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P46354

- PUNA_BACSU

UniProt

P46354 - PUNA_BACSU

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Protein

Purine nucleoside phosphorylase 1

Gene

punA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine and inosine.

Catalytic activityi

Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate.

Pathwayi

GO - Molecular functioni

  1. purine-nucleoside phosphorylase activity Source: UniProtKB-EC

GO - Biological processi

  1. nucleoside metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciBSUB:BSU23490-MONOMER.
RETL1328306-WGS:GSTH-199-MONOMER.
UniPathwayiUPA00606.

Names & Taxonomyi

Protein namesi
Recommended name:
Purine nucleoside phosphorylase 1 (EC:2.4.2.1)
Short name:
PNP 1
Alternative name(s):
Inosine phosphorylase
Inosine-guanosine phosphorylase
Purine nucleoside phosphorylase I
Short name:
PNP I
Short name:
PU-NPase I
Gene namesi
Name:punA
Synonyms:deoD, pnp, yqkO
Ordered Locus Names:BSU23490
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU23490. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Purine nucleoside phosphorylase 1PRO_0000184540Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP46354.

PTM databases

PhosSiteiP0802232.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU23490.

Structurei

3D structure databases

ProteinModelPortaliP46354.
SMRiP46354. Positions 1-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PNP/MTAP phosphorylase family.Curated

Phylogenomic databases

eggNOGiCOG0005.
HOGENOMiHOG000045183.
InParanoidiP46354.
KOiK03783.
OMAiDQPLSHD.
OrthoDBiEOG6423M2.
PhylomeDBiP46354.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
InterProiIPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011270. Pur_Nuc_Pase_Ino/Guo-sp.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PTHR11904:SF9. PTHR11904:SF9. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000477. PurNPase. 1 hit.
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01700. PNPH. 1 hit.
TIGR01697. PNPH-PUNA-XAPA. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46354-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKDRIERAAA FIKQNLPESP KIGLILGSGL GILADEIENP VKLKYEDIPE
60 70 80 90 100
FPVSTVEGHA GQLVLGTLEG VSVIAMQGRF HFYEGYSMEK VTFPVRVMKA
110 120 130 140 150
LGVEALIVTN AAGGVNTEFR AGDLMIITDH INFMGTNPLI GPNEADFGAR
160 170 180 190 200
FPDMSSAYDK DLSSLAEKIA KDLNIPIQKG VYTAVTGPSY ETPAEVRFLR
210 220 230 240 250
TMGSDAVGMS TVPEVIVANH AGMRVLGISC ISNAAAGILD QPLSHDEVME
260 270
VTEKVKAGFL KLVKAIVAQY E
Length:271
Mass (Da):29,127
Last modified:November 1, 1995 - v1
Checksum:i420B26E7309D9FC9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841A → D in M85047. (PubMed:1629150)Curated
Sequence conflicti227 – 2271G → A in M85047. (PubMed:1629150)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U32685 Genomic DNA. Translation: AAA74434.1.
D84432 Genomic DNA. Translation: BAA12651.1.
AL009126 Genomic DNA. Translation: CAB14281.1.
M85047 Genomic DNA. No translation available.
PIRiD69680.
RefSeqiNP_390230.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB14281; CAB14281; BSU23490.
GeneIDi938731.
KEGGibsu:BSU23490.
PATRICi18976517. VBIBacSub10457_2449.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U32685 Genomic DNA. Translation: AAA74434.1 .
D84432 Genomic DNA. Translation: BAA12651.1 .
AL009126 Genomic DNA. Translation: CAB14281.1 .
M85047 Genomic DNA. No translation available.
PIRi D69680.
RefSeqi NP_390230.1. NC_000964.3.

3D structure databases

ProteinModelPortali P46354.
SMRi P46354. Positions 1-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU23490.

PTM databases

PhosSitei P0802232.

Proteomic databases

PaxDbi P46354.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14281 ; CAB14281 ; BSU23490 .
GeneIDi 938731.
KEGGi bsu:BSU23490.
PATRICi 18976517. VBIBacSub10457_2449.

Organism-specific databases

GenoListi BSU23490. [Micado ]

Phylogenomic databases

eggNOGi COG0005.
HOGENOMi HOG000045183.
InParanoidi P46354.
KOi K03783.
OMAi DQPLSHD.
OrthoDBi EOG6423M2.
PhylomeDBi P46354.

Enzyme and pathway databases

UniPathwayi UPA00606 .
BioCyci BSUB:BSU23490-MONOMER.
RETL1328306-WGS:GSTH-199-MONOMER.

Family and domain databases

Gene3Di 3.40.50.1580. 1 hit.
InterProi IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011270. Pur_Nuc_Pase_Ino/Guo-sp.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view ]
PANTHERi PTHR11904. PTHR11904. 1 hit.
PTHR11904:SF9. PTHR11904:SF9. 1 hit.
Pfami PF01048. PNP_UDP_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000477. PurNPase. 1 hit.
SUPFAMi SSF53167. SSF53167. 1 hit.
TIGRFAMsi TIGR01700. PNPH. 1 hit.
TIGR01697. PNPH-PUNA-XAPA. 1 hit.
PROSITEi PS01240. PNP_MTAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleosides as a carbon source in Bacillus subtilis: characterization of the drm-pupG operon."
    Schuch R., Garibian A., Saxild H.H., Piggot P.J., Nygaard P.
    Microbiology 145:2957-2966(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / BR151.
  2. "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
    Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
    Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / JH642.
  3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  4. "Characterization of a Bacillus subtilis sporulation operon that includes genes for an RNA polymerase sigma factor and for a putative DD-carboxypeptidase."
    Wu J.-J., Schuch R., Piggot P.J.
    J. Bacteriol. 174:4885-4892(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-271.
    Strain: 168 / MB24.
  5. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
    Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
    Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: 168.

Entry informationi

Entry nameiPUNA_BACSU
AccessioniPrimary (citable) accession number: P46354
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3