(data stored in SCRATCH zone)

SWISSPROT: PUNA_BACSU

ID   PUNA_BACSU              Reviewed;         271 AA.
AC   P46354;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   11-DEC-2019, entry version 136.
DE   RecName: Full=Purine nucleoside phosphorylase 1;
DE            Short=PNP 1;
DE            EC=2.4.2.1;
DE   AltName: Full=Inosine phosphorylase;
DE   AltName: Full=Inosine-guanosine phosphorylase;
DE   AltName: Full=Purine nucleoside phosphorylase I;
DE            Short=PNP I;
DE            Short=Pu-NPase I;
GN   Name=punA; Synonyms=deoD, pnp, yqkO; OrderedLocusNames=BSU23490;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / BR151;
RX   PubMed=10537218; DOI=10.1099/00221287-145-10-2957;
RA   Schuch R., Garibian A., Saxild H.H., Piggot P.J., Nygaard P.;
RT   "Nucleosides as a carbon source in Bacillus subtilis: characterization of
RT   the drm-pupG operon.";
RL   Microbiology 145:2957-2966(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-271.
RC   STRAIN=168 / MB24;
RX   PubMed=1629150; DOI=10.1128/jb.174.15.4885-4892.1992;
RA   Wu J.-J., Schuch R., Piggot P.J.;
RT   "Characterization of a Bacillus subtilis sporulation operon that includes
RT   genes for an RNA polymerase sigma factor and for a putative DD-
RT   carboxypeptidase.";
RL   J. Bacteriol. 174:4885-4892(1992).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
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. Cleaves
CC       guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
CC       {ECO:0000250|UniProtKB:P77834}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-
CC         alpha-D-ribose 1-phosphate + a purine nucleobase;
CC         Xref=Rhea:RHEA:36431, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57259, ChEBI:CHEBI:142361; EC=2.4.2.1;
CC         Evidence={ECO:0000250|UniProtKB:P77834};
CC   -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P77834}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC       {ECO:0000305}.
DR   EMBL; U32685; AAA74434.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12651.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14281.1; -; Genomic_DNA.
DR   EMBL; M85047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; D69680; D69680.
DR   RefSeq; NP_390230.1; NC_000964.3.
DR   RefSeq; WP_003230447.1; NZ_JNCM01000036.1.
DR   SMR; P46354; -.
DR   STRING; 224308.BSU23490; -.
DR   iPTMnet; P46354; -.
DR   jPOST; P46354; -.
DR   PaxDb; P46354; -.
DR   PRIDE; P46354; -.
DR   EnsemblBacteria; CAB14281; CAB14281; BSU23490.
DR   GeneID; 938731; -.
DR   KEGG; bsu:BSU23490; -.
DR   PATRIC; fig|224308.179.peg.2559; -.
DR   eggNOG; ENOG4105CB1; Bacteria.
DR   eggNOG; COG0005; LUCA.
DR   HOGENOM; HOG000045183; -.
DR   InParanoid; P46354; -.
DR   KO; K03783; -.
DR   OMA; EGVYAQF; -.
DR   PhylomeDB; P46354; -.
DR   BioCyc; BSUB:BSU23490-MONOMER; -.
DR   BRENDA; 2.4.2.1; 658.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IBA:GO_Central.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1580; -; 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   PANTHER; PTHR11904; PTHR11904; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   PIRSF; PIRSF000477; PurNPase; 1.
DR   SUPFAM; SSF53167; SSF53167; 1.
DR   TIGRFAMs; TIGR01700; PNPH; 1.
DR   TIGRFAMs; TIGR01697; PNPH-PUNA-XAPA; 1.
DR   PROSITE; PS01240; PNP_MTAP_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P46354.
DR   SWISS-2DPAGE; P46354.
KW   Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..271
FT                   /note="Purine nucleoside phosphorylase 1"
FT                   /id="PRO_0000184540"
FT   REGION          79..81
FT                   /note="Phosphate binding"
FT                   /evidence="ECO:0000250|UniProtKB:P45563"
FT   BINDING         28
FT                   /note="Phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP01"
FT   BINDING         59
FT                   /note="Phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P45563"
FT   BINDING         111
FT                   /note="Phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P45563"
FT   BINDING         191
FT                   /note="Purine nucleoside"
FT                   /evidence="ECO:0000250|UniProtKB:P45563"
FT   BINDING         210
FT                   /note="Phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P45563"
FT   BINDING         233
FT                   /note="Purine nucleoside"
FT                   /evidence="ECO:0000250|UniProtKB:P45563"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
FT   CONFLICT        184
FT                   /note="A -> D (in Ref. 4; M85047)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        227
FT                   /note="G -> A (in Ref. 4; M85047)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   271 AA;  29127 MW;  420B26E7309D9FC9 CRC64;
     MKDRIERAAA FIKQNLPESP KIGLILGSGL GILADEIENP VKLKYEDIPE FPVSTVEGHA
     GQLVLGTLEG VSVIAMQGRF HFYEGYSMEK VTFPVRVMKA LGVEALIVTN AAGGVNTEFR
     AGDLMIITDH INFMGTNPLI GPNEADFGAR FPDMSSAYDK DLSSLAEKIA KDLNIPIQKG
     VYTAVTGPSY ETPAEVRFLR TMGSDAVGMS TVPEVIVANH AGMRVLGISC ISNAAAGILD
     QPLSHDEVME VTEKVKAGFL KLVKAIVAQY E
//

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