DB code: T00037

CATH domain 3.90.1170.30 : Aldehyde Oxidoreductase; domain 3
3.40.1030.10 : Pyrimidine Nucleoside Phosphorylase; Chain A, domain 2 Catalytic domain
1.20.970.10 : Transferase, Pyrimidine Nucleoside Phosphorylase; Chain A, domain 3
E.C. 2.4.2.2
CSA 1brw
M-CSA 1brw
MACiE M0091

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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P77836 Pyrimidine-nucleoside phosphorylase
PYNP
EC 2.4.2.2
PF02885 (Glycos_trans_3N)
PF00591 (Glycos_transf_3)
PF07831 (PYNP_C)
[Graphical View]

KEGG enzyme name
pyrimidine-nucleoside phosphorylase
Py-NPase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P77836 PDP_BACST A pyrimidine nucleoside + phosphate = a pyrimidine base + alpha-D-ribose 1-phosphate. Homodimer. Binds 1 potassium ion per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00240 Pyrimidine metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00238 C03169 C00009 C00396 C00620
E.C.
Compound Potassium Pyrimidine nucleoside Orthophosphate Pyrimidine alpha-D-Ribose 1-phosphate
Type univalent metal (Na+, K+) nucleoside phosphate group/phosphate ion aromatic ring (with nitrogen atoms) carbohydrate,phosphate group/phosphate ion
ChEBI 29103
 29103
 		26078
 26078
 		16898
 16898
 		16300
 16300
PubChem 813
 813
 		439920
 439920
 		1004
 22486802
 1004
 22486802
 		9260
 9260
 		439236
 439236
1brwA01 Unbound Unbound Unbound Unbound Unbound
1brwB01 Unbound Unbound Unbound Unbound Unbound
1brwA02 Analogue:_CA Unbound Bound:PO4 Unbound Unbound
1brwB02 Analogue:_CA Unbound Bound:PO4 Analogue:URA Unbound
1brwA03 Unbound Unbound Unbound Unbound Unbound
1brwB03 Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot & literature [2]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1brwA01
1brwB01
1brwA02 HIS 82;ARG 168;SER 183;LYS 187 GLY 88;THR 90;LEU 243;ALA 246;GLU 255(Na+ binding)
1brwB02 HIS 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
References Sections No. of steps in catalysis
[2]
p.1474, Fig.7 2
[4]
Fig.13

References
[1]
Resource
Comments
Medline ID
PubMed ID 6216943
Journal Can J Biochem
Year 1982
Volume 60
Pages 917-21
Authors Shriver JW, Sykes BD
Title In situ enzymatic removal of orthophosphate by the nucleoside phosphorylase catalyzed phosphorolysis of nicotinamide riboside.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS)
Medline ID 99036865
PubMed ID 9817849
Journal Structure
Year 1998
Volume 6
Pages 1467-79
Authors Pugmire MJ, Ealick SE
Title The crystal structure of pyrimidine nucleoside phosphorylase in a closed conformation.
Related PDB 1brw
Related UniProtKB P77836
[3]
Resource
Comments
Medline ID
PubMed ID 10089427
Journal Acta Crystallogr D Biol Crystallogr
Year 1999
Volume 55
Pages 287-90
Authors Zhou M, Pugmire MJ, Vuong BQ, Ealick SE
Title Cloning, expression and crystallization of pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 11743878
Journal Biochem J
Year 2002
Volume 361
Pages 1-25
Authors Pugmire MJ, Ealick SE
Title Structural analyses reveal two distinct families of nucleoside phosphorylases.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 12093726
Journal EMBO J
Year 2002
Volume 21
Pages 3245-54
Authors Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M
Title Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 12123839
Journal FEBS Lett
Year 2002
Volume 523
Pages 239-46
Authors Kim C, Xuong NH, Edwards S, Madhusudan, Yee MC, Spraggon G, Mills SE
Title The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-03-23 2009-02-26