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Database: UniProt
Entry: D6E6K2_9ACTN
LinkDB: D6E6K2_9ACTN
Original site: D6E6K2_9ACTN 
ID   D6E6K2_9ACTN            Unreviewed;       277 AA.
AC   D6E6K2;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=GPA_02400 {ECO:0000313|EMBL:CBL03349.1};
OS   Gordonibacter pamelaeae 7-10-1-b.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Gordonibacter.
OX   NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL03349.1, ECO:0000313|Proteomes:UP000008805};
RN   [1] {ECO:0000313|EMBL:CBL03349.1, ECO:0000313|Proteomes:UP000008805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.;
RT   "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL03349.1, ECO:0000313|Proteomes:UP000008805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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}.
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DR   EMBL; FP929047; CBL03349.1; -; Genomic_DNA.
DR   RefSeq; WP_015538699.1; NC_021021.1.
DR   AlphaFoldDB; D6E6K2; -.
DR   KEGG; gpa:GPA_02400; -.
DR   PATRIC; fig|657308.3.peg.2280; -.
DR   HOGENOM; CLU_054456_1_0_11; -.
DR   BioCyc; GPAM657308:GPA_RS01085-MONOMER; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000008805; Chromosome.
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; IPR011268; Purine_phosphorylase.
DR   NCBIfam; TIGR01697; PNPH-PUNA-XAPA; 1.
DR   PANTHER; PTHR11904:SF9; INOSINE PHOSPHORYLASE-RELATED; 1.
DR   PANTHER; PTHR11904; METHYLTHIOADENOSINE/PURINE NUCLEOSIDE PHOSPHORYLASE; 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   ECO:0000313|EMBL:CBL03349.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008805};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000477, ECO:0000313|EMBL:CBL03349.1}.
FT   DOMAIN          29..275
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   BINDING         35
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         66
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         86..88
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         118
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         198
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         217
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         240
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
SQ   SEQUENCE   277 AA;  29939 MW;  02E8BD26DE37CBF7 CRC64;
     MSQRNVLKEN LAESARVLRE RIGDRRPEVG MILGSGLGPL AGQIEDAVCV PYGEVPHMRT
     STATSHVGRF VCGVLGGKCV LAMQGRLHGY EGNTAQEVAY PVWLMHELGV DTLFATNAAG
     AINESYRVGD FCIIEDHINF TGRNPVAGLE PDGIAFRFFS MLDAYDPALR RLARETADEL
     GIRVQEGVYL GLLGPSFETP AEIRAFRAWG ADTVAMSVCE EVIAARHTGM RVLGMSLVSN
     MACGIEGASP TDEEVLDVAH DRAADFARLA TAIVERM
//
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