Protein ushA (P07024)

Identification
Name:Protein ushA
Synonyms:
  • UDP-sugar hydrolase
  • UDP-sugar diphosphatase
  • UDP-sugar pyrophosphatase
  • 5'-nucleotidase
  • 5'-NT
Gene Name:ushA
Enzyme Class:
Biological Properties
General Function:Involved in hydrolase activity
Specific Function:Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell
Cellular Location:Periplasm.
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+2.0Thumb+1.0Thumb
1.0Water + 1.0UDP-Glucose → 1.0Glucose 1-phosphate + 2.0Hydrogen ion + 1.0Uridine 5'-monophosphate
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine monophosphate + 1.0Water ↔ 1.0Adenosine + 1.0Phosphate
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Cytidine monophosphate + 1.0Water ↔ 1.0Cytidine + 1.0Phosphate
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Uridine 5'-monophosphate + 1.0Water ↔ 1.0Uridine + 1.0Phosphate
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Inosinic acid + 1.0Water ↔ 1.0Inosine + 1.0Phosphate
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Guanosine monophosphate + 1.0Water ↔ 1.0Guanosine + 1.0Phosphate
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.05-Thymidylic acid + 1.0Water ↔ 1.0Thymidine + 1.0Phosphate
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0dCMP + 1.0Water ↔ 1.0Deoxycytidine + 1.0Phosphate
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02'-Deoxyguanosine 5'-monophosphate + 1.0Water ↔ 1.0Deoxyguanosine + 1.0Phosphate
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Deoxyadenosine monophosphate + 1.0Water ↔ 1.0Deoxyadenosine + 1.0Phosphate
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Nicotinamide ribotide + 1.0Water ↔ 1.0Nicotinamide riboside + 1.0Phosphate
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Xanthylic acid + 1.0Water ↔ 1.0Xanthosine + 1.0Phosphate
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1.05'-Ribonucleotide+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.05'-Ribonucleotide + 1.0Water ↔ 1.0Ribonucleoside + 1.0Phosphate
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1.0UDP-sugar+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0UDP-sugar + 1.0Water ↔ 1.0Uridine 5'-monophosphate + 1.0alpha-D-Aldose 1-phosphate
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EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0dCMP + 1.0Water ↔ 1.0Deoxycytidine + 1.0Phosphate
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1.0a ribonucleoside monophosphate+1.0Thumb → 1.0a ribonucleoside+1.0Thumb
1.0a ribonucleoside monophosphate + 1.0Water → 1.0a ribonucleoside + 1.0Phosphate
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1.0a UDP-sugar+1.0Thumb → 1.0Thumb+1.0an α-D-aldose-1-phosphate+1.0Thumb
1.0a UDP-sugar + 1.0Water → 1.0Uridine 5'-monophosphate + 1.0an α-D-aldose-1-phosphate + 1.0Hydrogen ion
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Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine monophosphate + 1.0Water → 1.0Adenosine + 1.0Phosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Cytidine monophosphate + 1.0Water → 1.0Cytidine + 1.0Phosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0Uridine 5'-monophosphate → 1.0Phosphate + 1.0Uridine
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0Xanthylic acid → 1.0Phosphate + 1.0Xanthosine
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0Inosinic acid → 1.0Inosine + 1.0Phosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Deoxyadenosine monophosphate + 1.0Water → 1.0Deoxyadenosine + 1.0Phosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.02'-Deoxyguanosine 5'-monophosphate + 1.0Water → 1.0Deoxyguanosine + 1.0Phosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0dCMP + 1.0Water → 1.0Deoxycytidine + 1.0Phosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.05-Thymidylic acid + 1.0Water → 1.0Phosphate + 1.0Thymidine
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Guanosine monophosphate + 1.0Water → 1.0Guanosine + 1.0Phosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0dUMP + 1.0Water → 1.0Deoxyuridine + 1.0Phosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0DIMP + 1.0Water → 1.0Deoxyinosine + 1.0Phosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+2.0Thumb+1.0Thumb
1.0Water + 1.0Uridine diphosphate-N-acetylglucosamine → 1.0N-Acetyl-glucosamine 1-phosphate + 2.0Hydrogen ion + 1.0Uridine 5'-monophosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+2.0Thumb+1.0Thumb
1.0Water + 1.0Uridine diphosphategalactose → 1.0Galactose 1-phosphate + 2.0Hydrogen ion + 1.0Uridine 5'-monophosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+2.0Thumb+1.0Thumb
1.0Water + 1.0Uridine diphosphate glucuronic acid → 1.0D-Glucuronate 1-phosphate + 2.0Hydrogen ion + 1.0Uridine 5'-monophosphate
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1.0A 5'-ribonucleotide+1.0Thumb → 1.0a ribonucleoside+1.0Thumb
1.0A 5'-ribonucleotide + 1.0Water → 1.0a ribonucleoside + 1.0Inorganic phosphate
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1.0UDP-sugar+1.0Thumb → 1.0Thumb+1.0alpha-D-aldose 1-phosphate
1.0UDP-sugar + 1.0Water → 1.0Uridine 5'-monophosphate + 1.0alpha-D-aldose 1-phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB010442'-Deoxyguanosine 5'-monophosphateMetaboCard
ECMDB012275-Thymidylic acidMetaboCard
ECMDB00050AdenosineMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00089CytidineMetaboCard
ECMDB00095Cytidine monophosphateMetaboCard
ECMDB21198D-Glucuronate 1-phosphateMetaboCard
ECMDB01202dCMPMetaboCard
ECMDB00101DeoxyadenosineMetaboCard
ECMDB00905Deoxyadenosine monophosphateMetaboCard
ECMDB00014DeoxycytidineMetaboCard
ECMDB00085DeoxyguanosineMetaboCard
ECMDB00071DeoxyinosineMetaboCard
ECMDB00012DeoxyuridineMetaboCard
ECMDB06555DIMPMetaboCard
ECMDB01409dUMPMetaboCard
ECMDB04011Galactose 1-phosphateMetaboCard
ECMDB01586Glucose 1-phosphateMetaboCard
ECMDB00133GuanosineMetaboCard
ECMDB01397Guanosine monophosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00195InosineMetaboCard
ECMDB04085Inosinic acidMetaboCard
ECMDB21247N-Acetyl-D-galactosamine 1-phosphateMetaboCard
ECMDB01367N-Acetyl-glucosamine 1-phosphateMetaboCard
ECMDB00855Nicotinamide ribosideMetaboCard
ECMDB00229Nicotinamide ribotideMetaboCard
ECMDB23222NMNMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00273ThymidineMetaboCard
ECMDB04171UDP-GlucoseMetaboCard
ECMDB01384UDP-Glucuronic acidMetaboCard
ECMDB00296UridineMetaboCard
ECMDB00288Uridine 5'-monophosphateMetaboCard
ECMDB04166Uridine diphosphate glucuronic acidMetaboCard
ECMDB00290Uridine diphosphate-N-acetylglucosamineMetaboCard
ECMDB00302Uridine diphosphategalactoseMetaboCard
ECMDB00494WaterMetaboCard
ECMDB00299XanthosineMetaboCard
ECMDB01554Xanthylic acidMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
hydrolase activity
hydrolase activity, acting on ester bonds
ion binding
metal ion binding
nucleotide binding
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 catabolic process
nucleotide metabolic process
Gene Properties
Blattner:b0480
Gene OrientationClockwise
Centisome Percentage:10.87
Left Sequence End504138
Right Sequence End505790
Gene Sequence:
>1653 bp
ATGAAATTATTGCAGCGGGGCGTGGCGTTAGCGCTGTTAACCACATTTACACTGGCGAGT
GAAACTGCTCTGGCGTATGAGCAGGATAAAACCTACAAAATTACAGTTCTGCATACCAAT
GATCATCATGGGCATTTTTGGCGCAATGAATATGGCGAATATGGTCTGGCGGCGCAAAAA
ACGCTGGTGGATGGTATCCGCAAAGAGGTTGCGGCTGAAGGCGGTAGCGTGCTGCTACTT
TCCGGTGGCGACATTAACACTGGCGTGCCCGAGTCTGACTTACAGGATGCCGAACCTGAT
TTTCGCGGTATGAATCTGGTGGGCTATGACGCGATGGCGATCGGTAATCATGAATTTGAT
AATCCGCTCACCGTATTACGCCAGCAGGAAAAGTGGGCCAAGTTCCCGTTGCTTTCCGCG
AATATCTACCAGAAAAGTACTGGCGAGCGCCTGTTTAAACCGTGGGCGCTGTTTAAGCGT
CAGGATCTGAAAATTGCCGTTATTGGGCTGACAACCGATGACACAGCAAAAATTGGTAAC
CCGGAATACTTCACTGATATCGAATTTCGTAAGCCCGCCGATGAAGCGAAGCTGGTGATT
CAGGAGCTGCAACAGACAGAAAAGCCAGACATTATTATCGCGGCGACCCATATGGGGCAT
TACGATAATGGTGAGCACGGCTCTAACGCACCGGGCGATGTGGAGATGGCACGCGCGCTG
CCTGCCGGATCGCTGGCGATGATCGTCGGTGGTCACTCGCAAGATCCGGTCTGCATGGCG
GCAGAAAACAAAAAACAGGTCGATTACGTGCCGGGTACGCCATGCAAACCAGATCAACAA
AACGGCATCTGGATTGTGCAGGCGCATGAGTGGGGCAAATACGTGGGACGGGCTGATTTT
GAGTTTCGTAATGGCGAAATGAAAATGGTTAACTACCAGCTGATTCCGGTGAACCTGAAG
AAGAAAGTGACCTGGGAAGACGGGAAAAGCGAGCGCGTGCTTTACACTCCTGAAATCGCT
GAAAACCAGCAAATGATCTCGCTGTTATCACCGTTCCAGAACAAAGGCAAAGCGCAGCTG
GAAGTGAAAATAGGCGAAACCAATGGTCGTCTGGAAGGCGATCGTGACAAAGTGCGTTTT
GTACAGACCAATATGGGGCGGTTGATTCTGGCAGCCCAAATGGATCGCACTGGTGCCGAC
TTTGCGGTGATGAGCGGAGGCGGAATTCGTGATTCTATCGAAGCAGGCGATATCAGCTAT
AAAAACGTGCTGAAAGTGCAGCCATTCGGCAATGTGGTGGTGTATGCCGACATGACCGGT
AAAGAGGTGATTGATTACCTGACCGCCGTCGCGCAGATGAAGCCAGATTCAGGTGCCTAC
CCGCAATTTGCCAACGTTAGCTTTGTGGCGAAAGACGGCAAACTGAACGACCTTAAAATC
AAAGGCGAACCGGTCGATCCGGCGAAAACTTACCGTATGGCGACATTAAACTTCAATGCC
ACCGGCGGTGATGGATATCCGCGCCTTGATAACAAACCGGGCTATGTGAATACCGGCTTT
ATTGATGCCGAAGTGCTGAAAGCGTATATCCAGAAAAGCTCGCCGCTGGATGTGAGTGTT
TATGAACCGAAAGGTGAGGTGAGCTGGCAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:550
Protein Molecular Weight:60824
Protein Theoretical pI:5
PDB File:2USH
Signaling Regions:
  • 1-25
Transmembrane Regions:
  • None
Protein Sequence:
>Protein ushA
MKLLQRGVALALLTTFTLASETALAYEQDKTYKITVLHTNDHHGHFWRNEYGEYGLAAQK
TLVDGIRKEVAAEGGSVLLLSGGDINTGVPESDLQDAEPDFRGMNLVGYDAMAIGNHEFD
NPLTVLRQQEKWAKFPLLSANIYQKSTGERLFKPWALFKRQDLKIAVIGLTTDDTAKIGN
PEYFTDIEFRKPADEAKLVIQELQQTEKPDIIIAATHMGHYDNGEHGSNAPGDVEMARAL
PAGSLAMIVGGHSQDPVCMAAENKKQVDYVPGTPCKPDQQNGIWIVQAHEWGKYVGRADF
EFRNGEMKMVNYQLIPVNLKKKVTWEDGKSERVLYTPEIAENQQMISLLSPFQNKGKAQL
EVKIGETNGRLEGDRDKVRFVQTNMGRLILAAQMDRTGADFAVMSGGGIRDSIEAGDISY
KNVLKVQPFGNVVVYADMTGKEVIDYLTAVAQMKPDSGAYPQFANVSFVAKDGKLNDLKI
KGEPVDPAKTYRMATLNFNATGGDGYPRLDNKPGYVNTGFIDAEVLKAYIQKSSPLDVSV
YEPKGEVSWQ
References
External Links:
ResourceLink
Uniprot ID:P07024
Uniprot Name:USHA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674619
PDB ID:2USH
Ecogene ID:EG11060
Ecocyc:EG11060
ColiBase:b0480
Kegg Gene:b0480
EchoBASE ID:EB1053
CCDB:USHA_ECOLI
BacMap:16128464
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
  • Burns, D. M., Beacham, I. R. (1986). "Nucleotide sequence and transcriptional analysis of the E. coli ushA gene, encoding periplasmic UDP-sugar hydrolase (5'-nucleotidase): regulation of the ushA gene, and the signal sequence of its encoded protein product." Nucleic Acids Res 14:4325-4342. Pubmed: 3012467
  • 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
  • Knofel, T., Strater, N. (1999). "X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site." Nat Struct Biol 6:448-453. Pubmed: 10331872
  • Knofel, T., Strater, N. (2001). "E. coli 5'-nucleotidase undergoes a hinge-bending domain rotation resembling a ball-and-socket motion." J Mol Biol 309:255-266. Pubmed: 11491294
  • Knofel, T., Strater, N. (2001). "Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures." J Mol Biol 309:239-254. Pubmed: 11491293
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646