; IPR011268; Purine_phosphorylase.
DR InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR NCBIfam; TIGR01700; PNPH; 1.
DR NCBIfam; TIGR01697; PNPH-PUNA-XAPA; 1.
DR PANTHER; PTHR11904; METHYLTHIOADENOSINE/PURINE NUCLEOSIDE PHOSPHORYLASE; 1.
DR PANTHER; PTHR11904:SF9; PURINE NUCLEOSIDE PHOSPHORYLASE-RELATED; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR PIRSF; PIRSF000477; PurNPase; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR PROSITE; PS01240; PNP_MTAP_2; 1.
PE 3: Inferred from homology;
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726}.
FT DOMAIN 21..273
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEN44751.1"
SQ SEQUENCE 286 AA; 31390 MW; 25C5C88837B22DB2 CRC64;
TYEDIQHISD FLLKTTKYRP KVAVICGSGL GGLADVVQQQ DVIDYRDIPN FPQSTVQGHR
GRLVFGHLAG KSVICMQGRF HQYQGYPLWK VAMPVRVFKM IGVETLFVTN AAGGLNRNYN
IGDIMIVKDH ISMPGMTTDN PLKGFYDERF GKPSSPVTEL YDRGLRELAR RVAGDLGLGE
AVREGVLVQV GGPSFDTVSV FNMLRRLGAD CVGMSSAPEV TVARHCGIRV LGLSLVTDMA
PMESDLPPTN HQEILQTAKT RAVDVQNLVC EMISQLPNNN DSVQPS
//
