EzCatDB: T00037
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DB codeT00037
CATH domainDomain 13.90.1170.30 : Aldehyde Oxidoreductase; domain 3
Domain 23.40.1030.10 : Pyrimidine Nucleoside Phosphorylase; Chain A, domain 2Catalytic domain
Domain 31.20.970.10 : Transferase, Pyrimidine Nucleoside Phosphorylase; Chain A, domain 3
E.C.2.4.2.2
CSA1brw
MACiEM0091

CATH domainRelated DB codes (homologues)
1.20.970.10 : Transferase, Pyrimidine Nucleoside Phosphorylase; Chain A, domain 3T00038
3.40.1030.10 : Pyrimidine Nucleoside Phosphorylase; Chain A, domain 2T00038
3.90.1170.30 : Aldehyde Oxidoreductase; domain 3T00038

Enzyme Name
UniProtKBKEGG

P77836
Protein namePyrimidine-nucleoside phosphorylasepyrimidine-nucleoside phosphorylase
Py-NPase
SynonymsPYNP
EC 2.4.2.2
PfamPF02885 (Glycos_trans_3N)
PF00591 (Glycos_transf_3)
PF07831 (PYNP_C)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00240Pyrimidine metabolism

UniProtKB:Accession NumberP77836
Entry namePDP_BACST
ActivityA pyrimidine nucleoside + phosphate = a pyrimidine base + alpha-D-ribose 1-phosphate.
SubunitHomodimer.
Subcellular location
CofactorBinds 1 potassium ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00238C03169C00009C00396C00620
CompoundPotassiumPyrimidine nucleosideOrthophosphatePyrimidinealpha-D-Ribose 1-phosphate
Typeunivalent metal (Na+, K+)nucleosidephosphate group/phosphate ionaromatic ring (with nitrogen atoms)carbohydrate,phosphate group/phosphate ion
ChEBI29103

26078
16898
16300
PubChem813
439920
22486802
1004
9260
439236
             
1brwA01UnboundUnboundUnboundUnboundUnbound
1brwB01UnboundUnboundUnboundUnboundUnbound
1brwA02Analogue:_CAUnboundBound:PO4UnboundUnbound
1brwB02Analogue:_CAUnboundBound:PO4Analogue:URAUnbound
1brwA03UnboundUnboundUnboundUnboundUnbound
1brwB03UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot & literature [2]
pdbCatalytic residuesCofactor-binding residues
          
1brwA01 
 
1brwB01 
 
1brwA02HIS   82;ARG  168;SER  183;LYS  187
GLY   88;THR   90;LEU  243;ALA  246;GLU  255(Na+ binding)
1brwB02HIS 1082;ARG 1168;SER 1183;LYS 1187
GLY 1088;THR 1090;LEU 1243;ALA 1246;GLU 1255(Na+ binding)
1brwA03 
 
1brwB03 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[2]p.1474, Fig.72
[4]Fig.13

references
[1]
PubMed ID6216943
JournalCan J Biochem
Year1982
Volume60
Pages917-21
AuthorsShriver JW, Sykes BD
TitleIn situ enzymatic removal of orthophosphate by the nucleoside phosphorylase catalyzed phosphorolysis of nicotinamide riboside.
[2]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
Medline ID99036865
PubMed ID9817849
JournalStructure
Year1998
Volume6
Pages1467-79
AuthorsPugmire MJ, Ealick SE
TitleThe crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation.
Related PDB1brw
Related UniProtKBP77836
[3]
PubMed ID10089427
JournalActa Crystallogr D Biol Crystallogr
Year1999
Volume55
Pages287-90
AuthorsZhou M, Pugmire MJ, Vuong BQ, Ealick SE
TitleCloning, expression and crystallization of pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus.
[4]
PubMed ID11743878
JournalBiochem J
Year2002
Volume361
Pages1-25
AuthorsPugmire MJ, Ealick SE
TitleStructural analyses reveal two distinct families of nucleoside phosphorylases.
[5]
PubMed ID12093726
JournalEMBO J
Year2002
Volume21
Pages3245-54
AuthorsMayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M
TitleStructural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry.
[6]
PubMed ID12123839
JournalFEBS Lett
Year2002
Volume523
Pages239-46
AuthorsKim C, Xuong NH, Edwards S, Madhusudan, Yee MC, Spraggon G, Mills SE
TitleThe crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum.


createdupdated
2004-03-232009-02-26


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