ID C0ZC51_BREBN Unreviewed; 269 AA.
AC C0ZC51;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 Name=punA {ECO:0000313|EMBL:BAH43360.1};
GN Synonyms=pnp {ECO:0000313|EMBL:BAH43360.1}, pupG
GN {ECO:0000313|EMBL:BAH43360.1};
GN OrderedLocusNames=BBR47_23830 {ECO:0000313|EMBL:BAH43360.1};
OS Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH43360.1, ECO:0000313|Proteomes:UP000001877};
RN [1] {ECO:0000313|EMBL:BAH43360.1, ECO:0000313|Proteomes:UP000001877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47 / JCM 6285 / NBRC 100599
RC {ECO:0000313|Proteomes:UP000001877};
RA Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA Udaka S., Tanikawa S., Fujita N.;
RT "Brevibacillus brevis strain 47, complete genome.";
RL Submitted (MAR-2005) 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 -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006751, ECO:0000256|PIRNR:PIRNR000477}.
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DR EMBL; AP008955; BAH43360.1; -; Genomic_DNA.
DR RefSeq; WP_012686075.1; NC_012491.1.
DR AlphaFoldDB; C0ZC51; -.
DR STRING; 358681.BBR47_23830; -.
DR KEGG; bbe:BBR47_23830; -.
DR eggNOG; COG0005; Bacteria.
DR HOGENOM; CLU_054456_1_0_9; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000001877; 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; 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 Glycosyltransferase {ECO:0000256|PIRNR:PIRNR000477,
KW ECO:0000313|EMBL:BAH43360.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001877};
KW Transferase {ECO:0000256|PIRNR:PIRNR000477, ECO:0000313|EMBL:BAH43360.1}.
FT DOMAIN 20..266
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 27
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 58
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 78..80
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 110
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 190
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 209
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 232
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
SQ SEQUENCE 269 AA; 28966 MW; DC4E3DE0E2D9A4E4 CRC64;
MANFHDAVAY IEPKLTEKPT IGLVLGSGLG VLADEIENPV IIPYHEIPGF TVSTVVGHKG
QLVIGKLQGK QVVAMQGRFH FYEGHGLDAV VFPIRVMKLL GVETIMVTNA AGGINEGYNP
GDLMLISDHI NMTFRNPLIG ANDEQLGARF PDMSEAYSKQ LRKLAHEVAS EQGIQLREGV
YAGLLGPSYE TPAEIRMLRL LGGDAVGMST VPEVIVARHM GVKVLGISCI SNMAAGILEQ
PLSHDEVMET TEKVKSQFLA LVNGIVAKL
//
