ID A0A1A9LE95_9FLAO Unreviewed; 272 AA.
AC A0A1A9LE95;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|PIRNR:PIRNR000477};
DE EC=2.4.2.1 {ECO:0000256|PIRNR:PIRNR000477};
DE AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|PIRNR:PIRNR000477};
GN ORFNames=A7A78_03315 {ECO:0000313|EMBL:OAD91533.1};
OS Aequorivita soesokkakensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=1385699 {ECO:0000313|EMBL:OAD91533.1, ECO:0000313|Proteomes:UP000077552};
RN [1] {ECO:0000313|EMBL:OAD91533.1, ECO:0000313|Proteomes:UP000077552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSSK-12 {ECO:0000313|EMBL:OAD91533.1,
RC ECO:0000313|Proteomes:UP000077552};
RA Thevarajoo S., Selvaratnam C., Goh K.M., Chan K.-G., Chong C.S.;
RT "Genome sequencing of Vitellibacter soesokkakensis RSSK-12.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The purine nucleoside phosphorylases catalyze the
CC phosphorolytic breakdown of the N-glycosidic bond in the beta-
CC (deoxy)ribonucleoside molecules, with the formation of the
CC corresponding free purine bases and pentose-1-phosphate.
CC {ECO:0000256|PIRNR:PIRNR000477}.
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000256|ARBA:ARBA00005058, ECO:0000256|PIRNR:PIRNR000477}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006751, ECO:0000256|PIRNR:PIRNR000477}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAD91533.1}.
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DR EMBL; LXIE01000012; OAD91533.1; -; Genomic_DNA.
DR RefSeq; WP_068761707.1; NZ_LXIE01000012.1.
DR AlphaFoldDB; A0A1A9LE95; -.
DR STRING; 1385699.A7A78_03315; -.
DR OrthoDB; 1523230at2; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000077552; Unassembled WGS sequence.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
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 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.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|PIRNR:PIRNR000477};
KW Transferase {ECO:0000256|PIRNR:PIRNR000477}.
FT DOMAIN 24..270
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 272 AA; 30089 MW; 55179C9E8B12D835 CRC64;
MSSTKYIEEA ADYLKQRGFK NPEVGIILGT GLGKIVENIE IESEVSYNHI PNFPTATVEF
HKGKLIYGTL EGKKVVVMQG RFHVYEGYTL RDVTFPVRVM HLLGIKHLLV SNASGAINLN
FKKGEIMLID DHINLQGSSP LAFRGVEKMG ERFADMSAPY DTEMNKKLEL IASEKNITLH
KGVYASVVGP QLETRAEYRY LKIIGADAVG MSTVPEVIVA NHLKLPVSAV SVLTDECNPE
NLKPVDIADI IASAEQAEPD MITLFTELIK EL
//
