ECMDB: 5'-nucleotidase yjjG (P0A8Y1)

Identification

Name:

5'-nucleotidase yjjG

Synonyms:

Nucleoside 5'-monophosphate phosphohydrolase

Gene Name:

yjjG

Enzyme Class:

3.1.3.5

Biological Properties

General Function:

Involved in catalytic activity

Specific Function:

Nucleotidase that shows high phosphatase activity toward three nucleoside 5'-monophosphates, UMP, dUMP, and dTMP, and very low activity against TDP, IMP, UDP, GMP, dGMP, AMP, dAMP, and 6- phosphogluconate. Is strictly specific to substrates with 5'- phosphates and shows no activity against nucleoside 2'- or 3'- monophosphates. Might be involved in the pyrimidine nucleotide substrate cycles

Cellular Location:

Cytoplasm (Potential)

SMPDB Pathways:

Pyrimidine metabolism PW000942

KEGG Pathways:

Metabolic pathways eco01100
Nicotinate and nicotinamide metabolism ec00760
Purine metabolism ec00230
Pyrimidine metabolism ec00240

KEGG Reactions:

1.0

↔

1.0

1.0Adenosine monophosphate + 1.0Water ↔ 1.0Adenosine + 1.0Phosphate
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1.0

↔

1.0

1.0Cytidine monophosphate + 1.0Water ↔ 1.0Cytidine + 1.0Phosphate
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1.0

↔

1.0

1.0Uridine 5'-monophosphate + 1.0Water ↔ 1.0Uridine + 1.0Phosphate
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1.0

↔

1.0

1.0Inosinic acid + 1.0Water ↔ 1.0Inosine + 1.0Phosphate
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1.0

↔

1.0

1.0Guanosine monophosphate + 1.0Water ↔ 1.0Guanosine + 1.0Phosphate
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1.0

↔

1.0

1.05-Thymidylic acid + 1.0Water ↔ 1.0Thymidine + 1.0Phosphate
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1.0

↔

1.0

1.0dCMP + 1.0Water ↔ 1.0Deoxycytidine + 1.0Phosphate
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1.0

↔

1.0

1.02'-Deoxyguanosine 5'-monophosphate + 1.0Water ↔ 1.0Deoxyguanosine + 1.0Phosphate
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1.0

↔

1.0

1.0Deoxyadenosine monophosphate + 1.0Water ↔ 1.0Deoxyadenosine + 1.0Phosphate
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1.0

↔

1.0

1.0Nicotinamide ribotide + 1.0Water ↔ 1.0Nicotinamide riboside + 1.0Phosphate
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1.0

↔

1.0

1.0Xanthylic acid + 1.0Water ↔ 1.0Xanthosine + 1.0Phosphate
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1.05'-Ribonucleotide

1.0

↔

1.0

1.05'-Ribonucleotide + 1.0Water ↔ 1.0Ribonucleoside + 1.0Phosphate
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EcoCyc Reactions:

1.0

↔

1.0

1.0dCMP + 1.0Water ↔ 1.0Deoxycytidine + 1.0Phosphate
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1.0a ribonucleoside monophosphate

1.0

→

1.0a ribonucleoside

1.0

1.0a ribonucleoside monophosphate + 1.0Water → 1.0a ribonucleoside + 1.0Phosphate
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB01044	2'-Deoxyguanosine 5'-monophosphate	MetaboCard
ECMDB01227	5-Thymidylic acid	MetaboCard
ECMDB00050	Adenosine	MetaboCard
ECMDB00045	Adenosine monophosphate	MetaboCard
ECMDB00089	Cytidine	MetaboCard
ECMDB00095	Cytidine monophosphate	MetaboCard
ECMDB01202	dCMP	MetaboCard
ECMDB00101	Deoxyadenosine	MetaboCard
ECMDB00905	Deoxyadenosine monophosphate	MetaboCard
ECMDB00014	Deoxycytidine	MetaboCard
ECMDB00085	Deoxyguanosine	MetaboCard
ECMDB00012	Deoxyuridine	MetaboCard
ECMDB01409	dUMP	MetaboCard
ECMDB00133	Guanosine	MetaboCard
ECMDB01397	Guanosine monophosphate	MetaboCard
ECMDB21380	Inorganic phosphate	MetaboCard
ECMDB00195	Inosine	MetaboCard
ECMDB04085	Inosinic acid	MetaboCard
ECMDB00855	Nicotinamide riboside	MetaboCard
ECMDB00229	Nicotinamide ribotide	MetaboCard
ECMDB23222	NMN	MetaboCard
ECMDB01429	Phosphate	MetaboCard
ECMDB00273	Thymidine	MetaboCard
ECMDB00296	Uridine	MetaboCard
ECMDB00288	Uridine 5'-monophosphate	MetaboCard
ECMDB00494	Water	MetaboCard
ECMDB00299	Xanthosine	MetaboCard
ECMDB01554	Xanthylic acid	MetaboCard

GO Classification:

Function
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
phosphatase activity
phosphoglycolate phosphatase activity
phosphoric ester hydrolase activity
Process
metabolic process

Gene Properties

Blattner:

b4374

Gene Orientation

Clockwise

Centisome Percentage:

99.29

Left Sequence End

4606669

Right Sequence End

4607346

Gene Sequence:

>678 bp
ATGAGTGCGTCGTTGGCGATCCTGACCATCGGCATTGTACCTATGCAGGAAGTTTTGCCG
CTCCTGACGGAATACATTGACGAAGATAATATTTCCCATCATAGCCTGCTGGGGAAGTTA
AGTCGTGAAGAAGTGATGGCGGAGTACGCGCCAGAAGCAGGCGAAGACACCATTCTCACA
TTATTAAATGACAACCAGCTGGCCCATGTTTCGCGTCGCAAAGTGGAGCGTGACCTGCAA
GGTGTGGTTGAAGTGCTCGATAATCAGGGTTATGACGTCATTTTATTAATGAGTACAGCA
AACATTAGTAGTATGACTGCGCGTAATACGATCTTTCTTGAGCCGTCGCGAATATTGCCT
CCACTGGTTTCCTCTATTGTTGAAGATCATCAGGTGGGGGTTATCGTTCCGGTTGAGGAG
ATGCTGCCCGTTCAGGCGCAAAAATGGCAAATTTTGCAGAAATCGCCGGTATTTTCATTG
GGTAACCCCATTCATGATTCAGAACAAAAAATCATTGATGCCGGGAAAGAATTACTGGCA
AAAGGGGCTGATGTCATCATGCTGGATTGTTTAGGATTTCACCAACGTCATCGCGATTTA
CTGCAAAAACAGCTCGATGTTCCTGTCTTGCTGTCTAACGTATTGATTGCACGGCTGGCT
GCGGAATTACTGGTGTAA

Protein Properties

Pfam Domain Function:

Hydrolase (PF00702 )

Protein Residues:

225

Protein Molecular Weight:

25300

Protein Theoretical pI:

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>5'-nucleotidase yjjG
MKWDWIFFDADETLFTFDSFTGLQRMFLDYSVTFTAEDFQDYQAVNKPLWVDYQNGAITS
LQLQHGRFESWAERLNVEPGKLNEAFINAMAEICTPLPGAVSLLNAIRGNAKIGIITNGF
SALQQVRLERTGLRDYFDLLVISEEVGVAKPNKKIFDYALEQAGNPDRSRVLMVGDTAES
DILGGINAGLATCWLNAHHREQPEGIAPTWTVSSLHELEQLLCKH

References

External Links:

Resource	Link
Uniprot ID:	P0A8Y1
Uniprot Name:	YJJG_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	85674531
Ecogene ID:	EG12115
Ecocyc:	EG12115
ColiBase:	b4374
Kegg Gene:	b4374
EchoBASE ID:	EB2038
CCDB:	YJJG_ECOLI
BacMap:	16132192

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
Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
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
Proudfoot, M., Kuznetsova, E., Brown, G., Rao, N. N., Kitagawa, M., Mori, H., Savchenko, A., Yakunin, A. F. (2004). "General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG." J Biol Chem 279:54687-54694. Pubmed: 15489502