Uridylate kinase (P0A7E9)

Identification
Name:Uridylate kinase
Synonyms:
  • UK
  • Uridine monophosphate kinase
  • UMP kinase
  • UMPK
Gene Name:pyrH
Enzyme Class:
Biological Properties
General Function:Involved in cellular amino acid biosynthetic process
Specific Function:Catalyzes the reversible phosphorylation of UMP to UDP, with ATP as the most efficient phosphate donor
Cellular Location:Cytoplasm.
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Uridine 5'-monophosphate ↔ 1.0ADP + 1.0Uridine 5'-diphosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Adenosine diphosphate+1.0Uridine 5'-diphosphate+1.0Thumb+1.0Thumb
1.0Uridine 5'-monophosphate + 1.0Adenosine triphosphate → 1.0Adenosine diphosphate + 1.0Uridine 5'-diphosphate + 1.0ADP + 1.0Uridine 5'-diphosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Uridine 5'-monophosphate ↔ 1.0ADP + 1.0Uridine 5'-diphosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Uridine 5'-monophosphate → 1.0ADP + 1.0Uridine 5'-diphosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB00295Uridine 5'-diphosphateMetaboCard
ECMDB00288Uridine 5'-monophosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
catalytic activity
phosphotransferase activity, phosphate group as acceptor
transferase activity
transferase activity, transferring phosphorus-containing groups
UMP kinase activity
uridylate kinase activity
Process
cellular amino acid and derivative metabolic process
cellular amino acid biosynthetic process
cellular amino acid metabolic process
cellular metabolic process
cellular nitrogen compound metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
pyrimidine nucleotide biosynthetic process
pyrimidine nucleotide metabolic process
Gene Properties
Blattner:b0171
Gene OrientationClockwise
Centisome Percentage:4.14
Left Sequence End191855
Right Sequence End192580
Gene Sequence:
>726 bp
ATGGCAACTGTTTCCATGCGCGACATGCTCAAGGCTGGTGTTCACTTCGGTCACCAGACC
CGTTACTGGAACCCGAAAATGAAGCCGTTCATCTTCGGTGCGCGTAACAAAGTTCACATC
ATCAACCTTGAGAAAACTGTACCGATGTTCAACGAAGCTCTGGCTGAACTGAACAAGATT
GCTTCTCGCAAAGGTAAAATCCTTTTCGTTGGTACTAAACGCGCTGCAAGCGAAGCGGTG
AAAGACGCTGCTCTGAGCTGCGACCAGTTCTTCGTGAACCATCGCTGGCTGGGCGGTATG
CTGACTAACTGGAAAACCGTTCGTCAGTCCATCAAACGTCTGAAAGACCTGGAAACTCAG
TCTCAGGACGGTACTTTCGACAAGCTGACCAAGAAAGAAGCGCTGATGCGCACTCGTGAG
CTGGAGAAACTGGAAAACAGCCTGGGCGGTATCAAAGACATGGGCGGTCTGCCGGACGCT
CTGTTTGTAATCGATGCTGACCACGAACACATTGCTATCAAAGAAGCAAACAACCTGGGT
ATTCCGGTATTTGCTATCGTTGATACCAACTCTGATCCGGACGGTGTTGACTTCGTTATC
CCGGGTAACGACGACGCAATCCGTGCTGTGACCCTGTACCTGGGCGCTGTTGCTGCAACC
GTACGTGAAGGCCGTTCTCAGGATCTGGCTTCCCAGGCGGAAGAAAGCTTCGTAGAAGCT
GAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:241
Protein Molecular Weight:25970
Protein Theoretical pI:8
PDB File:2BNE
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Uridylate kinase
MATNAKPVYKRILLKLSGEALQGTEGFGIDASILDRMAQEIKELVELGIQVGVVIGGGNL
FRGAGLAKAGMNRVVGDHMGMLATVMNGLAMRDALHRAYVNARLMSAIPLNGVCDSYSWA
EAISLLRNNRVVILSAGTGNPFFTTDSAACLRGIEIEADVVLKATKVDGVFTADPAKDPT
ATMYEQLTYSEVLEKELKVMDLAAFTLARDHKLPIRVFNMNKPGALRRVVMGEKEGTLIT
E
References
External Links:
ResourceLink
Uniprot ID:P0A7E9
Uniprot Name:PYRH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21239023
PDB ID:2BNE
Ecogene ID:EG11539
Ecocyc:EG11539
ColiBase:b0171
Kegg Gene:b0171
EchoBASE ID:EB1501
CCDB:PYRH_ECOLI
BacMap:16128164
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Briozzo, P., Evrin, C., Meyer, P., Assairi, L., Joly, N., Barzu, O., Gilles, A. M. (2005). "Structure of Escherichia coli UMP kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation." J Biol Chem 280:25533-25540. Pubmed: 15857829
  • Bucurenci, N., Serina, L., Zaharia, C., Landais, S., Danchin, A., Barzu, O. (1998). "Mutational analysis of UMP kinase from Escherichia coli." J Bacteriol 180:473-477. Pubmed: 9457846
  • Evrin, C., Straut, M., Slavova-Azmanova, N., Bucurenci, N., Onu, A., Assairi, L., Ionescu, M., Palibroda, N., Barzu, O., Gilles, A. M. (2007). "Regulatory mechanisms differ in UMP kinases from gram-negative and gram-positive bacteria." J Biol Chem 282:7242-7253. Pubmed: 17210578
  • Fujita, N., Mori, H., Yura, T., Ishihama, A. (1994). "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Nucleic Acids Res 22:1637-1639. Pubmed: 8202364
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Landais, S., Gounon, P., Laurent-Winter, C., Mazie, J. C., Danchin, A., Barzu, O., Sakamoto, H. (1999). "Immunochemical analysis of UMP kinase from Escherichia coli." J Bacteriol 181:833-840. Pubmed: 9922246
  • Serina, L., Blondin, C., Krin, E., Sismeiro, O., Danchin, A., Sakamoto, H., Gilles, A. M., Barzu, O. (1995). "Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP." Biochemistry 34:5066-5074. Pubmed: 7711027
  • Yamanaka, K., Ogura, T., Koonin, E. V., Niki, H., Hiraga, S. (1994). "Multicopy suppressors, mssA and mssB, of an smbA mutation of Escherichia coli." Mol Gen Genet 243:9-16. Pubmed: 8190075
  • Yamanaka, K., Ogura, T., Niki, H., Hiraga, S. (1992). "Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coli." J Bacteriol 174:7517-7526. Pubmed: 1447125